Found 8 matching records:
Displaying record number 315
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Vaccine Details
Notes
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8 notes.
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10/76b: Position 167 in V2 dictates the specificities of three type-specific neutralizing MAbs that bind to an otherwise relatively conserved epitope in involving V2: 2909, C108g, and 10/76b. Introduction of D167G mutation in YU2 Env resulted in weak neutralization by 10/76b. Removing the glycan at position N131 resulted in increase in sensitivity to 10/76b while removing of V1 glycosylation site 140 had minimal effect. Eliminating the glycan at position 160 in V2 in conjunction with V1 glycan and D167G mutations resulted in an increase in sensitivity to 10/76b, indicating that the glycan in this position acts as a potent masking element for the 10/76b epitope.
Honnen2007
(antibody binding site, variant cross-reactivity)
-
10/76b: This study is about the MAb C108g, and 10/76b was a control. C108g is type-specific and neutralizes BaL and HXB2. It is the most potent anti-V2 MAb, and is glycan dependent and contrary to earlier reports requires disulfide bonds. Neutralization by C108g is not mediated by CD4 or CCR5 receptor blockage on the cell surface. JR-FL is a neutralization resistant strain; modification of JRFL at positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The MAb 10/76b, that binds to a linear V2 epitope that is unaffected by deglycosylation or reduction eliminating disulfide bonds, could only weakly neutralize this modified JR-FL. Similarly SF162 substitutions in the neutralization sensitive virus SF162 GVK->NMK (167-169) plus the glycoslyation site at 160, created a G108g neutralization sensitive virus. In contrast, 10/76b binds to the NMK substituted variant, but addition of the glycosylation site inhibited binding.
Pinter2005
(antibody binding site)
-
10/76b: UK Medical Research Council AIDS reagent: ARP3077.
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10/76b: Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
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10/76b: HX10 strain specificity -- binds native, deglycosylated, or denatured gp120.
Wu1995
(antibody binding site, variant cross-reactivity)
-
10/76b: Included in cross-competition and neutralization studies.
Shotton1995
(antibody binding site)
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10/76b: Cross-competes with MAbs 10/76b and 11/4b -- HXB2 neutralization escape mutant has the substitution I/T at residue 165.
Shotton1995
(antibody binding site)
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10/76b: This MAb was obtained from a hybridoma cell line. An R to L substitution abrogated binding. Human sera recognize the 10/76 epitope.
McKeating1993a
(antibody generation)
References
Showing 7 of
7 references.
Isolation Paper
McKeating1993a
J. A. McKeating, C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, S. C. Kayman, Z. Wu, A. Pinter, C. Dean, J. Sodroski, and R. A. Weiss. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol., 67:4932-4944, 1993. Substitutions in the V2 loop can result in complete dissociation of gp120 and gp41, suggesting alterations in V2 can affect subunit assembly. Other substitutions allowed gp120-gp41 association and expression, but inhibited viral entry or syncytia. Binding of some neutralizing MAbs was altered by V2 substitutions. For MAb CRA-4, changes at residues 191/192/193 (YSL/GSS), and for 11/68b, changes at residues 183/184 (PI/SG), within V2, and for both MAbs a position 435 (Y/H) change in C4, abrogate binding. These MAbs can bind to V1 and V2 domains in the absence of C4 domain, so the C4 substitution probably results in conformational change. PubMed ID: 7687306.
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McKeating1993b
J. A. McKeating, J. Bennett, S. Zolla-Pazner, M. Schutten, S. Ashelford, A. Leigh-Brown, and P. Balfe. Resistance of a Human Serum-Selected Human Immunodeficiency Virus Type 1 Escape Mutant to Neutralization by CD4 Binding Site Monoclonal Antibodies Is Conferred by a Single Amino Acid Change in gp120. J. Virol., 67:5216-5225, 1993. PubMed ID: 7688820.
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Shotton1995
C. Shotton, C. Arnold, Q. Sattentau, J. Sodroski, and J. A. McKeating. Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 69:222-230, 1995. Anti-V2 linear and conformation dependent MAbs were studied. All V2 Abs studied could bind IIIB, but failed to neutralize non-clonal stocks. Epitope exposure is different in rgp120 compared to native gp120. HXB2 V2-MAb neutralization escape mutants were sequenced. PubMed ID: 7527084.
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Wu1995
Z. Wu, S. C. Kayman, W. Honnen, K. Revesz, H. Chen, S. V. Warrier, S. A. Tilley, J. McKeating, C. Shotton, and A. Pinter. Characterization of Neutralization Epitopes in the V2 Region of Human Immunodeficiency Virus Type 1 gp120: Role of Glycosylation in the Correct Folding of the V1/V2 Domain. J. Virol., 69:2271-2278, 1995. Most epitopes based only on numbering. PubMed ID: 7533854.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Pinter2005
Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930.
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Honnen2007
W. J. Honnen, C. Krachmarov, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and A. Pinter. Type-Specific Epitopes Targeted by Monoclonal Antibodies with Exceptionally Potent Neutralizing Activities for Selected Strains of Human Immunodeficiency Virus Type 1 Map to a Common Region of the V2 Domain of gp120 and Differ Only at Single Positions from the Clade B Consensus Sequence. J. Virol., 81(3):1424-1432, Feb 2007. PubMed ID: 17121806.
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Displaying record number 326
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Vaccine Details
Notes
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3 notes.
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12b: This epitope is similar to a fragment of the human protein macrophage colony stimulating factor I receptor SISIRLKVQK. Database note: Consistent with published papers, author Maksiutov is also shown as Maksyutov in this database.
Maksiutov2002
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12b: Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
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12b: V2 MAb neutralized HXB2 -- position 179-180 LD to DL abrogates binding -- competes with 60b, but not 74.
Shotton1995
References
Showing 3 of
3 references.
Maksiutov2002
A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Shotton1995
C. Shotton, C. Arnold, Q. Sattentau, J. Sodroski, and J. A. McKeating. Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 69:222-230, 1995. Anti-V2 linear and conformation dependent MAbs were studied. All V2 Abs studied could bind IIIB, but failed to neutralize non-clonal stocks. Epitope exposure is different in rgp120 compared to native gp120. HXB2 V2-MAb neutralization escape mutants were sequenced. PubMed ID: 7527084.
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Displaying record number 485
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MAb ID |
268-D (268-11-D-IV, 268D, 268, 268-11D, 268-10D, MAb 268, 268-10-D, ARP, 268-D IV) |
HXB2 Location |
Env(310-315) DNA(7152..7169) |
Env Epitope Map
|
Author Location |
gp120( MN) |
Research Contact |
Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center) |
Epitope |
HIGPGR
|
Epitope Alignment
|
Subtype |
B |
Ab Type |
gp120 V3 // V3 glycan (V3g) |
Neutralizing |
L |
Species
(Isotype)
|
human(IgG1λ) |
Patient |
268 |
Immunogen |
HIV-1 infection |
Keywords |
antibody binding site, antibody generation, antibody interactions, antibody sequence, binding affinity, dendritic cells, mimotopes, neutralization, review, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses |
Notes
Showing 39 of
39 notes.
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268-D: Two conserved tyrosine (Y) residues within the V2 loop of gp120, Y173 and Y177, were mutated individually or in combination, to either phenylalanine (F) or alanine (A) in several strains of diverse subtypes. In general, these mutations increased neutralization sensitivity, with a greater impact of Y177 over Y173 single mutations, of double over single mutations, and of A over F substitutions. The Y173A Y177A double mutation in HIV-1 BaL increased sensitivity to most of the weakly neutralizing MAbs tested (2158, 447-D, 268-D, B4e8, D19, 17b, 48d, 412d) and even rendered the virus sensitive to non-neutralizing antibodies against the CD4 binding site (F105, 654-30D, and b13). In the case of V2 mAb 697-30D, residue Y173 is part of its epitope, and thus abrogates its binding and has no effect on neutralization; the Y177A mutant alone did increase neutralization sensitivity to this mAb. When the double mutant was tested against bnAbs, there was a large decrease in neutralization sensitivity compared to WT for many bnAbs that target V1, V2, or V3 (PG9, PG16, VRC26.08, VRC38, PGT121, PGT122, PGT123, PGT126, PGT128, PGT130, PGT135, VRC24, CH103). The double mutation had lesser or no effect on neutralization by one V3 bnAb (2G12) and by most bnAbs targeting the CD4 binding site (VRC01, VRC07, VRC03, VRC-PG04, VRC-CH31, 12A12, 3BNC117, N6), the gp120-gp41 interface (35O22, PGT151), or the MPER (2F5, 4E10, 10E8).
Guzzo2018
(antibody binding site, neutralization)
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268-D: Most published structures of bnAbs, yet none of non- or poorly-neutralizing mAbs, were structurally compatible with a newly generated crystal structure of a mature ligand-free endoglycosidase H-treated BG505 SOSIP.664 Env trimer. Robust binding of the structurally incompatible V3- and CD4-bs targeting nAbs could be induced with CD4. A “DS” variant of BG505 SOSIP.664, containing a stabilizing disulfide bond between 201C and 433C mutations, was developed and appeared to represent an obligate intermediate in that it bound only a single CD4 and remained in a prefusion closed conformation. V3-targeting mAb CH58 was author-defined as ineffective (<15% neutralization breadth). This was consistent with structural modeling which suggested that CH58 was incompatible with BG505 SOSIP.664 when considering antibody-antigen-volume overlap yet compatible when considering epitope r.m.s deviation.
Kwon2015
(vaccine antigen design, structure)
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268: Antibody generation paper.
Gorny1991
(antibody generation)
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268: The capacity of 268-D IV to block completely the activity of the anti-HIV peptide T20 was investigated. T20 inhibited the fusion or syncytia formation between co-cultured CHO-WT cells expressing HIV-1 HXB2 envelope glycoprotein on their surface and HeLaT4 cells. 268-D IV was not able to block the anti-fusion effect of T20.
Vincent2012
(antibody interactions)
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268-D: Signature motifs specific for neutralization epitopes present in the V3 loop crown were used to determine the presence or absence of MAb-specific epitopes in vaccine immunogens and in break-through viruses infecting vaccine and placebo recipients in the VAX003 and VAX004 Phase III clinical trials. Of the six epitopes present in the immunogens and targeted by known NAbs, only the one targeted by anti-V3 NAb 2219 exhibited a significant reduction in occurrence in vaccinated subjects from VAX003 Thailand cohort compared to the placebo group. The signature motif used for MAb 268-D is [K,R]10, [H,R]13, P16, R18 in V3-loop position numbers.
Shmelkov2011
(vaccine-induced immune responses)
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268-D: Structure of 268-D bound to a peptide containing the sequence of the V3 loop was used to derive sensitive and specific signature motifs for its neutralization epitope. 268-D epitope (10[R,K]xx[H,R]xxPxR18) was found conserved in less than 10% of circulating HIV-1 strains, predominantly appearing in subtype B strains.
Swetnam2010
(antibody binding site, neutralization, subtype comparisons, structure)
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268-D: Crystal structure of 268-D in complex with V3 peptide revealed that 268-D binds predominantly to the side chains of three basic residues of the V3 crown: Lys305, His308, and Arg315. These are among the most variable residues in the V3 crown and may explain the narrow neutralizing activity of 268-D. Unlike 268-D, broadly neutralizing MAbs 2219, 2557 and 1006 engage conserved elements in four regions of the V3: the arch, the circlet, the band, and the V3 peptide main chain backbone. These conserved elements are either unaffected by or are subjected to minimal sequence variation. A mimotope that preserved the key structural elements in the circlet and band regions, but with GPG of the arch replaced by a disulfide bond, interacted with broadly reactive MAbs 2557, 1006 and 2219. It did not react with 447-52D nor 268-D, which are dependent on the Arg in the arch. Thus, mimotopes can be constructed that may focus the immune response on structurally conserved elements.
Jiang2010
(antibody binding site, mimotopes, structure)
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268-D IV: NL4.3 virus was cultured with cyclotriazadisulfonamide (CADA) and CADA-resistant virus was selected. 268-D MAb showed enhanced binding to the CADA-resistant virus compared to wildtype. The mutations in CADA-resistant virus are suggested to stabilize the conformation of gp120 and reduce glycosylation.
Vermeire2009
(binding affinity)
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268-11D: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:4-59*01, IGHD:5-12, D-RF:3, IGHJ:3. There was a preferential usage of the VH5-51 gene segment for V3 Abs. The usage of the VH4 family for the V3 Abs was restricted to only one gene segment, VH4-59, and the VH3 gene family was used at a significantly lower level by these Abs. The V3 Abs preferentially used the JH3 and D2-15 gene segments.
Gorny2009
(antibody sequence)
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268: Two chimeras were constructed from a new HIV-2KR.X7 proviral scaffold where the V3 region was substituted with the V3 from HIV-1 YU2 and Ccon, generating subtype B and C HIV-2 V3 chimera. The YU2 subtype B derived chimera was sensitive to neutralization by 268 MAb.
Davis2009
(neutralization)
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268-DI V: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 268-DI V belonged to the group 3 MAbs, which are able to bind subtype B but not subtype C gp120 and V3 peptide. 268-DI V was able to bind subtype B V3 in the subtype C Env backbone chimera, but not the reverse, indicating that 268-DI V binds to a structure created by the subtype B V3 sequence that is not impacted by the gp120 backbone. For both subtypes B and C, 268-DI V required H13 and R18 residues in order to bind, indicating that these residues likely define key aspects of the Ab epitope. 268-DI V was not able to neutralize JR-FL or SF162 isolates, but a chimeric SF162 variant with a JR-FL-like V3 sequence was hypersensitive to neutralization by this Ab.
Patel2008
(neutralization, binding affinity, subtype comparisons)
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268-D IV: This Ab was shown to inhibit HIV-1 BaL replication in macrophages but not in PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication occurs by an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles.
Holl2006
(neutralization, dendritic cells)
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268-D: The epitope for the MAb D19 is conserved and embedded in V3. D19 is unique in that for R5 viruses, it was cryptic and did not bind without exposure to sCD4, and for X4 and R5X4 isolates it was constitutively exposed. It had an overlapping binding region with MAbs 447-52D, B4e8, and 268-D, but different reactivity patterns and fine specificity.
Lusso2005
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268-D: Called 268: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4 induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not show as much ability to neutralize as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 268 was selected using V3 peptides.
Gorny2004
(antibody binding site)
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268-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, while many neutralize some TCLA strains, a subset can also neutralize some primary isolates.
Gorny2003
(review)
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268-D: NIH AIDS Research and Reference Reagent Program: 1511.
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268-D: UK Medical Research Council AIDS reagent: ARP3024.
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268-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera---2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5---thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain.
Zhang2002
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268-D: Called ARP3024: Herpesvirus saimiri-immortalized CD4+ T lymphocytes (HVS T cells) were used to isolate virus and perform HIV-1 neutralization assays, and compared with a standard PBMC protocol -- neutralization sensitivities to a panel of MAbs and to homologous or heterologous plasma/sera were similar for HVS T cells (CN-2 cells) and PBMCs.
Vella2002
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268-D: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding -- one of the TCLA V3 viruses 320SI-C3.3 shows reduced binding with this MAb, the sequence of the epitope in 320SI is HIGPGR and in 320SI-C3.3 is RIGPGR.
York2001
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268-D: Called 268D -- six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes.
Park2000
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268-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 268-D showed weak reactivity.
Nyambi2000
-
268-D: Ab responses, because of their capacity to alter antigen uptake and processing, can influence helper T cell responses -- CD4BS MAbs or serum Ig from HIV+ individuals inhibited proliferative responses of gp120 specific T cells -- V3 MAbs 447-52-D and 268-10-D did not affect proliferation.
Hioe2000
-
268-D: Called MAb 268 -- To identify potential mimotopes of V3, a hexapeptide phage library was screened with MAb 268 -- two hexamers were identified, HLGPGR or KAIHRI that bind to 268 with the same binding site as the V3 loop and inhibit 268 MN gp120 -- KLH conjugated hexamer KAIHRI stimulates Abs in rabbits that cross-react with ML gp120.
Laisney1999
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268-D: Called 268-11D -- Study of a live-vector mucosal vaccine that expresses HIV-1 V3 domains using the bacterium Streptococcus gordonii which can express heterologous Ag and can colonize the oral cavity and vagina of mice -- 268-D and 257-D recognized S. gordonii expressing the V3 domain of MN -- the vaccine stimulated V3-specific IgG2a in mice.
Oggioni1999
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268-D: rgp120 derived from a R5X4 subtype B virus, HIV-1 W61D, was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- 268-D bound rgp120 W61D but could only neutralize the W61D isolate following T-cell line adaptation.
Beddows1999
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268-D: Peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group -- MAb 453, with an identical core epitope to 268 based on prior experiments (HIGPGR), was not part of this reactivity group, illustrating that context can be critical.
Zolla-Pazner1999a
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268-D: Review of clade specificity and anti-V3 HIV-1-Abs.
Zolla-Pazner1999b
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268-D: A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to be neutralized by anti-V3 MAbs -- the primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, however the TCLA derivative uses CXCR4 only and is neutralized.
LaCasse1998
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268-D: Poor reactivity against HIV-1 isolates SF162 and SF128A and no neutralization, in contrast to MAbs 391/95-D and 257-D.
Stamatatos1997
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268-D: 268-D is V H4 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals.
Wisnewski1996
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268-D: Failed to neutralize HXB2 and chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
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268-D: The binding of conformation-dependent anti-V2, anti-V3, and anti-CD4BS MAbs to monomeric and virion-associated gp120 from HIV-1 isolates with differences in cell tropism was studied -- V3 loop epitopes were less accessible to Ab binding on the virion surface than in the gp120 monomer, particularly for macrophage-tropic isolates SF162 and SF128a, relative to T-cell tropic SF2 -- sCD4 association with gp120 did not influence the binding of 268-D to virion-associated gp120, although sCD4 binding did alter epitope exposure for other anti-V3 MAbs.
Stamatatos1995
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268-D: Serotyping study using flow-cytometry, if H of HIGPGR was substituted in virus, 268-D did not bind.
Zolla-Pazner1995
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268-D: Moderate dissociation rate and homologous neutralization titer.
VanCott1994
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268-D: Mediated deposition of complement component C3 on HIV infected cells, but not in the presence of sCD4.
Spear1993
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268-D: Neutralizes MN -- binds SF2: YIGPGR -- specificity: MN, SF2, NY5, RF, CDC4.
Gorny1993
-
268-D: Reacts with MN, NY5, CDC4, RF and SF2, does not cross-react with WM52 or HXB2.
Karwowska1992a
-
268-D: Called 268-11-D-IV -- strain specific weakly neutralizing.
DSouza1991
References
Showing 39 of
39 references.
Isolation Paper
Gorny1991
M. K. Gorny, J.-Y. Xu, V. Gianakakos, S. Karwowska, C. Williams, H. W. Sheppard, C. V. Hanson, and S. Zolla-Pazner. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein. Proc. Natl. Acad. Sci. U.S.A., 88:3238-3242, 1991. PubMed ID: 2014246.
Show all entries for this paper.
Beddows1999
S. Beddows, S. Lister, R. Cheingsong, C. Bruck, and J. Weber. Comparison of the Antibody Repertoire Generated in Healthy Volunteers following Immunization with a Monomeric Recombinant gp120 Construct Derived from a CCR5/CXCR4-Using Human Immunodeficiency Virus Type 1 Isolate with Sera from Naturally Infected Individuals. J. Virol., 73:1740-1745, 1999. PubMed ID: 9882391.
Show all entries for this paper.
Davis2009
Katie L. Davis, Frederic Bibollet-Ruche, Hui Li, Julie M. Decker, Olaf Kutsch, Lynn Morris, Aidy Salomon, Abraham Pinter, James A. Hoxie, Beatrice H. Hahn, Peter D. Kwong, and George M. Shaw. Human Immunodeficiency Virus Type 2 (HIV-2)/HIV-1 Envelope Chimeras Detect High Titers of Broadly Reactive HIV-1 V3-Specific Antibodies in Human Plasma. J. Virol., 83(3):1240-1259, Feb 2009. PubMed ID: 19019969.
Show all entries for this paper.
DSouza1991
M. P. D'Souza, P. Durda, C. V. Hanson, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 by Neutralization and Serological Assays: An International Collaboration. AIDS, 5:1061-1070, 1991. PubMed ID: 1718320.
Show all entries for this paper.
Fontenot1995
J. D. Fontenot, T. C. VanCott, B. S. Parekh, C. P. Pau, J. R. George, D. L. Birx, S. Zolla-Pazner, M. K. Gorny, and J. M. Gatewood. Presentation of HIV V3 Loop Epitopes for Enhanced Antigenicity, Immunogenicity and Diagnostic Potential. AIDS, 9:1121-1129, 1995. PubMed ID: 8519447.
Show all entries for this paper.
Gorny1993
M. K. Gorny, J.-Y. Xu, S. Karwowska, A. Buchbinder, and S. Zolla-Pazner. Repertoire of Neutralizing Human Monoclonal Antibodies Specific for The V3 Domain of HIV-1 gp120. J. Immunol., 150:635-643, 1993. Characterizaton of 12 human MAbs that bind and neutralize the MN isolate with 50\% neutralization. Two of these antibodies also bound and neutralized IIIB: 447-52-D and 694/98-D; all others could not bind HXB2 peptides. All but two, 418-D and 412-D could bind to SF2 peptides. PubMed ID: 7678279.
Show all entries for this paper.
Gorny2003
Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162.
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Gorny2004
Miroslaw K. Gorny, Kathy Revesz, Constance Williams, Barbara Volsky, Mark K. Louder, Christopher A. Anyangwe, Chavdar Krachmarov, Samuel C. Kayman, Abraham Pinter, Arthur Nadas, Phillipe N. Nyambi, John R. Mascola, and Susan Zolla-Pazner. The V3 Loop is Accessible on the Surface of Most Human Immunodeficiency Virus Type 1 Primary Isolates and Serves as a Neutralization Epitope. J. Virol., 78(5):2394-2404, Mar 2004. PubMed ID: 14963135.
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Gorny2009
Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295.
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Hioe1997b
C. E. Hioe, S. Xu, P. Chigurupati, S. Burda, C. Williams, M. K. Gorny, and S. Zolla-Pazner. Neutralization of HIV-1 Primary Isolates by Polyclonal and Monoclonal Human Antibodies. Int. Immunol., 9(9):1281-1290, Sep 1997. PubMed ID: 9310831.
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Hioe2000
C. E. Hioe, G. J. Jones, A. D. Rees, S. Ratto-Kim, D. Birx, C. Munz, M. K. Gorny, M. Tuen, and S. Zolla-Pazner. Anti-CD4-Binding Domain Antibodies Complexed with HIV Type 1 Glycoprotein 120 Inhibit CD4+ T Cell-Proliferative Responses to Glycoprotein 120. AIDS Res. Hum. Retroviruses, 16:893-905, 2000. PubMed ID: 10875615.
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Holl2006
Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957.
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Jiang2010
Xunqing Jiang, Valicia Burke, Maxim Totrov, Constance Williams, Timothy Cardozo, Miroslaw K. Gorny, Susan Zolla-Pazner, and Xiang-Peng Kong. Conserved Structural Elements in the V3 Crown of HIV-1 gp120. Nat. Struct. Mol. Biol., 17(8):955-961, Aug 2010. PubMed ID: 20622876.
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Karwowska1992a
S. Karwowska, M. K. Gorny, A. Buchbinder, and S. Zolla-Pazner. Type-specific human monoclonal antibodies cross-react with the V3-loop of various HIV-1 isolates. Vaccines 92, :171-174, 1992. Editors: F. Brown, H. S. Ginsberg and R. Lerner, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
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LaCasse1998
R. A. LaCasse, K. E. Follis, T. Moudgil, M. Trahey, J. M. Binley, V. Planelles, S. Zolla-Pazner, and J. H. Nunberg. Coreceptor utilization by human immunodeficiency virus type 1 is not a primary determinant of neutralization sensitivity. J. Virol., 72:2491-5, 1998. A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to to be neutralized by anti-V3 MAbs 257-D, 268-D and 50.1. The primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, but the TCLA derivative uses CXCR4 only and is neutralized. Thus coreceptor usage is not the primary determinant of differential neutralization sensitivity in primary versus TCLA strains. PubMed ID: 9499111.
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Laisney1999
I. L. Laisney and A. D. Strosberg. Dual Specificity of a Human Neutralizing Monoclonal Antibody, Specific for the V3 Loop of GP120 (HIV-1). Immunol. Lett., 67:185-192, 1999. PubMed ID: 10369125.
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Lusso2005
Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Nyambi2000
P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650.
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Oggioni1999
M. R. Oggioni, D. Medaglini, L. Romano, F. Peruzzi, T. Maggi, L. Lozzi, L. Bracci, M. Zazzi, F. Manca, P. E. Valensin, and G. Pozzi. Antigenicity and Immunogenicity of the V3 Domain of HIV Type 1 Glycoprotein 120 Expressed on the Surface of Streptococcus gordonii. AIDS Res. Hum. Retroviruses, 15:451-459, 1999. PubMed ID: 10195755.
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Park2000
E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031.
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Patel2008
Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735.
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Shmelkov2011
Evgeny Shmelkov, Arthur Nadas, James Swetnam, Susan Zolla-Pazner, and Timothy Cardozo. Indirect Detection of an Epitope-Specific Response to HIV-1 gp120 Immunization in Human Subjects. PLoS One, 6(11):e27279, 2011. PubMed ID: 22076145.
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Spear1993
G. T. Spear, D. M. Takefman, B. L. Sullivan, A. L. Landay, and S. Zolla-Pazner. Complement activation by human monoclonal antibodies to human immunodeficiency virus. J. Virol., 67:53-59, 1993. This study looked at the ability of 16 human MAbs to activate complement. MAbs directed against the V3 region could induce C3 deposition on infected cells and virolysis of free virus, but antibodies to the CD4BS and C-terminal region and two regions in gp41 could induce no complement mediated effects. Pre-treatment with sCD4 could increase complement-mediated effects of anti-gp41 MAbs, but decreased the complement-mediated effects of V3 MAbs. Anti-gp41 MAbs were able to affect IIIB but not MN virolysis, suggesting spontaneous shedding of gp120 on IIIB virions exposes gp41 epitopes. IgG isotype did not appear to have an effect on virolysis or C3 deposition. PubMed ID: 7677959.
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Stamatatos1995
L. Stamatatos and C. Cheng-Mayer. Structural Modulations of the Envelope gp120 Glycoprotein of Human Immunodeficiency Virus Type 1 upon Oligomerization and the Differential V3 Loop Epitope Exposure of Isolates Displaying Distinct Tropism upon Viral-Soluble Receptor Binding. J. Virol., 69:6191-6198, 1995. PubMed ID: 7545244.
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Stamatatos1997
L. Stamatatos, S. Zolla-Pazner, M. K. Gorny, and C. Cheng-Mayer. Binding of Antibodies to Virion-Associated gp120 Molecules of Primary-Like Human Immunodeficiency Virus Type 1 (HIV-1) Isolates: Effect on HIV-1 Infection of Macrophages and Peripheral Blood Mononuclear Cells. Virology, 229:360-369, 1997. PubMed ID: 9126249.
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Swetnam2010
James Swetnam, Evgeny Shmelkov, Susan Zolla-Pazner, and Timothy Cardozo. Comparative Magnitude of Cross-Strain Conservation of HIV Variable Loop Neutralization Epitopes. PLoS One, 5(12):e15994, 2010. PubMed ID: 21209919.
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VanCott1994
T. C. VanCott, F. R. Bethke, V. R. Polonis, M. K. Gorny, S. Zolla-Pazner, R. R. Redfield, and D. L. Birx. Dissociation Rate of Antibody-gp120 Binding Interactions Is Predictive of V3-Mediated Neutralization of HIV-1. J. Immunol., 153:449-459, 1994. Using surface plasmon resonance it was found that the rate of the dissociation of the MAb-gp120 complex, but not the association rate, correlated with MAbs ability to neutralize homologous virus (measured by 50\% inhibition of p24 production). Association constants were similar for all MAbs tested, varying less than 4-fold. Dissociation rate constants were quite variable, with 100-fold differences observed. PubMed ID: 7515931.
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Vella2002
Cherelyn Vella, Natalie N. Zheng, Philippa Easterbrook, and Rod S. Daniels. Herpesvirus saimiri-Immortalized Human Lymphocytes: Novel Hosts for Analyzing HIV Type 1 in Vitro Neutralization. AIDS Res. Hum. Retroviruses, 18(13):933-946, 1 Sep 2002. PubMed ID: 12230936.
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Vermeire2009
Kurt Vermeire, Kristel Van Laethem, Wouter Janssens, Thomas W. Bell, and Dominique Schols. Human Immunodeficiency Virus Type 1 Escape from Cyclotriazadisulfonamide-Induced CD4-Targeted Entry Inhibition Is Associated with Increased Neutralizing Antibody Susceptibility. J. Virol., 83(18):9577-9583, Sep 2009. PubMed ID: 19570853.
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Vincent2012
Nadine Vincent and Etienne Malvoisin. Ability of Antibodies Specific to the HIV-1 Envelope Glycoprotein to Block the Fusion Inhibitor T20 in a Cell-Cell Fusion Assay. Immunobiology, 217(10):943-950, Oct 2012. PubMed ID: 22387075.
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Wisnewski1996
A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730.
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York2001
J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697.
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Zhang2002
Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155.
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Zolla-Pazner1995
S. Zolla-Pazner, J. O'Leary, S. Burda, M. K. Gorny, M. Kim, J. Mascola, and F. McCutchan. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J. Virol., 69:3807-3815, 1995. A set of 13 human MAbs to a variety of epitopes were tested against a panel of primary isolates of HIV-1, representing different genetic clades. The V3 loop tended to be B clade restricted, and a single gp120 C-terminus binding antibody was clade specific. Two other gp120 C-terminus binding antibodies were group specific. PubMed ID: 7745728.
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Zolla-Pazner1999a
S. Zolla-Pazner, M. K. Gorny, P. N. Nyambi, T. C. VanCott, and A. Nadas. Immunotyping of Human Immunodeficiency Virus Type 1 (HIV): An Approach to Immunologic Classification of HIV. J. Virol., 73:4042-4051, 1999. 21 human anti-V3 MAbs were studied with respect to cross-clade reactivity and immunological relationship to other human anti-V3 MAbs. Broad cross-reactivities were observed, and V3 peptides were grouped into immunotypes that contained peptides from several clades. PubMed ID: 10196300.
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Zolla-Pazner1999b
S. Zolla-Pazner, M. K. Gorny, and P. N. Nyambi. The implications of antigenic diversity for vaccine development. Immunol. Lett., 66:159-64, 1999. PubMed ID: 10203049.
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Kwon2015
Young Do Kwon, Marie Pancera, Priyamvada Acharya, Ivelin S. Georgiev, Emma T. Crooks, Jason Gorman, M. Gordon Joyce, Miklos Guttman, Xiaochu Ma, Sandeep Narpala, Cinque Soto, Daniel S. Terry, Yongping Yang, Tongqing Zhou, Goran Ahlsen, Robert T. Bailer, Michael Chambers, Gwo-Yu Chuang, Nicole A. Doria-Rose, Aliaksandr Druz, Mark A. Hallen, Adam Harned, Tatsiana Kirys, Mark K. Louder, Sijy O'Dell, Gilad Ofek, Keiko Osawa, Madhu Prabhakaran, Mallika Sastry, Guillaume B. E. Stewart-Jones, Jonathan Stuckey, Paul V. Thomas, Tishina Tittley, Constance Williams, Baoshan Zhang, Hong Zhao, Zhou Zhou, Bruce R. Donald, Lawrence K. Lee, Susan Zolla-Pazner, Ulrich Baxa, Arne Schön, Ernesto Freire, Lawrence Shapiro, Kelly K. Lee, James Arthos, James B. Munro, Scott C. Blanchard, Walther Mothes, James M. Binley, Adrian B. McDermott, John R. Mascola, and Peter D. Kwong. Crystal Structure, Conformational Fixation and Entry-Related Interactions of Mature Ligand-Free HIV-1 Env. Nat. Struct. Mol. Biol., 22(7):522-531, Jul 2015. PubMed ID: 26098315.
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Guzzo2018
Christina Guzzo, Peng Zhang, Qingbo Liu, Alice L. Kwon, Ferzan Uddin, Alexandra I. Wells, Hana Schmeisser, Raffaello Cimbro, Jinghe Huang, Nicole Doria-Rose, Stephen D. Schmidt, Michael A. Dolan, Mark Connors, John R. Mascola, and Paolo Lusso. Structural Constraints at the Trimer Apex Stabilize the HIV-1 Envelope in a Closed, Antibody-Protected Conformation. mBio, 9(6), 11 Dec 2018. PubMed ID: 30538178.
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Displaying record number 815
Download this epitope
record as JSON.
MAb ID |
2F5 (IAM 2F5, IAM-41-2F5, IAM2F5, c2F5) |
HXB2 Location |
Env(662-667) DNA(8208..8225) |
Env Epitope Map
|
Author Location |
gp41(662-667) |
Research Contact |
Hermann Katinger, Institute of Applied Microbiology, Vienna, or Polymun Scientific Inc., Vienna, Austria |
Epitope |
ELDKWA
|
Epitope Alignment
|
Subtype |
B |
Ab Type |
gp41 MPER (membrane proximal external region) |
Neutralizing |
L P (tier 2) View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human(IgG3κ) |
Patient |
|
Immunogen |
HIV-1 infection |
Keywords |
acute/early infection, adjuvant comparison, anti-idiotype, antibody binding site, antibody gene transfer, antibody generation, antibody interactions, antibody lineage, antibody polyreactivity, antibody sequence, assay or method development, autoantibody or autoimmunity, autologous responses, binding affinity, brain/CSF, broad neutralizer, co-receptor, complement, computational prediction, contact residues, dendritic cells, drug resistance, dynamics, early treatment, effector function, elite controllers and/or long-term non-progressors, enhancing activity, escape, genital and mucosal immunity, germline, glycosylation, HAART, ART, HIV exposed persistently seronegative (HEPS), HIV reservoir/latency/provirus, immunoprophylaxis, immunotherapy, immunotoxin, isotype switch, kinetics, memory cells, mimics, mimotopes, mother-to-infant transmission, mutation acquisition, neutralization, polyclonal antibodies, rate of progression, responses in children, review, SIV, structure, subtype comparisons, supervised treatment interruptions (STI), therapeutic vaccine, transmission pair, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity, viral fitness and/or reversion |
Notes
Showing 591 of
591 notes.
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2F5: The study describes the generation, crystal structure, and immunogenic properties of a native-like Env SOSIP trimer based on a group M consensus (ConM) sequence. A crystal structure of ConM SOSIP.v7 trimer together with nAbs PGT124 and 35O22 revealed that ConM SOSIP.v7 is structurally similar to other Env trimers. In rabbits, the ConM SOSIP trimer induced serum nAbs that neutralized the autologous Tier 1A virus (ConM from 2004) and a related Tier 1B ConS virus (ConM from 2001). These responses target the trimer apex and were enhanced when the trimers were presented on ferritin nanoparticles. The neutralization of ConM and ConS pseudoviruses was tested against a large panel of nAbs and non-nAbs (2219, 2557, 3074, 3869, 447-52D, 830A, 654-30D, 1008-30D, 1570D, 729-30D, F105, 181D, 246D, 50-69D, sCD4, VRC01, 3BNC117, CH31, PG9, PG16, CH01, PGDM1400, PGT128, PGT121, 10-1074, PGT151, VRC43.01, 2G12, DH511.2_K3, 10E8, 2F5, 4E10); most nAbs were able to neutralize these pseudoviruses. Soluble ConM trimers were able to weakly activate B cells expressing PGT121 and PG16 BCRs but were inactive against those expressing VRC01 and PGT145. In contrast, at the same molar amount of trimers, the ConM SOSIP.v7-ferritin nanoparticles activated all 4 B cells efficiently. Binding of bnAbs 2G12 and PGT145 and non-nAbs F105 and 19b to ConM SOSIP.v7 trimer and SOSIP showed that the ferritin-bound trimer bound more avidly than the soluble trimer. This study shows that native-like HIV-1 Env trimers can be generated from consensus sequences, and such immunogens might be suitable vaccine components to prime and/or boost desirable nAb responses.
Sliepen2019
(neutralization, vaccine antigen design)
-
2F5: A SHIV carrying a highly neutralization-sensitive Env (SHIVCNE40) was passaged in macaques. SHIVCNE40 developed enhanced replication kinetics associated with neutralization resistance against autologous serum, CD4-Ig, and several nAbs (17b, 3BNC117, N6, PGT145, PGT121, PGT128, 35O22, 2F5, 10E8). A gp41 substitution, E658K, was the major determinant for this resistance. Structural modeling and functional verification indicate that the substitution disrupts an intermolecular salt bridge with the neighboring protomer, thereby promoting fusion and facilitating immune evasion. This effect is applicable across many HIV-1 viruses of diverse subtypes. These results highlight the critical role of gp41 in shaping the neutralization profile and conformation of Env during viral adaptation. The unique intermolecular salt bridge could potentially be utilized for rational vaccine design involving more stable HIV-1 Env trimers.
Wang2019
(mutation acquisition, neutralization, structure)
-
2F5: A panel of 30 contemporary subtype B pseudoviruses (PSVs) was generated. Neutralization sensitivities of these PSVs were compared with subtype B strains from earlier in the pandemic using 31 nAbs (PG9, PG16, PGT145, PGDM1400, CH02, CH03, CH04, 830A, PGT121, PGT126, PGT128, PGT130, 10-1074, 2192, 2219, 3074, 3869, 447-52D, b12, NIH45-46, VRC01, VRC03, 3BNC117, HJ16, sCD4, 10E8, 4E10, 2F5, 7H6, 2G12, 35O22). A significant reduction in Env neutralization sensitivity was observed for 27 out of 31 nAbs for the contemporary, as compared to earlier-decade subtype B PSVs. A decline in neutralization sensitivity was observed across all Env domains; the nAbs that were most potent early in the pandemic suffered the greatest decline in potency over time. A metaanalysis demonstrated this trend across multiple subtypes. As HIV-1 Env diversification continues, changes in Env antigenicity and neutralization sensitivity should continue to be evaluated to inform the development of improved vaccine and antibody products to prevent and treat HIV-1.
Wieczorek2023
(neutralization, viral fitness and/or reversion)
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2F5: Pseudoviruses were made from 13 env sequences of subtypes A6 and CRF63_02A6, based on genetic variants of HIV-1 circulating in the Siberian Federal District. Neutralization of these viruses was tested for 8 bnAbs. Most of the pseudoviruses were sensitive to neutralization by VRC01, PGT126, and 10E8, moderately sensitive to PG9 and 4E10, and resistant to 2G12, PG16, and 2F5. All obtained variants of pseudoviruses were CCR5-tropic.
Rudometova2022
(co-receptor, neutralization, subtype comparisons)
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2F5:This study identified a B cell lineage of bNAbs in an HIV-1 elite post-treatment controller (ePTC; donor: PTC-005002). Circulating viruses in PTC escaped bNAb pressure but remained sensitive to autologous neutralization by other Ab populations. 2F5 was used as a reference control IgG. 2F5, 4E10 and 10E8 were used as positive controls, and mGO53 as a negative control in determining reactivity of IgG Abs and conserved neutralizing epitopes in the autologous virus isolated from PTC-005002.
Molinos-Albert2023
(antibody binding site, binding affinity)
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2F5: This study reports the glycan binding specificities and atomic level details of PG16 epitope and somatic mechanisms of clonal antibody diversification. MAb 2F5 was positive in an assay of autoreactivity.
Pancera2013
(autoantibody or autoimmunity)
-
2F5: A panel of 58 mAbs was cloned from a rhesus macaque immunized with envelope glycoprotein immunogens developed from HIV-1 clade B-infected human donor VC10014. Neutralizing mAbs predominantly targeted linear epitopes in the V3 region in the cradle orientation (V3C), with others targeting the V3 ladle orientation (V3L), the CD4 binding site, C1, C4, or gp41. Nonneutralizing mAbs bound C1, C5, or undetermined gp120 conformational epitopes. Neutralization potency strongly correlated with the magnitude of binding to infected primary macaque splenocytes and to the level of ADCC, but did not correlate with ADCP. MAbs were traced to 23 of 72 functional IgHV germline alleles. Neutralizing V3C mAbs displayed minimal nucleotide SHM in the H chain V region (3.77%), indicating that relatively little affinity maturation was needed to achieve in-clade neutralization breadth. This study underscores the polyfunctional nature of vaccine-elicited tier 2-neutralizing V3 Abs and demonstrates partial reproduction of a human donor’s Ab response through nonhuman primate vaccination. Several previously-isolated mAbs were used in binding assays: b12, VRC01, N6, 3BNC117, 2558, 2219, 1006-15D, 447-52D, 10-1074, 830A, 2F5, F240, PGDM1400, 2219.
Spencer2021
(vaccine antigen design, binding affinity)
-
2F5: This study analyzed Env sequences of early HIV-1 clonal variants from 31 individuals from the Amsterdam Cohort Studies with diverse levels of heterologous neutralization at 2-4 years post-seroconversion. A number of Env signatures coincided with neutralization development. These included a statistically shorter variable region 1 and a lower probability of glycosylation. Induction of neutralization was associated with a lower probability of glycosylation at position 332, which is involved in the epitopes of many bnAbs. 2G12 and PGT126 were tested for their ability to block infectivity by patient viruses with predicted glycosylation at N332; the NLS glycosylation motif was associated with resistance to these mAbs more often than the NIS glycosylation motif. Sequence Harmony software identified amino acid changes associated with the development of heterologous neutralization. These residues mapped to various Env subdomains, but in particular to the first and fourth variable region, as well as the underlying α2 helix of the third constant region. These findings imply that the development of heterologous neutralization might depend on specific characteristics of early Env. Env signatures that correlate with the induction of neutralization might be relevant for the design of effective HIV-1 vaccines. Primary virus isolates from 21 of the patients were assayed for neutralization by 11 well-known nAbs (b12, VRC01, 447-52D, 2G12, PGT121, PGT126, PG9, PG16, PGT145, 2F5, 4E10).
vandenKerkhof2013
(glycosylation, neutralization, vaccine antigen design, polyclonal antibodies)
-
2F5: The polyclonal response of human subjects VC20013 and VC10014 demonstrated increasing neutralization breadth against a panel of HIV-1 isolates over time. Full-length functional env genes were cloned longitudinally from these subjects from months after infection through 2.6 to 5.8 years of infection. Motifs associated with the development of breadth in published, cross-sectional studies were found in the viral sequences of both subjects. To test the immunogenicity of envelope vaccines derived from time points obtained during and after broadening of neutralization activity within these subjects, rabbits were coimmunized 4 times with selected multiple gp160 DNAs and gp140-trimeric envelope proteins. In an assay of rabbit polyclonal responses, the most rapid and persistent neutralization of multiclade tier 1 viruses was elicited by envelopes that were circulating in plasma at time points prior to the development of 50% neutralization breadth in both human subjects. The breadth elicited in rabbits was not improved by exposure to later envelope variants. Env immunogen sequences were tested for binding to a panel of well studied mAbs of various binding types (VRC01, HJ16, b12, b6, PG9, PGT121, 2G12, 2F5, F240); all gp140s bound to weak or non-neutralizing antibodies b6 and F240. MAb b6 also bound BG505 SOSIP, while F240 did not, suggesting that cluster I gp41 epitopes, which become exposed during gp120 shedding, are more easily accessed on these trimers than on BG505-SOSIP. These data have implications for vaccine development in describing a target time point to identify optimal env immunogens.
Malherbe2014
(vaccine antigen design, vaccine-induced immune responses, binding affinity, polyclonal antibodies)
-
2F5: This study explored the basis of the neutralization resistance of tier 3 virus 253-11 (subtype CRF02_AG). Virus 253-11 was resistant to neutralization by 17b, b12, VRC03, F105, SCD4, CH12, Z13e1, PG16, PGT145, 2G12, PGT121, PGT126, PGT128, PGT130, 39F, F240, and 35O22; the virus was sensitive to 3BNC117, NIH45-46G54W, VRC01, 10E8, 2F5, 4E10, PG9, VRC26.26, 10-1074, and PGT151. Virus 253-11 was strikingly resistant to most tested antibodies that target V3/glycans, despite possessing key potential N-linked glycosylation sites, especially N301 and N332, needed for the recognition of this class of antibodies. The resistance of 253-11 was not associated with an unusually long V1/V2 loop, nor with polymorphisms in the V3 loop and N-linked glycosylation sites. The 253-11 MPER was rarely recognized by sera, but was more often recognized in a chimera consisting of a HIV-2 backbone with the 253-11 MPER, suggesting steric or kinetic hindrance of the MPER. Mutations in the 253-11 MPER previously reported to increase the lifetime of the prefusion Env conformation (Y681H, L669S), decreased the resistance of 253-11 to several mAbs, presumably destabilizing its otherwise stable, closed trimer structure. A crystal structure of a recombinant 253-11 SOSIP trimer revealed that the heptad repeat helices in gp41 are drawn in close proximity to the trimer axis and that gp120 protomers also showed a relatively compact form around the trimer axis.
Moyo2018
(neutralization, structure)
-
2F5: This study used directed evolution to overcome the instability and heterogeneity of a primary Env isolate (ADA) in order to design better immunogens. HIV-1 virions were subjected to iterative cycles of destabilization and replication to select for Envs with enhanced stability. Several mutations in Env were associated with increased trimer stability, primarily in the heptad repeat regions of gp41 and V1 of gp120. Mutations from the most stable Envs were combined into a variant Env, termed "comb-mut", with superior homogeneity and stability. Comb-mut had greater binding affinity for PGT128, PG9, PG16, 2G12, VRC01, b12, and CD4-IgG2, but decreased binding to 4E10, 2F5, b6, 19b, 17b, 7B2, and D50. Comb-mut was more sensitive to neutralization by PG9. One specific mutation (K574) was shown to decrease the neutralization IC50 of mAbs b12, 2F5, 4E10, b6, 2G12, 8K8 and inhibitors sCD4, T-20, and PF-68742. Several of the Env substitutions were shown to stabilize Env spikes from HIV-1 clades A, B, and C. Spike stabilizing mutations may be useful in the development of Env immunogens that stably retain native, trimeric structure.
Leaman2013
(mimics, neutralization, vaccine antigen design, binding affinity)
-
2F5: Persistent (VP-1) and Non-persistent (VP-2) viruses were compared in a longitudinal study of a cross-reactive neutralizing serum-possessing patient, Patient B (H19554) over 9 years. Persisting VP-1 viral clones had more mutations in variable loops V1V2 and constant region C3 of Env, particularly in the number of PNGS (potential N-linked glycosylation sites) in V1V2. While VP-1 in vitro virus chimeras showed slower replication kinetics than VP-2, there was no neutralization sensitivity change based on whether they were R5 or X4 variants. The gp160 Env was longer in the VP-2 population; but both VP-1 and VP-2 chimeras had widely varying sensitivities to bnAb 2F5.
vanGils2011a
(glycosylation, mutation acquisition, escape)
-
2F5: This paper describes the development and characterization of soluble, cleaved SOSIP gp140 Env trimers using a JR-FL background. In addition to a stabilizing disulfide bond, mediated by engineered mutations A501C and T605C that are also present in SOS gp140 proteins, SOSIP gp140 proteins have an I559P mutation (aka “IP”) that increases trimer stability. Further analyses suggested that I559P destabilizes the N-terminal helix necessary for the six-helix bundle structure in the postfusion conformation. Immunoprecipitation assays with mAbs CD4-IgG2, b12 (aka IgG1b12), 17b, 2F5, 2.2B and 4D4 demonstrated that I559P did not alter expected structural epitopes when compared to SOS gp140 proteins. MAb b12 was able to bind efficiently to its epitope, located close to the C terminus of gp41, on both SOS and SOSIP gp140 proteins.
Sanders2002a
(vaccine antigen design)
-
2F5: REVIEW: This review discusses isotype switching. Several anti-HIV mAbs are mentioned as having isotype switch variants: F105, F425 B4e8, F240, 2F5, and PGT121.
Janda2016
(isotype switch, review)
-
2F5: A recombinant native-like Env SOSIP trimer, AMC009, was developed based on viral founder sequences of elite neutralizer H18877. The subtype B AMC009 Env was defined as a Tier 2 virus based on a neutralization assay against well known nAbs (VRC01, 3BNC117, CH31, CH01, PG9, PG16, PGDM1400, 10-1074, PGT128, PGT121, PGT151, VRC34.01, 2G12, 2F5, 4E10, DH511.2.K3_4, 10E8, and the mAb mixture CH01-31).The AMC009 SOSIP protein formed stable native-like trimers that displayed multiple bnAb epitopes. Its overall structure was similar to that of BG505 SOSIP.664, and it resembled one from another elite neutralizer, AMC011, in having a dense and complete glycan shield. When tested as immunogens in rabbits, AMC009 trimers did not induce autologous neutralizing antibody responses efficiently, while the AMC011 trimers did so very weakly, outcomes that may reflect the completeness of their glycan shields. The AMC011 trimer induced antibodies that occasionally cross-neutralized heterologous tier 2 viruses, sometimes at high titer. Cross-neutralizing antibodies were more frequently elicited by a trivalent combination of AMC008, AMC009, and AMC011 trimers, all derived from subtype B viruses. Each of these three individual trimers could deplete the nAb activity from rabbit sera. Mapping the polyclonal sera by electron microscopy revealed that antibodies of multiple specificities could bind to sites on both autologous and heterologous trimers.
Schorcht2020
(neutralization, vaccine-induced immune responses, structure)
-
2F5: A chronic HIV-1 infected patient (CBJC504) had neutralizing activity against Env MPER. Fifty full-length HIV-1 env genes were isolated from the patient’s plasma at 2 time points (2006 and 2009). The neutralization sensitivity of 14 Env pseudoviruses to autologous plasma and mAbs 4E10, 2F5, and 10E8 was evaluated. Env sequencing revealed that the diversity of Env increased over time, and 4 mutation positions in MPER acquired mutations (659D, 662K, 671S, and 677N/R). The K677R mutation increased the IC50 values of pseudoviruses approximately twofold for 4E10 and 2F5, and E659D increased the IC50 up to ninefold for 4E10 and fourfold for 2F5. These 2 mutations also decreased the contact between gp41 and mAbs. Almost all mutant pseudoviruses were resistant to autologous plasma at both time points. These findings shed light on MPER evolution.
Tang2023
(autologous responses, mutation acquisition, neutralization, escape, polyclonal antibodies)
-
2F5: HIV-1 bnAbs require high levels of activation-induced cytidine deaminase (AID)-catalyzed somatic mutations. Probable mutations occur at sites of frequent AID activity, while improbable mutations occur where AID activity is infrequent. The paper introduced the ARMADiLLO program, which estimates how probable a particular mAb mutation is, and thus the key improbable mutations were defined for a panel of 26 bnAbs. The number of improbable mutations ranged from 7 (PGT128) to 23 (VRC01 and 35O22); 2F5 had 10 improbable mutations out of 31 total AA mutations, and 0 indels. Single-amino acid reversion mutants were made for key improbable mutations of 3 bnAbs (CH235, VRC01, and BF520.1), and these mutant mAbs were tested for their neutralization ability. The study also noted that bnAbs that had relatively small numbers of improbable single somatic mutations had other unusual characteristics that were due to additional improbable events, such as indels (PGT128) or extraordinary CDR H3 lengths (VRC26.25).
Wiehe2018
(neutralization)
-
2F5: The study assessed the breadths and potencies of 14 bnAbs against 36 viruses reactivated from peripheral blood CD4+ T cells from ARV-treated HIV-infected individuals by using paired neutralization and infected cell binding assays. Infected cell binding correlated with virus neutralization for 10 of 14 antibodies (VRC01, VRC07-523, 3BNC117, N6, PGT121, 10-1074, PGDM1400, PG9, 10E8, and 10E8v4-V5R-100cF). For example, the correlation for 3BNC117 had r=0.82 and P<0.0001. Heterogeneity was observed, however, with a lack of significant correlation for 2G12, CAP256.VRC26.25, 2F5, and 4E10. The study also performed paired infected cell binding and ADCC assays by using two reservoir virus isolates in combination with 9 bNAbs, and the results were consistent with previous studies indicating that infected cell binding is moderately predictive of ADCC activity for bNAbs with matched Fc domains. These data provide guidance on the selection of antibodies for clinical trials.
Ren2018
(effector function, neutralization, binding affinity, HIV reservoir/latency/provirus)
-
2F5: The authors review Fc effector functions, which cooperatively with Fab neutralization functions, could be used passively as immunotherapeutic or immunoprophylactic agents of HIV reservoir control or even infection prevention. One effector function, antibody-dependent complement-mediated lysis (ADCML), is seen with IgG1 and IgG3 anti-V1/V2 glycan bnAbs, PG9, PG16, PGT145; but not with 2F5, 4E10, 2G12, VRC01 and 3BNC117 unless they are delivered with anti-regulators of complement activation (RCA) antibodies. Another effector function, antibody-dependent cellular cytotoxicity (ADCC) can slow disease progression by NK-mediated degranulation of infected cells that are coated by bnAbs whose Fc region is recognized by the low affinity NK receptor, FcγRIIIA (or CD16). Strong ADCC was induced by NIH45-46, 3BNC117, 10-1074, PGT121 and 10E8, with intermediate activity for PG16 and VRC01, but no ADCC activation for 12A12, 8ANC195 and 4E10. A final effector function, antibody-dependent phagocytosis (ADP) also eliminates infected cells but through phagocytosis mediated by Fc portions of coating anti-HIV antibodies interacting with other FcγR (or FcαR) on the surface of granulocytes, monocytes or macrophages. This protective mode is less well studied but bnAbs like VRC01 have been engineered to increase phagocytosis by neutrophils. Protein engineering of bispecifics against the surface of infected or reservoir virus cells has potential in the future.
Danesh2020
(antibody interactions, assay or method development, complement, effector function, immunoprophylaxis, neutralization, immunotherapy, early treatment, review, broad neutralizer, HIV reservoir/latency/provirus)
-
2F5: This study assessed cross-reactivity of anti-HIV-1 antibodies with SARS-CoV-2. In binding ELISA and surface binding assays, several nAbs showed significant binding with the RBD and S2P regions of SARS-CoV-2 (VRC07.523LS, N6, NIH45-46G54W, Z13e1, 4E10, 2F5). VRC07.523LS (but not VRC01 or VRC03) cross-reacted with the RBD and S2P of SARS-CoV-2. In a neutralization assay, these nAbs showed weak neutralization of a SARS-CoV-2 pseudovirus. BnAb N6 had the highest potency, with an IC50 of approximately 1.0 μg/ml, but N6 failed to neutralize live SARS-CoV-2 virus. Polyclonal sera from 10 HIV-1-infected children were tested for binding and neutralization; all 10 showed significant binding to both RBD and S2P, and 3 children showed potent and near-complete neutralization of SARS-CoV-2 pseudoviruses (AIIMS329, AIIMS330, AIIMS346). The study suggests that human Abs that tolerate extensive epitope variability can be leveraged to neutralize pathogens with related antigenic profiles.
Mishra2021
(antibody polyreactivity)
-
2F5: In vertically-infected infant AIIMS731, a rare HIV-1 mutation in hypervariable loop 2 (L184F) was studied. In patient sequences, this mutation was present in the majority of clones. A panel of 6 V2 bnAbs (PG9, PG16, PGT145, PGDM1400, CAP256.25, and CH01) was assayed for neutralization of 6 patient viral clones. The AIIMS731 viral variants segregated into 4 neutralization-sensitive and 2 resistant clones; sensitive clones carried 184F, while resistant clones carried the rare 184L mutation. A large panel of bnAbs targeting non-V2 epitopes was used to assess the neutralization of the 6 patient viral variants. The bnAb panel consisted of V3/N332 glycan supersite bnAbs (10-1074, BG18, AIIMS-P01, PGT121, PGT128, and PGT135), CD4bs bnAbs (VRC01, VRC03, VRC07-523LS, N6, 3BNC117, and NIH45-46 G54W), a silent face-targeting bnAb (PG05), fusion peptide and gp120-gp41 interface bnAbs (PGT151, 35O22, and N123-VRC34.01), and MPER bnAbs (10E8, 4E10, and 2F5). All of these bnAbs had similar neutralization efficiencies for all 6 clones, suggesting that the L184F mutation was specific for viral escape from neutralization by V2 apex bnAbs. A panel of non-neutralizing mAbs (V3 loop-targeting non-nAbs 447-52D and 19b, and CD4-induced non-nAbs 17b, A32, 48d, and b6), were also assessed; 2 of the variants (the same 2 susceptible to the V2 bnAbs) showed moderate neutralization by 447-52D, 19b, 17b, and 48d. The structure of ligand-free BG505 SOSIP trimer revealed that the side chain of L184 was outward facing and did not make significant intraprotomeric interactions, but upon mutating L184 to F184, a disruption of the accessible surface between the bulky side chain of F184 on one protomer and R165 on the neighboring protomer was seen. Thus, the L184F mutation resulted in increased susceptibility to neutralization by antibodies known to target the relatively more open conformation of Env on tier 1 viruses, suggesting that the rare L184F mutation allowed Env to sample more open states resembling the CD4-bound conformation where the CCR5 binding site is exposed.
Mishra2020
(neutralization, polyclonal antibodies)
-
2F5: Five novel functional HIV-1/HCV monoclonal cross-reactive antibodies (180, 692, 688, 803, and KP1-8) with diverse epitope specificities were isolated from a chronically HIV-1/HCV co-infected donor, VC10014, and characterized. MAb 2F5 was used as a positive control for binding to strain MN gp41.
Pilewski2023
-
2F5: HIV-1 env genes were sequenced from 16 mother/infant transmitting pairs. Infant transmitted-founder (T/F) and representative maternal non-transmitted Env variants were identified and used to generate pseudoviruses for paired maternal plasma neutralization analysis. Eighteen out of 21 (85%) infant T/F Env pseudoviruses were neutralization resistant to paired maternal plasma, while all infant T/F viruses were neutralization sensitive to a panel of HIV-1 broadly neutralizing antibodies (2G12, CH01, PG9, PG16, PGT121, PGT126, DH429, b12, VRC01, NIH45-46, CH31, 4E10, 2F5, 10E8, DH512) and variably sensitive to heterologous plasma neutralizing antibodies. Antibody mixture CH01/31 was used as a positive control for neutralization. The infant T/F pseudoviruses were overall more neutralization resistant to paired maternal plasma in comparison to pseudoviruses from maternal non-transmitted variants. These findings suggest that autologous neutralization of circulating viruses by maternal plasma antibodies select for neutralization-resistant viruses that initiate peripartum transmission, raising the speculation that enhancement of this response at the end of pregnancy could reduce infant HIV-1 infection risk.
Kumar2018
(neutralization, acute/early infection, mother-to-infant transmission, transmission pair)
-
2F5: Novel Env clones of subtypes G (n=15) and F (n=7) were produced and tested for neutralization and coreceptor usage. All 15 subtype G-enveloped pseudoviruses were resistant to neutralization by MAbs b12 and 2G12, while a majority were neutralized by 2F5 and 4E10. All 7 subtype F pseudoviruses were resistant to 2F5 and b12, 6 were resistant to 2G12, and 6 were neutralized by 4E10. Coreceptor usage testing revealed that 21 of 22 envelopes were CCR5-tropic, including all 15 subtype G envelopes, 7 of which were from patients with CD4 T cell counts <200/ml. TriMab (a mixture of b12 + 2G12 + 2F5) neutralized only four (27%) viruses, and this activity correlated with that of the 2F5 component. These results confirm the broadly neutralizing activity of 4E10 on envelope clones across all tested group M clades, including subtypes G and F, reveal the resistance of most subtype F pseudoviruses to broadly neutralizing MAbs b12, 2G12, and 2F5, and suggest that, similarly to subtype C, CXCR4 tropism is uncommon in subtype G, even at advanced stages of infection.
Revilla2011
(neutralization, subtype comparisons)
-
2F5: Rabbits were immunized with a DNA vaccine encoding JR-CSF gp120. Five sera with potent autologous neutralizing activity were selected and compared with a human neutralizing plasma (Z23) and monoclonal antibodies targeting various regions of gp120 (VRC01, b12, b6, F425, 2F5, 2G12, and X5). The rabbit sera contained different neutralizing activities dependent on C3 and V5, C3 and V4, or V4 regions of the glycan-rich outer domain of gp120. All sera showed enhanced neutralizing activity toward an Env variant that lacked a glycosylation site in V4. The JR-CSF gp120 epitopes recognized by the sera were distinct from those of the mAbs. The activity of one serum required specific glycans that are also important for 2G12 neutralization, and this serum blocked the binding of 2G12 to gp120. The findings show that different fine specificities can achieve potent neutralization of HIV-1, yet this strong activity does not result in improved breadth.
Narayan2013
(neutralization, polyclonal antibodies)
-
2F5: The study identified a primary HIV-1 Env variant from patient 653116 (GenBank MT023027) that consistently supports >300% increased viral infectivity in the presence of autologous or heterologous HIV-positive plasma. In the absence of HIV-positive plasma, viruses with this Env exhibited reduced infectivity that was not due to decreased CD4 binding. This phenotype was mapped to a change Q563R, in the gp41 heptad repeat 1 (HR1) region. The authors provide evidence that Q563R reduces viral infection by disrupting formation of the gp41 six-helix bundle required for virus-cell membrane fusion. Anti-cluster I monoclonal antibodies (240-D, 246-D, F240, T32) targeting HR1 and the C-C loop of gp41 restored infectivity defects observed with Q563R. Viruses with the Q563R mutation were shown to have increased sensitivity to MPER mAbs (10E8, 7H6, 2F5, Z13e1, 4E10).
Joshi2020
(mutation acquisition, viral fitness and/or reversion)
-
2F5: Plasma from donor PG13 was found to have MPER neutralization activity, and mAb PGZL1 was isolated. When compared to a 4E10, PGZL1 was found to share similar crystal structure, contacts, and some common germline genes, but its neutralization and polyreactivity were less strong. The germline gene usage of PGZL1 was compared with other MPER antibodies: 4E10, VRC42.01, 10E8, DH511.2, DH517, Z13, and 2F5.
Zhang2019a
(neutralization, structure, contact residues, germline)
-
2F5: An R5 virus isolated from chronic patient NAB01 (Patient Record# 4723) was adapted in culture to growth in the presence of target cells expressing reduced levels of CD4. Entry kinetics of the virus were altered, and these alterations resulted in extended exposure of CD4-induced neutralization-sensitive epitopes to CD4. Adapted and control viruses were assayed for their neutralization by a panel of neutralizing antibodies targeting several different regions of Env (PGT121, PGT128, 1-79, 447-52d, b6, b12, VRC01, 17b, 4E10, 2F5, Z13e1). Adapted viruses showed greater sensitivity to antibodies targeting the CD4 binding site and the V3 loop. This evolution of Env resulted in increased CD4 affinity but decreased viral fitness, a phenomenon seen also in the immune-privileged CNS, particularly in macrophages.
Beauparlant2017
(neutralization, viral fitness and/or reversion, dynamics, kinetics)
-
2F5: The Chinese HIV Reference Laboratory produced 124 pseudoviruses from patients with subtype B, BC, and CRF01 infections. These viruses were assigned to tiers based on their neutralization by a panel of patient sera. Their neutralization sensitivities were also measured against a panel of well-characterized mAbs (2F5, b12, 2G12, 4E10, 10E8, VRC01, VRC-CH31, CH01, PG9, PG16, PGT121, PGT126).
Nie2020
(assay or method development, neutralization)
-
2F5: Pseudoviruses were produced from 37 Env clones of BC subtypes from chronically-infected patients from several regions of China. Neutralization was tested for mAbs 4E10 and 2F5. Three signature sites were identified in association with sensitivity to neutralization: L22, S29, and N706.
Wang2011b
(neutralization)
-
2F5: This study characterized 3 lineages of MPER-targeting mAbs (VRC42, VRC43 & VRC46) isolated from subject RV217-40512 plasma 646 days after the first HIV RNA+ sample (pRNA+), but detectable by next-generation sequencing (NGS) by day 154 pRNA+ which was prior to superinfection between days 330 & 401 pRNA+. MAb VRC46.01 was most similar to known MPER-targeting bnAb 2F5 in a neutralization fingerprint analysis. In this study, 2F5 neutralized 58% of 208 diverse pseudoviruses with a median IC50 of 2.01 μg/ml against sensitive viruses. 2F5 was able to recognize the clade B, but not the clade C, full MPER epitope and the minimal epitope ALDKWA (near N-terminus MPER, 662-667).
Krebs2019
(antibody binding site, neutralization, broad neutralizer)
-
2F5: Novel Env pseudoviruses were derived from 22 patients in China infected with subtype CRF01_AE viruses. Neutralization IC50 was determined for 11 bNAbs: VRC01, NIH45-46G54W, 3BNC117, PG9, PG16, 2G12, PGT121, 10-1074, 2F5, 4E10, and 10E8. The CRF01_AE pseudoviruses exhibited different susceptibility to these bNAbs. Overall, 4E10, 10E8, and 3BNC117 neutralized all 22 env-pseudotyped viruses, followed by NIH45-46G54W and VRC01, which neutralized more than 90% of the viruses. 2F5, PG9, and PG16 showed only moderate breadth, while the other three bNAbs neutralized none of these pseudoviruses. Specifically, 10E8, NIH45-46G54Wand 3BNC117 showed the highest efficiency, combining neutralization potency and breadth. Mutations at position 160, 169, 171 were associated with resistance to PG9 and PG16, while loss of a potential glycan at position 332 conferred insensitivity to V3-glycan-targeting bNAbs. These results may help in choosing bNAbs that can be used preferentially for prophylactic or therapeutic approaches in China.
Wang2018a
(assay or method development, neutralization, subtype comparisons)
-
2F5: HIV Env glycoproteins were expressed by incorporation into live attenuated rubella viral vectors strain RA27/3. These vectors can stably express Env core derived glycoproteins ranging in size up to 363 amino acids from HIV clade C strain 426c. By themselves, the vectors elicited modest Ab titers to the Env insert. But the combination of rubella/env prime followed by a homologous protein boost gave a strong response. Env 426c antigens were immunoprecipitated and detected by western blot with monoclonal 2F5 specific for an MPER tag present on the constructs.
Virnik2018
(vaccine antigen design)
-
2F5: This study looks at the role of somatic mutations within antibody variable and framework regions (FWR) in bNAbs and how these mutations alter thermostability and neutralization as the Ab lineage reaches maturation. The emergence and selection of different mutations in the complementarity-determining and framework regions are necessary to maintain a balance between antibody function and stability. The study shows that all major classes of bNAbs (DH270, CH103, CH235, VRC01, PGT lineage etc.) have lower thermostability than their corresponding inferred UCA antibodies. Fab interdomain flexibility mutations are selected early in Ab development.
Henderson2019
(neutralization, antibody lineage, broad neutralizer)
-
2F5: The authors used nuclear magnetic resonance (NMR) to define the structure of the HIV-1 MPER when linked to the transmembrane domain (MPER-TMD) in the context of a lipid bilayer. In particular, they looked at the accessibility of the MPER-TMD to 2F5, 4E10, 10E8 and DH570. The MPER appears to be accessible up to ∼10% of the time to the 2F5, 4E10, and 10E8 Fabs but ∼40% of time to the DH570 Fab. To assess possible functional roles for the MPER in membrane fusion, they generated 17 Env mutants using the sequence of a clade A isolate, 92UG037.8, mutating each of the three structural elements: hydrophobic core, turn, and kink. Mutants W670A (hydrophobic core), F673A (turn), and W680A (kink), while still sensitive to VRC01, became much more resistant to the trimer-specific bNAbs and also gained sensitivity to b6, 3791, and 17b. All mutants with changes at W666 in the hydrophobic core and K683 at the kink lost infectivity almost completely. For the rest of the mutants, infectivity ranged from 4.3 to 50.8% of that of the wild type, showing that key residues important for stabilizing the MPER structure are also critical for Env-induced membrane fusion activity, especially in the context of viral infection.
Fu2018
(antibody binding site, antibody interactions, neutralization, variant cross-reactivity, binding affinity, structure)
-
2F5: Isolation of human MPER-targeting mAb, E10, from an HIV-1-infected patient sample by single B cell sorting and single cell PCR has been reported. E10 had lower neutralization activity than mAb b12 but higher ADCC activity than mAb 2F5 at low concentrations. Positive responses to 3 overlapping consensus B clade linear 15mer peptides identified a 2F5-specific epitope core of ELDKWA immediately downstream of the E10 epitope. MAb 2F5 was also used as a positive standard for cardiolipin binding assessing autoreactivity and MPER peptide fusion protein F7-Fc binding.
Yang2018
(antibody binding site, autoantibody or autoimmunity)
-
2F5: Two HIV-1-infected individuals, VC10014 and VC20013, were monitored from early infection until well after they had developed broadly neutralizing activity. The bNAb activity developed about 1 year after infection and mapped to a single epitope in both subjects. Isolates from each subject, taken at five different time points, were tested against monoclonal bNAbs: VRC01, B12, 2G12, PG9, PG16, 4E10, and 2F5. In subject VC10014, the bNAb activity developed around 1 year postinfection and targeted an epitope that overlaps the CD4-BS and is similar to (but distinct from) bNAb HJ16. In the case of VC20013, the bNAb activity targeted a novel epitope in the MPER that is critically dependent on residue 677 (mutation K677N). All of the isolates from VC20013 were sensitive to both 2F5 and 4E10.
Sather2014
(neutralization, broad neutralizer)
-
2F5: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of nAb responses compared with Env 459C alone. The 4 MPER bNAbs studied were grouped by epitope, either 2F5 or 4E10/10E8/DH511. Clade C showed resistance to 2F5 which might be explained by absence of conserved Ala, A667.
Bricault2019
(antibody binding site, neutralization, vaccine antigen design, computational prediction, broad neutralizer)
-
2F5: Improvements to the standardization of the HIV-1 pseudovirus production procedure by implementing an automated system for aliquoting of HIV-1 pseudovirus stocks up to liter-scale are described. The automated platform and the aliquoting process were validated on as accuracy, precision, specificity and robustness. Lot-to-lot variations and virus stock integrity were assessed through two parallel neutralization assays run with the automatically aliquoted HIV pseudovirus and a manually aliquoted reference virus of the same type, by using five control reagents: sCD4, b12, 2F5, 4E10 and TriMab consisting of 2G12, IgG1b12 and 2F5.
Schultz2018
(assay or method development, neutralization)
-
2F5: Polyreactive properties of natural and artificially engineered HIV-1 bNAbs were studied, with almost 60% of the tested HIV-1 bNAbs (including this one) exhibiting low to high polyreactivity in different immunoassays. A previously unappreciated polyreactive binding for PGT121, PGT128, NIH45-46W, m2, and m7 was reported. Binding affinity, thermodynamic, and molecular dynamics analyses revealed that the co-emergence of enhanced neutralizing capacities and polyreactivity was due to an intrinsic conformational flexibility of the antigen-binding sites of bNAbs, allowing a better accommodation of divergent HIV-1 Env variants.
Prigent2018
(antibody polyreactivity)
-
2F5: The authors selected an optimal panel of diverse HIV-1 envelope glycoproteins to represent the antigenic diversity of HIV globally in order to be used as antigen candidates. The selection was based on genetic and geographic diversity, and experimentally and computationally evaluated humoral responses. The eligibility of the envelopes as vaccine candidates was evaluated against a panel of antibodies for breadth, affinity, binding and durability of vaccine-elicited responses. The antigen panel was capable of detecting the spectrum of V2-specific antibodies that target epitopes from the V2 strand C (V2p), the integrin binding motif in V2 (V2i), and the quaternary epitope at the apex of the trimer (V2q).
Yates2018
(vaccine antigen design, vaccine-induced immune responses, binding affinity)
-
2F5: A panel of bnAbs were studied to assess ongoing adaptation of the HIV-1 species to the humoral immunity of the human population. Resistance to neutralization is increasing over time, but concerns only the external glycoprotein gp120, not the MPER, suggesting a high selective pressure on gp120. Almost all the identified major neutralization epitopes of gp120 are affected by this antigenic drift, suggesting that gp120 as a whole has progressively evolved in less than 3 decades.
Bouvin-Pley2014
(neutralization)
-
2F5: Assays of poly- and autoreactivity demonstrated that broadly neutralizing NAbs are significantly more poly- and autoreactive than non-neutralizing NAbs. 2F5 is autoreactive, but not polyreactive.
Liu2015a
(autoantibody or autoimmunity, antibody polyreactivity)
-
2F5: A panel of 14 pseudoviruses of subtype CRF01_AE was developed to assess the neutralization of several neutralizing antibodies (b12, PG9, PG16, 4E10, 10E8, 2F5, PGT121, PGT126, 2G12). Neutralization was assessed in both TZM-bl and A3R5 cell-based assays. Most viruses were more susceptible to mAb-neutralization in A3R5 than in the TZM-bl cell-based assay. The increased neutralization sensitivity observed in the A3R5 assay was not linked to the year of virus transmission or to the stages of infection, but chronic viruses from the years 1990-92 were more sensitive to neutralization than the more current viruses, in both assays.
Chenine2018
(assay or method development, neutralization, subtype comparisons)
-
2F5: The immunologic effects of mutations in the Env cytoplasmic tail (CT) that included increased surface expression were explored using a vaccinia prime/protein boost protocol in mice. After vaccinia primes, CT- modified Envs induced up to 7-fold higher gp120-specific IgG, and after gp120 protein boosts, they elicited up to 16-fold greater Tier-1 HIV-1 neutralizing antibody titers. Envs with or without the TM1 mutations were expressed in HEK 293T cells and analyzed for the relative expression of Ab epitopes including the membrane-proximal external region (MPER) in gp41 for 2F5.
Hogan2018
(vaccine antigen design)
-
2F5: A panel of mAbs (2G12, VRC01, HJ16, 2F5, 4E10, 35O22, PG9, PGT121, PGT126, 10-1074) was tested to compare efficacy in cell-free versus cell-cell transmission environment. Almost all bNAbs (with the exception of anti-CD4 mAb Leu3a) blocked cell-free infection with greater potency than cell-cell infection, and showed greater potency in neutralization of cell-free viruses. The lower effectiveness on neutralization was particularly pronounced for transmitted/founder viruses, and less pronounced for chronic and lab-adapted viruses. The study highlights that the ability of an antibody to inhibit cell-cell transmission may be an important consideration in the development of Abs for prophylaxis.
Li2017
(immunoprophylaxis, neutralization)
-
2F5: The next generation of a computational neutralization fingerprinting (NFP) being used as a way to predict polyclonal Ab responses to HIV infection is presented. A new panel of 20 pseudoviruses, termed f61, was developed to aid in the assessment of experimental neutralization. This panel was used to assess 22 well-characterized bNAbs and mixtures thereof (HJ16, VRC01, 8ANC195, IGg1b12, PGT121, PGT128, PGT135, PG9, PGT151, 35O22, 10E8, 2F5, 4E10, VRC27, VRC-CH31, VRC-PG20, PG04, VRC23, 12A12, 3BNC117, PGT145, CH01). The new algorithms accurately predicted VRC01-like and PG9-like antibody specificities.
Doria-Rose2017
(neutralization, computational prediction)
-
2F5: This review discusses host controls of bNAb responses and why highly antigenic vaccine Envs do not induce bNAbs when used as vaccine immunogens. 2F5 is polyreactive for human host lipids and proteins. It binds to the ELDKWA epitope present in both dp41 and an enzyme of tryptophan metabolism, kynureninase (Kynu). Kl mice expressing VDJ rearrangements of 2F5 exhibit severe defects in B-cell development with 95% of immature bone marrow B cells lost at the first tolerance checkpoint and peripheral B cells anergic similar result is seen for 2F5 unmutated common ancestor (UCA). Mice and macaques vaccination with 2F5 UCA resulted in B cells activated with minimal affinity maturation.
Kelsoe2017
(review, antibody polyreactivity)
-
2F5: This review focuses on the potential role of HIV-1-specific NAbs in preventing HIV-1 infection. Several NAbs have provided protection from infection in SHIV challenge studies in primates: b12, VRC01, VRC07-523LS, 3BNC117, PG9, PGT121, PGT126, 10-1074, 2G12, 4E10, 2F5, 10E8.
Pegu2017
(immunoprophylaxis, review)
-
2F5: The ability of neutralizing and nonneutralizing mAbs to block infection in models of mucosal transmission was tested. Neutralization potency did not fully predict activity in mucosal tissue. CD4bs-specific bNAbs, in particular VRC01, blocked HIV-1 infection across all cellular and tissue models. MPER (2F5) and outer domain glycan (2G12) bNAbs were also efficient in preventing infection of mucosal tissues, while bNAbs targeting V1-V2 glycans (PG9 and PG16) were more variable. Non-nAbs alone and in combinations, were poorly protective against mucosal infection. The protection provided by specific bNAbs demonstrates their potential over that of nonneutralizing antibodies for preventing mucosal entry. 2F5 and 4E10 were selected as representative mAbs of the MPER class.
Cheeseman2017
(genital and mucosal immunity, immunoprophylaxis)
-
2F5: To understand HIV neutralization mediated by the MPER, antibodies and viruses were studied from CAP206, a patient known to produce MPER-targeted neutralizing mAbs. 41 human mAbs were isolated from CAP206 at various timepoints after infection, and 4 macaque mAbs were isolated from animals immunized with CAP206 Env proteins. Two rare, naturally-occuring single-residue changes in Env were identified in transmitted/founder viruses (W680G in CAP206 T/F and Y681D in CH505 T/F) that made the viruses less resistant to neutralization. The results point to the role of the MPER in mediating the closed trimer state, and hence the neutralization resistance of HIV. CH58 was one of several mAbs tested for neutralization of transmitted founder viruses isolated from clade C infected individuals CAP206 and CH505, compared to T/F viruses containing MPER mutations that confer enhanced neutralization sensitivity.
Bradley2016a
(neutralization)
-
2F5: This study investigated the ability of native, membrane-expressed JR-FL Env trimers to elicit NAbs. Rabbits were immunized with virus-like particles (VLPs) expressing trimers (trimer VLP sera) and DNA expressing native Env trimer, followed by a protein boost (DNA trimer sera). N197 glycan- and residue 230- removal conferred sensitivity to Trimer VLP sera and DNA trimer sera respectively, showing for the first time that strain-specific holes in the "glycan fence" can allow the development of tier 2 NAbs to native spikes. All 3 sera neutralized via quaternary epitopes and exploited natural gaps in the glycan defenses of the second conserved region of JR-FL gp120. 2F5 used as a reference Ab.
Crooks2015
(glycosylation, neutralization)
-
2F5: This study assessed the ADCC activity of antibodies of varied binding types, including CD4bs (b6, b12, VRC01, PGV04, 3BNC117), V2 (PG9, PG16), V3 (PGT126, PGT121, 10-1074), oligomannose (2G12), MPER (2F5, 4E10, 10E8), CD4i (17b, X5), C1/C5 (A32, C11), cluster I (240D, F240), and cluster II (98-6, 126-7). ADCC activity was correlated with binding to Env on the surfaces of virus-infected cells. ADCC was correlated with neutralization, but not always for lab-adapted viruses such as HIV-1 NLA-3.
vonBredow2016
(effector function)
-
2F5: This review summarizes representative anti-HIV MAbs of the first generation (2G12, b12, 2F5, 4E10) and second generation (PG9, PG16, PGT145, VRC26.09, PGDM1400, PGT121, PGT124, PGT128, PGT135, 10-1074, VRC01, 3BNC117, CH103, PGT151, 35O22, 8ANC195, 10E8). Structures, epitopes, VDJ usage, CDR usage, and degree of somatic hypermutation are compared among these antibodies. The use of SOSIP trimers as immunogens to elicit B-cell responses is discussed.
Burton2016
(review, structure)
-
2F5: Two stable homogenous gp140 Env trimer spikes, Clade A 92UG037.8 Env and Clade C C97ZA012 Env, were identified. 293T cells stably transfected with either presented fully functional surface timers, 50% of which were uncleaved. A panel of neutralizing and non-neutralizing Abs were tested for binding to the trimers. MPER Ab 2F5 did not bind cell surface whether gp160 was missing C-terminal or not, but did neutralize 92UG037.8 HIV-1 isolate weakly.
Chen2015
(neutralization, binding affinity)
-
2F5: Factors that independently affect bNAb induction and evolution were identified as viral load, length of untreated infection, and viral diversity. Black subjects induced bNAbs more than white subjects, but this did not correlate with type of Ab response. Fingerprint analyses of induced bNAbs showed strong subtype dependency, with subtype B inducing significantly higher levels of CD4bs Abs and non-subtype B inducing V2-glycan specific Abs. Of the 239 bNAb antibody inducers found from 4,484 HIV-1 infected subjects, the top 105 inducers' neutralization fingerprint and epitope specificity was determined by comparison to the following antibodies - PG9, PG16, PGDM1400, PGT145 (V2 glycan); PGT121, PGT128, PGT130 (V3 glycan); VRC01, PGV04 (CD4bs) and PGT151 (interface) and 2F5, 4E10, 10E8 (MPER).
Rusert2016
(neutralization, subtype comparisons, broad neutralizer)
-
2F5: This review discusses the application of bNAbs for HIV treatment and eradication, focusing on bNAbs that target key epitopes, specifically those of: 2G12, 2F5, 4E10, VRC01, 3BNC117, PGT121, VRC26.08, VRC26.09, PGDM1400, and 10-1074. Antibodies 2G12, 2F5, and 4E10 were among the first bNAbs available for clinical testing, and a cocktail of these 3 Abs was assessed in human trials.
Stephenson2016
(immunotherapy, review)
-
2F5: This review discusses the breakthroughs in understanding of the biology of the transmitted virus, the structure and nature of its envelope trimer, vaccine-induced CD8 T cell control in primates, and host control of bnAb elicitation.
Haynes2016
(review)
-
2F5: A mathematical model was developed to predict the Ab concentration at which antibody escape variants outcompete their ancestors, and this concentration was termed the mutant selection window (MSW). The MSW was determined experimentally for 12 pairings of diverse HIV strains against 7 bnAbs (b12, 2G12, PG9, PG16, PGT121, PGT128, 2F5). The neutralization of 2F5 was assayed against JRFL-D664N (resistant strain) and JRFL (sensitive strain).
Magnus2016
(neutralization, escape)
-
2F5: Neutralization breadth in 157 antiretroviral-naive individuals infected for less than 1 year post-infection was studied and compared to a cohort of 170 untreated chronic patients. A range of neutralizing activities was observed with a panel of six recombinant viruses from five different subtypes. Some sera were broadly reactive, predominantly targeting envelope epitopes within the V2 glycan-dependent region. The Env neutralization breadth was positively associated with time post infection. 2F5 has been used as a control in testing CD4 binding site neutralizing specificity of the sera.
Sanchez-Merino2016
(neutralization, acute/early infection)
-
2F5: Ten mAbs were isolated from a vertically-infected infant BF520 at 15 months of age. Ab BF520.1 neutralized pseudoviruses from clades A, B and C with a breadth of 58%, putting it in the same range as second-generation bNAbs derived from adults, but its potency was lower. BF520.1 was shown to target the base of the V3 loop at the N332 supersite. MPER-binding, first-generation mAb, 2F5 when compared had a geometric mean of IC50=6.86 µg/ml for the 6/12 viruses it neutralized at a potency of 50%. The infant-derived antibodies had a lower rate of somatic hypermutation (SHM) and no indels compared to adult-derived anti-V3 mAbs. This study shows that bnAbs can develop without SHM or prolonged affinity maturation.
Simonich2016
(antibody binding site, neutralization, responses in children, structure)
-
2F5: This study examined the neutralization of group N, O, and P primary isolates of HIV-1 by diverse antibodies. Cross-group neutralization was observed only with the bNAbs targeting the N160 glycan-V1/V2 site. Four group O isolates, 1 group N isolate, and the group P isolates were neutralized by PG9 and/or PG16 or PGT145 at low concentrations. None of the non-M primary isolates were neutralized by bNAbs targeting other regions, except 10E8, which weakly neutralized 2 group N isolates, and 35O22 which neutralized 1 group O isolate. Bispecific bNAbs (PG9-iMab and PG16-iMab) very efficiently neutralized all non-M isolates with IC50 below 1 ug/mL, except for 2 group O strains. Anti-MPER bNAb 2F5 was unable to neutralize any of the 16 tested non-M primary isolates at an IC50< 10µg/ml.
Morgand2015
(neutralization, subtype comparisons)
-
2F5: The neutralization of 14 bnAbs was assayed against a global panel of 12 or 17 Env pseudoviruses. From IC50, IC80, IC90, and IC99 values, the slope of the dose-response curve was calculated. Each class of Ab had a fairly consistent slope. Neutralization breadth was strongly correlated with slope. An IIP (Instantaneous Inhibitory Potential) value was calculated, based on both the slope and IC50, and this value may be predictive of clinical efficacy. 2F5, a gp41 MPER bnAb belonged to a group with slopes <1 (like others 10E8 and 4E10), but 10E8 had a significantly lower IC50.
Webb2015
(neutralization)
-
2F5: A gp41 immunogen, gp41-HR1-54Q, was developed, consisting of shortened heptad repeat regions 1 and 2 and the MPER. It was efficiently recognized by 3 MPER-binding Abs (2F5, Z13e1 and 4E10). In rabbits, the antigen was highly immunogenic but failed to develop neutralization ability.
Habte2015
(vaccine antigen design)
-
2F5: HIV gp41 bNAbs have characteristics that predispose them to be controlled by immunological tolerance. The study explored whether the germline unmutated ancestors (UA) of MPER bNAbs are also controlled by tolerance, and, if so, whether any remaining B cells can be activated to clonally expand. Germline knock-in mice expressing precursors of bNAb 2F5 showed B cell deletion in the bone marrow prevaccination, and the anergic bnAb precursors that survived in the periphery could be partially rescued, become activated, and clonally expand by immunization with MPER peptide-liposomes. Immunized macaques made B cell clonal lineages targeted to the 2F5 bnAb epitope, but 2F5-like antibodies were either deleted or did not attain sufficient affinity for gp41-lipid complexes to achieve the neutralization potency of 2F5. Structural analysis of members of a vaccine-induced antibody lineage DH570 revealed that heavy chain complementarity-determining region 3 (HCDR3) hydrophobicity was important for neutralization. 2F5 light chain interacts with the gp41 MPER nominal epitope-containing peptide, gp41660-670.
Zhang2016
(antibody lineage)
-
2F5: A large cross-sectional study of sera from 205 ART-naive patients infected with different HIV clades was tested against a panel of 219 cross-clade Env-pseudotyped viruses. Their neutralization was compared to the neutralization of 10 human bNAbs (10E8, 4E10, VRC01, PG9, PGT145, PGT128, 2F5, CH01, b12, 2G12) tested with a panel of 119 Env-pseudotyped viruses. Results from b12 and 2G12 suggested that these bnAbs may not be as broadly neutralizing as previously thought. 2F5 neutralized 58% of the 199 viruses tested.
Hraber2014
(neutralization)
-
2F5: This study aim to develop a replicating vector system for the delivery of HIV-1 antigens on the basis of an apathogenic foamy virus. This consists of the MPER and the fusion peptide proximal region (FPPR). By stepwise shortening of distinct linker residues between both the domains lead to enhanced recognition by 2F5. This indicates that a specific positioning of FPPR and MPER domains is critical for improved Ab binding.
Muhle2013
-
2F5: The effect of PNGS on viral infectivity and antibody neutralization (2F5, 4E10, b12, VRC01, VRC03, PG9, PG16, 3869) was evaluated through systemic mutations of each PNGS on CRF07_BC strain. Mutations at N197 (C2), N301 (V3), N442 (C4), and N625 (gp41) rendered the virus more susceptible to neutralization by MAbs that recognize the CD4 binding site or gp41. Generally, mutations on V4/V5 loops, C2/C3/C4 regions, and gp41 reduced the neutralization sensitivity to PG16. However, mutation of N289 (C2) made the virus more sensitive to both PG9 and PG16. Mutations at N142 (V1), N355 (C3) and N463 (V5) conferred resistance to neutralization by anti-gp41 MAbs. Available structural information of HIV Env and homology modeling was used to provide a structural basis for the observed biological effects of these mutations.
Wang2013
(neutralization, structure)
-
2F5: Incomplete neutralization may decrease the ability of bnAbs to protect against HIV exposure. In order to determine the extent of non-sigmoidal slopes that plateau at <100% neutralization, a panel of 24 bnMAbs targeting different regions on Env was tested in a quantitative pseudovirus neutralization assay on a panel of 278 viral clones. All bNAbs had some viruses that they neutralized with a plateau <100%, but those targeting the V2 apex and MPER did so more often. All bnMAbs assayed had some viruses for which they had incomplete neutralization and non-sigmoidal neutralization curves. bNAbs were grouped into 3 groups based on their neutralization curves: group 1 antibodies neutralized more than 90% of susceptible viruses to >95% (PGT121-123, PGT125-128, PGT136, PGV04); group 2 was less effective, resulting in neutralization of 60-84% of susceptible viruses to >95% (b12, PGT130-131, PGT135, PGT137, PGT141-143, PGT145, 2G12, PG9); group 3 neutralized only 36-60% of susceptible viruses to >95% (PG16, PGT144, 2F5, 4E10).
McCoy2015
(neutralization)
-
2F5: Autoreactivity and polyspecificity of 2F5 using a synthetic human peptidome has been reported and compared with 4E10. 2F5 was shown to be polyreactive, binding peptides from various proteins, but only in a limited manner. Analysis of B cell development in 2F5 heavy-chain knock-in mice confirmed that 2F5 does recognize self-antigens.
Finton2013
(structure, antibody polyreactivity)
-
2F5: This paper showed that FcγRI occasionally potentiates neutralization by Abs against the V3 loop of gp120 and cluster I of gp41. FcγRI providing a kinetic advantage for neutralizing Abs against partially cryptic epitopes independent of phagocytosis has been reported. The antibiotic bafilomycin A1 and the weak base chloroquine were used as lysosomotropic agents to block phagocytosis in TZM-bl and TZM-bl/FcγRI cells. These treated cells and 2 HIV-1 subtype B Env-pseudotyped viruses (6535.3 and QH0692.42) were assayed with 2F5. Expression of FcγRI dramatically improved the neutralizing activity of 2F5 against both viruses in the absence of lysosomotropic agents. Moreover, neither lysosomotropic agent showed any evidence of reversing the FcγRI-mediated effect on 2F5.
Perez2013
(antibody interactions)
-
2F5: Galactosyl ceramide (Galcer), a glycosphingolipid, is a receptor for the HIV-1 Env glycoprotein. This study has mimicked this interaction by using an artificial membrane containing synthetic Galcer and recombinant HIV-1 Env proteins to identify antibodies that would block the HIV-1 Env-Galcer interaction. HIV-1 ALVAC/AIDSVAX vaccinee-derived MAbs specific for the gp120 C1 region blocked Galcer binding of a transmitted/founder HIV-1 Env gp140. The antibody-dependent cellular cytotoxicity-mediating CH38 IgG and its natural IgA isotype were the most potent blocking antibodies. 2F5 did not block Env-Galcer binding.
Dennison2014
(antibody binding site, antibody interactions, effector function, glycosylation)
-
2F5: Molecular dynamics (MD) simulations of the tridecapeptide corresponding to residues 659–671 of gp41 (covering 2F5 epitope ELDKWA) are reported. X-ray crystallography, nuclear magnetic resonance, and circular dichroism experiments have yielded conflicting conformational information. AMBER force fields technique was used to describe the complex conformational landscape of gp41659–671. In contrast to previous MD simulations, these results are consistent with the bulk of the experimental findings. The amount of helical population is important in aqueous solution, but this structure forms part of a flexible conformational ensemble.
Zhang2014a
(computational prediction, structure)
-
2F5: This review surveyed the Vectored Immuno Prophylaxis (VIP) strategy, which involves passive immunization by viral vector-mediated delivery of genes encoding bnAbs for in vivo expression. Recently published studies in humanized mice and macaques were discussed as well as the pros and cons of VIP towards clinical applications to control HIV endemics. A single injection of AAV8 vector achieved peak 2F5 (˜25 μg/mL) production in serum at week 6 and offered moderate protection.
Yang2014
(immunoprophylaxis, review, antibody gene transfer)
-
2F5: The ability of bNAbs to inhibit the HIV cell entry was tested for b12, VRC01,VRC03, PG9, PG16, PGT121, 2F5, 10E8, 2G12. Among them, PGT121, VRC01, and VRC03 potently inhibited HIV entry into CD4+ T cells of infected individuals whose viremia was suppressed by ART.
Chun2014
(immunotherapy)
-
2F5: Pairwise combinations of 6 NAbs (4E10, 2F5, 2G12, b12, PG9, PG16) were tested for neutralization of pseudoviruses and transmitted/founder viruses. Each of the NAbs tested targets a different region of gp120 or gp41. Some pairwise combinations enhanced neutralization synergistically, suggesting that combinations of NAbs may enhance clinical effectiveness.
Miglietta2014
(neutralization)
-
2F5: The study used computational design to develop a protein that interacted with the CDR H3 loop of 2F5. The protein bound to 2F5 with 10-fold greater affinity than either the full-length epitope peptide on HIV gp41 and any previously-designed epitope-scaffold.
Azoitei2014
(vaccine antigen design)
-
2F5: Cross-group neutralization of HIV-1 isolates from groups M, N, O, and P was tested with diverse patient sera and bNAbs PG9, PG16, 4E10, b12, 2F5, 2G12, VRC01, VRC03, and HJ16. The primary isolates displayed a wide spectrum of sensitivity to neutralization by the human sera, with some cross-group neutralization clearly observed. Among the bNAbs, only PG9 and PG16 showed any cross-group neutralization. The group N prototype strain YBF30 was highly sensitive to neutralization by PG9, and the interaction between their key residues was confirmed by molecular modeling. The conservation of the PG9/PG16 epitope within groups M and N suggests its relevance as a vaccine immunogen.
Braibant2013
(neutralization, variant cross-reactivity)
-
2F5: Tolerance deletion due to mAb autoreactivity limits 2F5 bNAb induction. Autoantigen recognized by 2F5 is kynureninase (KYNU), so that most 2F5-bearing B cells are deleted in the bone marrow and a minor population survives as anergic B cells.
Haynes2013
(review)
-
2F5: This study analyzes the structure and immunogenic properties of MPERp, a peptide vaccine(656NEQELLELDKWASLWN671), that includes the following: (i) the complete sequence protected from proteolysis by the 2F5 paratope; (ii) downstream residues postulated to establish weak contacts with the CDR-H3 loop of 2F5, which are crucial for neutralization; and (iii) an aromatic rich anchor to the membrane interface. MPERp structures confirmed folding of the complete 2F5 epitope within continuous kinked helices. MPER-based peptides in combination with liposomes serves as stand-alone immunogens and suggest new approaches for structure-aided MPER vaccine development.
Serrano2014
(therapeutic vaccine, structure)
-
2F5: 2F5 was one of 10 MAbs used to study chronic vs. consensus vs. transmitted/founder (T/F) gp41 Envs for immunogenicity. Consensus Envs were the most potent eliciters of response but could only neutralize tier 1 and some tier 2 viruses. T/F Envs elicited the greatest breadth of NAb response; and chronic Envs elicited the lowest level and narrowest response. This MPER binding Nab bound well at <10 nM to 3/5 chronic Envs, 5/6 Consensus Envs and 4/7 T/F Envs.
Liao2013c
(antibody interactions, binding affinity)
-
2F5: Avid reaction of 2F5 with a conserved mammalian self-Ag, kynureninase is reported. B cell tetramer reagents were used to track the frequencies of B cells recognizing the HIV-1 2F5 epitope (SP62) in C57BL/6 mice. Reconstitution of Rag1null mice with matured congenic B cells restores the capacity to mount significant serum Ab and germinal center responses to 2F5/SP62. The recovery of humoral responses to the 2F5/SP62 by reconstitution with autoreactive clones of B cells, provides direct evidence towards latent generation of humoral responses in C57BL/6 mice.
Holl2014
-
2F5:This study identified human kynureninase (KYNU) and splicing factor 3b subunit 3 (SF3B3) as the primary conserved, vertebrate self-antigens recognized by the 2F5 and 4E10 antibodies, respectively. 2F5 binds the H4 domain of KYNU which contains the complete 2F5 linear epitope (ELDKWA). 4E10 recognizes an epitope of SF3B3 that is strongly dependent on hydrophobic interactions. Opossums carry a rare KYNU H4 domain that abolishes 2F5 binding, but they retain the SF3B3 4E10 epitope. Immunization of opossums with HIV-1 gp140 induced extraordinary titers of serum antibody to the 2F5 ELDKWA epitope but little or nothing to the 4E10 determinant. Identification of structural motifs shared by vertebrates and HIV-1 provides direct evidence that immunological tolerance can impair humoral responses to HIV-1.
Yang2013
-
2F5: A model that predicts the concentrations at which MAbs 2F5 and 4E10 effectively neutralize HIV-1 is presented. The model predicts that for these antibodies to be effective at neutralization, the time to disable an epitope must be shorter than the time the antibody remains bound in this conformation, about five minutes or less for 4E10 and 2F5. 2F5 IgG, but not 4E10, is much more effective at neutralization than its Fab fragment.
Hu2014
(neutralization)
-
2F5: The effect of low pH and HIV-1 Abs which increased the transcytosis of the virus by 20 fold, has been reported. This enhanced transcytosis was due to the Fc neonatal receptor (FcRn), which facilitates HIV-1's own transmission by usurping Ab responses directed against itself. Both infectious and noninfectious viruses were transcytosed by 2F5. Knocking down FcRn in HEC-1A cells didn't affect transcytosis by 2F5.
Gupta2013
-
2F5: Several anti-HIV-1 broadly neutralizing Abs have unusually long and often protruding CDRH3 loops. This study examined 2F5 mutants with variations in CDRH3. Some variants had improved binding to the MPER region of Env. The CDRH3 tolerated elongations and reductions up to four residues, displaying a range of binding affinities and retaining some neutralizing capacity. The data suggest a mechanism of action in which the 2F5 CDRH3 contacts and destabilizes the MPER helix downstream of its core epitope to allow induction of the extended-loop conformation.
Guenaga2012
(neutralization, structure)
-
2F5: This study examined how the conserved gp120-gp41 association site adapts to glycan changes that are linked to neutralization sensitivity. A DSR mutant virus (K601D) with defective gp120-association, which was sequentially passaged in peripheral blood mononuclear cells to select suppressor mutations was used. Neutralization by 2F5, which targets MPER of gp41, was not affected by V1 mutation as shown against T138N and ΔN.
Drummer2013
(antibody interactions, glycosylation)
-
2F5: Clade A Env sequence, BG505, was identified to bind to bNAbs representative of most of the known NAb classes. This sequence is the best natural sequence match (73%) to the MRCA sequence from 19 Env sequences derived from PG9 and PG16 MAbs' donor. A point mutation at position L111A of BG505 enabled more efficient production of a stable gp120 monomer, preserving the major neutralization epitopes. The antisera produced by this adjuvanted formulation of gp120 competed with bnAbs from 3 classes of non-overlapping epitopes. 2F5 showed high neutralization titer against BG505 pseudovirusin a competitive binding assay as shown in Table 1.
Hoffenberg2013
(antibody interactions, neutralization)
-
2F5: The neutralization profile of 1F7, a human CD4bs mAb, is reported and compared to other bnNAbs. 1F7 exhibited extreme potency against primary HIV-1, but limited breadth across clades. 2F5 neutralized 62% of a cross-clade panel of 157 HIV-1 isolates (Fig. S1) while 1F7 neutralized only 20% of the isolates.
Gach2013
(neutralization)
-
2F5: This study reported Ab binding titers and neutralization of 51 patients with chronic HIV-1 infection on supressive ART for 3 yrs. A high titer of Ab against gp120, gp41, and MPER was found. Patient sera, 2F5 and a serum control were evaluated for binding recombinant gp120JR-FL mutants lacking either the V1/V2 loop or the V3 loop. Significantly higher end point binding titers and HIV1JR-FL neutralization were noticed in patients with >10 compared to <10 yrs of detectable HIV RNA.
Gach2014
(neutralization, HAART, ART)
-
2F5: MHC Class II-restricted TH activation was shown to be a key determinant controlling nonneutralizing MPER Ab responses. The TH H2d epitope KWASLWNWF, that partially overlaps the 2F5 MPER epitope, was required for MPER Ab induction.
Zhang2014
-
2F5: This study reports the development of a new cell-line (A3R5)-based highly sensitive Ab detection assay. This T-lymphoblastoid cell-line stably expreses CCR5 and recognizes CCR5-tropic circulating strains of HIV-1. A3R5 cells showed greater neutralization potency compared to the current cell-line of choice TZM-bl. 2F5 was used as a reference Ab in neutralization assay comparing A3R5 and TZM-bl.
McLinden2013
(assay or method development)
-
2F5: This is a review of identified bNAbs, including the ontogeny of B cells that give rise to these antibodies. Breadth and magnitude of neutralization, unique features and similar bNAbs are listed. 2F5 is an MPER Ab, with breadth 48%, IC50 9.42 μg per ml, and its unique feature listed is ELDKWAS recognition. A similar MAb is m66.
Kwong2013
(review)
-
2F5: Biosynthesis and structure determination by NMR analysis of a micelle-bound MPER trimer, designated gp41-M-MAT, showed that MPER peptides adopt symmetric α helical conformations exposing binding sites. In the 2F5 co-crystal structure, the MPER fragment exhibits a β hairpin at the core 2F5 epitope, but in case of gp41-M-MAT the 2F5 epitope has an α helical conformation. Contact residues F49, W56 and K59 played major roles in conferring binding affinity in the nanomolar range.
Reardon2014
(antibody binding site)
-
2F5: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. m66, m66.6 and 2F5 utilize similar mechanistic elements to recognize a common gp41-MPER epitope and neutralize HIV-1.
Ofek2014
(structure)
-
2F5: 2 HIV-1 infectious molecular clones (IMCs) derived from subtypes C and CRF01_AE HIV-1 primary isolates expressing LucR (IMC.LucR) were engineered to express heterologous gp160 Envs. The IMCs were generally resistant to neutralization by 2F5.
Chenine2013
(assay or method development, neutralization)
-
2F5: Knockin (KI) mice models expressing H chains from MAbs 4E10 and 48d were generated, in addition to previously used KI mice expressing 2F5. Only KI mice expressing MPER+ BnAb HCs triggered a profound early BM developmental blockade, consistent with the self-reactivity of both the 2F5 and 4E10 BnAb HCs being sufficient to trigger clonal B cell deletion.
Chen2013
-
2F5: Env pseudo-typed viruses generated from 7 transmitting and 4 non-transmitting mothers and their children were studied to identify phenotypes that associate with the risk of mother to child transmission. There were no differences in neutralization with 2F5, 2G12, 4E10 and b12, but transmitting mothers had higher autologous NAb responses against gp120/gp41, suggesting that strong autologous neutralization activity can associate with risk of transmission.
Baan2013
(neutralization, mother-to-infant transmission)
-
2F5: A statistical model selection method was used to identify a global panel of 12 reference Env clones among 219 Env-pseudotyped viruses that represent the spectrum of neutralizing activity seen with sera from 205 chronically HIV-1-infected individuals. The small final panel was also highly sensitive for detection of many of the known bNAbs, including 2F5. The panel of 12 Env clones should facilitate assessments of vacine-elicited NAbs.
Decamp2014
(assay or method development)
-
2F5: A computational method to predict Ab epitopes at the residue level, based on structure and neutralization panels of diverse viral strains has been described. This method was evaluated using 19 Env-Ab including 2F5, against 181 diverse HIV-1 strains with available Ab-Ag complex structures.
Chuang2013
(computational prediction)
-
2F5: A panel of NAbs and non-neutralizing Abs (NoNAbs) displaying the highest Fc γR-mediated inhibitory activity and significant ADCC were selected and formulated in a microbicidal gel and tested for antiviral activity against SHIVSF162P3 vaginal challenge in non-human primates. Combination of 2G12, 2F5 and 4E10 fully prevented vaginal transmission. Two NoNAbs, 246-D and 4B3, had no impact on viral acquisition, but reduced plasma viral load.
Moog2014
(effector function, SIV)
-
2F5: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 2F5 is discussed as the MPER region-targeting, potent and broadly neutralizing anti-gp41 mAb exhibiting ADCC activity that has a linear epitope. It is hypothesized that 2F5 blockable neutralizing Ab responses are delayed due to immune dysregulation.
Pollara2013
(effector function, review)
-
2F5: "Neutralization fingerprints" for 30 neutralizing antibodies were determined using a panel of 34 diverse HIV-1 strains. 10 antibody clusters were defined: VRC01-like, PG9-like, PGT128-like, 2F5-like, 10E8-like and separate clusters for b12, CD4, 2G12, HJ16, 8ANC195.
Georgiev2013
(neutralization)
-
2F5: This paper reported the nature of junk Env glycan that undermine the development of Ab responses against gp120/gp41 trimers and evaluated enzyme digestion as a way to remove aberrant Env to produce "trimer VLPs". 2F5 was used in the anti-gp41 Ab cocktail in SDS-PAGE and western blot experiments to prove that enzymes removed junk Env from VLPs and inactivated virus.
Crooks2011
(glycosylation)
-
2F5: Generation of a series of chemically modified MPER immunogens through derivatization of amino acid side chains and evaluation of the binding affinity to their cognate mAbs are described. The modification of peptides has little effect on binding to the antibodies. A selected immunogen containing both 2F5 and 4E10 epitopes and a threonine at T676 elicited the highest anti-peptide IgG titer but not high neutralization. 2F5 has been used as a bnAb directed to MPER.
Venditto2013
(antibody interactions, vaccine antigen design, binding affinity)
-
2F5: The sera of 20 HIV-1 patients were screened for ADCC in a novel assay measuring granzyme B (GrB) and T cell elimination and reported that complex sera mediated greater levels of ADCC than anti-HIV mAbs. The data suggested that total amount of IgG bound is an important determinant of robust ADCC which improves the vaccine potency. 2F5 was used as an anti-gp41 Ab to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets.
Smalls-Mantey2012
(assay or method development, effector function)
-
2F5: Immunogenicity of gp120 immunogens from two pairs of clade B and two pairs of clade C mother-to-child transmitted HIV-1 variants was studied in rabbits. While high level Env-specific antibody responses were elicited by all immunogens, their abilities to NAb responses differed and neutralization-resistant variants elicited broader NAb. All 4 C-lade immunogens had K to S substitution in the critical recognition determinant DKW, which is associated with resistance to 2F5 neutralization.
Wang2012
(mother-to-infant transmission)
-
2F5: This study shows that maize-derived HIV-neutralizing mAb 2F5 is assembled correctly in plants and binds to its antigen with the same affinity as 2F5 produced in mammalian cells. However, although 2F5 has been produced at high levels in non-plant platforms, the yield in maize seeds is lower than previously achieved with 2G12. This suggests that the intrinsic properties of the antibody (e.g. sensitivity to specific proteases) and the environment provided by the production host (e.g. the relative abundance of different proteases, potential transgene silencing) may limit the accumulation of some antibodies.
Sabalza2012
-
2F5: This work provides a proof-of-principle for the retention of an immunogenic MPER/conserved amino-terminalfusion peptide (FP) complex at the surface of lipid vesicles. These MPER:FP peptide-vesicle formulations could be specifically bound by the 2F5 antibody and could trigger cross-reactive anti-MPER antibodies in rabbits, suggesting that contacts with N-terminal regions of gp41 may stabilize the 2F5 epitope as a membrane-surface antigen.
Huarte2012
(structure)
-
2F5: A computational tool (Antibody Database) identifying Env residues affecting antibody activity was developed. As input, the tool incorporates antibody neutralization data from large published pseudovirus panels, corresponding viral sequence data and available structural information. The model consists of a set of rules that provide an estimated IC,50 based on Env sequence data. Important residues are found by minimizing the difference between logarithms of actual and estimated IC50. The program was validated by analysis of MAb 8ANC195, which had unknown specificity. Predicted critical N-glycosylation for 8ANC195 was confirmed in vitro and in humanized mice. The key associated residues for each MAb are summarized in the Table 1 of the paper and also in the Neutralizing Antibody Contexts & Features tool at Los Alamos Immunology Database.
West2013
(glycosylation, computational prediction)
-
2F5: Identification of broadly neutralizing antibodies, their epitopes on the HIV-1 spike, the molecular basis for their remarkable breadth, and the B cell ontogenies of their generation and maturation are reviewed. Ontogeny and structure-based classification is presented, based on MAb binding site, type (structural mode of recognition), class (related ontogenies in separate donors) and family (clonal lineage). This MAb's classification: gp41 MPER, ELDKWAS loop, 2F5 class, 2F5 family.
Kwong2012
(review, structure, broad neutralizer)
-
2F5: This review discusses the new research developments in bnAbs for HIV-1, Influenza, HCV. Models of the HIV-1 Env spike and of Influenza visrus spike with select bnAbs bound are shown.
Burton2012
(review)
-
2F5: Different adjuvants, including Freund's adjuvant (FCA/FIA), MF59, Carbopol-971P and 974P were compared on their ability to elicit antibody responses in rabbits. Combination of Carbopol-971P and MF59 induced potent adjuvant activity with significantly higher titer nAbs than FCA/FIA. There was no difference in binding of this MAb to gp140 SF162 with FIA adjuvant, but there was 3-fold decrease of antigenicity with MF59, C971, C974, C971+MF59 C971+MF59 as compared to the unadjuvanted sample.
Lai2012
(adjuvant comparison)
-
2F5: Somatic hypermutations are preferably found in CDR loops, which alter the Ab combining sites, but not the overall structure of the variable domain. FWR of CDR are usually resistant to and less tolerant of mutations. This study reports that most bnAbs require somatic mutations in the FWRs which provide flexibility, increasing Ab breadth and potency. To determine the consequence of FWR mutations the framework residues were reverted to the Ab's germline counterpart (FWR-GL) and binding and neutralizing properties were then evaluated. 2F5, an MPER Ab, was among the 17 bnAbs which were used in studying the mutations in FWR. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 2F5.
Klein2013
(neutralization, structure, antibody lineage)
-
2F5: Antigenic properties of 2 biochemically stable and homogeneous gp140 trimers (A clade 92UG037 and C clade CZA97012) were compared with the corresponding gp120 monomers derived from the same percursor sequences. The trimers had nearly all the antigenic properties expected for native viral spikes and were markedly different from monomeric gp120. 2F5 has been referred as NAb against MPER.
Kovacs2012
(antibody binding site, neutralization, binding affinity)
-
2F5: Crystal structure and mechanistic analysis of 2F5-gp41 complex is reported. The structures revealed an extended gp41 conformation that made contacts with 5 CDR of 2F5. Studies with protoliposome confirms the importance of lipid membrane and hydrophobic context in the binding of 2F5 to gp41.
Ofek2004
(antibody interactions, structure)
-
2F5: Intrinsic reactivity of HIV-1, a new property regulating the level of both entry and sensitivity to Abs has been reported. This activity dictates the level of responsiveness of Env protein to co-receptor, CD4 engagement and Abs. 2F5 was discussed in relation to H66N and S375W gp120 changes that didn't affect 2F5 binding.
Haim2011
(antibody interactions)
-
2F5: The goal of this study was to improve the humoral response to HIV-1 by targeting trimeric Env gp140 to B cells. The gp140 was fused to a proliferation-inducing ligand (APRIL), B cell activation factor (BAFF) and CD40 ligand (CD40L). These fusion proteins increased the expression of activation-induced-cytidine deaminase (AID) responsible for somatic hypermutation, Ab affinity maturation, and Ab class switching. The Env-APRIL induced high anti-Env responses against tier1 viruses.2F5 was used in BN-PAGE trimer shift assay and immunoprecipitation assay.
Melchers2012
(neutralization)
-
2F5: This paper describes immune-correlates analysis of an HIV-1 vaccine efficiency trial. In the RV144 trial the estimated efficacy was 31.2%. In this study a case-control analysis to identify Ab and cellular immune correlates of infection risk. Out of 17 Abs 6 were chosen for primary analysis to determine the roles of T cell, IgG Ab, IgA Ab responses. Assays were performed on 41 infected vaccinees and 205 uninfected vaccinees. 2F5 was used as a control in the HIV1 binding antibody multiplex assay.
Haynes2012a
(therapeutic vaccine, vaccine-induced immune responses)
-
2F5: Existing structural and sequence data was analyzed. A set of signature features for potent VRC01-like (PVL) and almost PVL abs was proposed and verified by mutagenesis. 2F5 has been referred in discussing the breadth and potency of antiCD4 abs.
West2012a
(antibody lineage)
-
2F5: Synthesis of an engineered soluble heterotrimeric gp140 is described. These gp140 protomers were designed against clade A and clade B viruses. The heterotrimer gp140s exhibited broader anti-tier1 isolate neutralizing antibody responses than homotrimer gp140. 2F5 and 4E10 bound similarly to the homotrimeric clade A and B Q168/SF162L, Q259/SF162NL and Q461/SF1621 heretotrimers and the corresponding homotrimers.
Sellhorn2012
(vaccine antigen design)
-
2F5: This paper showed that nAb 2G12, which binds to gp120 N glycans with α (1,2)-linked mannose termini and inhibits replication after passive transfer to patients, neutralizes by slowing entry of adsorbed virus. It is suggested that 2G12 competitively inhibits interactions between gp120 V3 loop and the tyrosine sulfate containing amino terminus, thus reducing assembly of complexes that catalyze entry. 2F5 was used as a control.
Platt2012
(antibody interactions, glycosylation)
-
2F5: This study shows that epitope mapping of plasma antibodies followed by the rational design of MPER peptide tetramer can successfully isolate antigen-reactive single B cells for Ig rescue. CAP206 was isolated from a South African individual infected with HIV-1 subtype C. Comparison of IC50 suggested that CAP206-CH12 is more cross-reactive than 2F5, which generally fails to neutralize subtype c viruses.
Morris2011
-
2F5: The use of computationally derived B cell clonal lineages as templates for HIV-1 immunogen design is discussed. 2F5 has been discussed in terms of immunogenic and functional characteristics of representative HIV-1 BnAbs and their reactions to antigens.
Haynes2012
(antibody interactions, memory cells, vaccine antigen design, review, antibody polyreactivity, broad neutralizer)
-
2F5: Role of CH1 heavy chain of 2F5 in Ag binding was reported. 2F5IgA2 containing CH1 was constructed and compared for binding affinity and functional activities. 2F5 IgA2 and IgG1 acted synergistically to fully block HIV-1 transfer to CD4+ cells and IgA2 more efficiently bound to gp41 MPER and blocked HIV-1 transcytosis than IgG1. The authors concluded that CH1 region of 2F5 contributed to shape its epitope specificity, binding and functional activities.
Tudor2012
(neutralization, binding affinity, antibody sequence)
-
2F5: Polyclonal B cell responses to conserved neutralization epitopes are reported. Cross-reactive plasma samples were identified and evaluated from 308 subjects tested. 2F5 was used as a control mAb in the comprehensive set of assays performed.
Tomaras2011
(neutralization, polyclonal antibodies)
-
2F5: Role of envelope deglycosylation in enhancing antigenicity of HIV-1 gp41 epitopes is reported. The mechanism of induction of broad neutralizing Abs is discussed. The hypothesis of presence of "holes" in the naive B cell repertoires for unmutated B cell receptor against HIV-1 Env was tested. Native deglycosylated clade B JFRL gp140 and group M consensus gp140 Env CON-S increased 2F5 reactivity, whereas fully glycosylated gp140 env didn't bind. Enhanced immunogenicity of 2F5 MPER epitope on deglycosylated JFRL in rhesus macaques was reported. The authors inferred that glycan interferences control the binding of unmutated ancestor Abs of broad neutralizing mAb to Env gp41.
Ma2011
(glycosylation, neutralization)
-
2F5:The rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1 is discussed in relation to understanding of vaccine recognition sites, the structural basis of interaction with HIV-1 env and vaccine developmental pathways. 2F5 has been discussed regarding the sites of HIV-1 vulnerability to neutralizing antibodies and particularly recognition of highly conserved MPER region of Env.
Kwong2011
(antibody binding site, neutralization, vaccine antigen design, review)
-
2F5: Several antibodies including 10-1074 were isolated from B-cell clone encoding PGT121, from a clade A-infected African donor using YU-2 gp140 trimers as bait. These antibodies were segregated into PGT121-like (PGT121-123 and 9 members) and 10-1074-like (20 members) groups distinguished by sequence, binding affinity, carbohydrate recognition, neutralizing activity, the V3 loop binding and the role of glycans in epitope formation. 2F5 was used as a control in virus neutralization assay. Detail information on the binding and neutralization assays are described in the figures S2-S11.
Mouquet2012a
(glycosylation, neutralization, binding affinity)
-
2F5: A panel of glycan deletion mutants was created by point mutation into HIV gp160, showing that glycans are important targets on HIV-1 glycoproteins for broad neutralizing responses in vivo. Enrichment of high mannose N-linked glycan(HM-glycan) of HIV-1 glycoprotein enhanced neutralizing activity of sera from 8/9 patients. 2F5 was used as a control to compare the neutralizing activity of patients' sera.
Lavine2012
(neutralization)
-
2F5: Ab-driven escape and Ab role in infection control and prevention are reviewed. Main focus is on NAbs, but Ab acting through effector mechanisms are also discussed. 2F5 (amino-terminal MPER) is discussed in the context of developing broadly cross-neutralizing antibodies.
Overbaugh2012
(escape, review)
-
2F5: Neutralization activity was compared against MAb 10E8 and other broad and potent neutralizers in a 181-isolate Env-pseudovirus panel. 2F5 neutralized 57% of viruses at IC50<50 μg/ml and 16% of viruses at IC50<1 μg/ml, compared with 98% and 72% of MAb 10E8, respectively.
Huang2012a
(neutralization)
-
2F5: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared. Among all the MAb tested, 2F5 is an exception to exhibit weak binding to digested uncleaved VLPs and even to bald VLPs, perhaps due to lipid cross-reactivity. Binding to E168K+ N189A WT VLPs was merely a trend of better antibody binding compared to the parent WT VLPs. There was no significant correlation between E168K+N189A WT VLP binding and 2F5 neutralization.
Tong2012
(neutralization, binding affinity)
-
2F5: Prior to this study, no one has been able to elicit potent and broad neutralizing antibodies, like 2F5 or 4E10, targeting the gp41 MPER region. To address this problem, a recombinant immunogen, designated NCM, consisting of the N- and C-terminal heptad repeats that can form a six-helix bundle (6HB) and the MPER region of gp41 was constructed and expressed. Two mutations (T569A and I675V) previously reported to expose the neutralization epitopes were introduced. NCM and its mutants could react with MAbs NC-1, 2F5, 4E10 specific for 6HB and MPER of gp41, suggesting that these antigens are in the form of a trimer of heterodimer (i.e., 6HB) with three exposed MPER tails. Antigen with double mutations elicited strong antibody response in rabbits and these antibodies exhibited broad and potent neutralizing activity.
Wang2011a
(vaccine antigen design)
-
2F5: The ability of several broadly neutralizing antibodies that bind gp10 or gp41 to inhibit cell-cell fusion between Clone69TRevEnv cells induced to express the viral envelope proteins, gp120/gp41 and highly CD4-positive SupT1 cells was investigated. Little or no inhibitory effect on cell-cell fusion was observed. MAbs b12, m14 IgG and 2G12 had moderate inhibitory activity; MAbs 4E10 and 2F5 had no inhibitory activity.
Yee2011
(antibody interactions)
-
2F5: To determine how B cells expressing the original 2F5 MAb are limited by tolerance mechanisms in vivo and if they can be rescued from such controls while retaining neutralization potential, a novel mouse strain for which B cells have the potential to express the original 2F5 VH/VL pair was generated: the 2F5 complete knock in (KI) mouse. While essentially no arrest in B cell development was observed in the 2F5 VL KI strain, the BM B cell developmental arrest observed in the 2F5 VH KI strain was dramatically accentuated in 2F5 complete KI mice. It was shown also that surface Ig BM B cells bearing 2F5 VH/VL pairs can be rescued from tolerance control in vitro, with the majority being developmentally arrested at the immature B cell stage, and express nonneutralizing Igs due to loss of MPER specificity via replacement of their 2F5 LCs.
Verkoczy2011
-
2F5: The role of V1V2 in the resistance of HIV-1 to neutralizing Abs was studied using a panel of neutralization-sensitive and -resistant HIV-1 variants and through exchanging regions of Env between neutralization-sensitive and -resistant viruses. An increase in the length of the V1V2 loop and/or the number of potential N-linked glycosylation sites (PNGS) in that same region of Env was directly involved in the neutralization resistance. The virus that was sensitive to neutralization by autologous serum was also sensitive to neutralization by MAbs b12, 2G12, 2F5, and 4E10, while the virus that was resistant to neutralization by autologous serum was also resistant to neutralization by all of these antibodies except MAb 2G12.
vanGils2011
(glycosylation, neutralization, escape)
-
2F5: To improve the immunogenicity of HIV-1 Env vaccines, a chimeric gp140 trimer in which V1V2 region was replaced by the GM-CSF cytokine was constructed. We selected GM-CSF was selected because of its defined adjuvant activity. Chimeric EnvGM-CSF protein enhanced Env-specific Ab and T cell responses in mice compared with wild-type Env. Probing with neutralizing antibodies showed that both the Env and GM-CSF components of the chimeric protein were folded correctly. 3 proteins were studied: Env-wild-type, Env-ΔV1V2, Env-hGM-CSF. MAb 2F5, directed to the gp41 epitope located far from the GM-CSF insertion, bound identically to the three proteins.
vanMontfort2011
(vaccine antigen design)
-
2F5: Antibody-dependent cellular cytotoxicity (ADCC) potential of 2F5 was studied in vitro. 2F5 triggered ADCC of HIV-1 envelope subunit coated cells. 2F5 at ng/ml concentration elicited ADCC of both X4-tropic HIV-1 envelope-expressing cells, and R5-HIV-infected cells. ADCC relied on binding to the FcγRI on effector cell and was abolished by preincubation of 2F5 with its cognate epitope ELDKWA.
Tudor2011
(effector function)
-
2F5: A standardized proficiency testing program for measurements of HIV-1-specific NAbs in the TZM-bl assay was developed. Three rounds of optimization involving 21 different test laboratories were required to design the final proficiency testing kit. MAbs b12, 2G12, 2F5, 4E10 and TriMab (b12+2G12+2F5) were used for testing.
Todd2012
(assay or method development)
-
2F5: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors.
Peressin2011
(genital and mucosal immunity, dendritic cells)
-
2F5: The reactivity profiles of MAbs 4E10, 2F5 and 2G12 to those of four pathogenic autoAbs derived from patients with antiphospholipid-syndrome (APS), and to serum from a patient with systemic lupus erythematosus (SLE) were compared using an autoantigen microarray comprising 106 connective tissue disease-related autoantigens. The reactivity profiles of bNt anti-HIV-1 MAbs were distinct from those of pathogenic autoAbs. Anti-HIV-1 MAb reactivity was limited mainly to HIV-1-related antigens. The APS autoAbs reacted strongly with cardiolipin (CL), yet only 4E10 bound CL at high concentrations; both 2F5 and 4E10 bound their HIV-1 epitopes with a 2-3-log higher apparent affinity than CL.
Singh2011
(antibody polyreactivity)
-
2F5: Small sized CD4 mimetics (miniCD4s) were engineered. These miniCD4s by themselves are poorly immunogenic and do not induce anti-CD4 antibodies. Stable covalent complexes between miniCD4s and gp120 and gp140 were generated through a site-directed coupling reaction. These complexes were recognized by CD4i antibodies as well as by the HIV co-receptor CCR5 and elicited CD4i antibody responses in rabbits. A panel of MAbs of defined epitope specificities, was used to analyze the antigenic integrity of the covalent complexes using capture ELISA. There was a slight increase in binding for the 2F5 MAb on the complex compared to gp140 alone.
Martin2011
(mimics, binding affinity)
-
2F5: Sensitivity to neutralization was studied in 107 full-length Env molecular clones from multiple risk groups in various locations in China. Neutralization sensitivity to plasma pools and bNAbs was not correlated. MAbs 2F5 and G12 failed to neutralize almost all viruses in the C/07/08/B'C subtype group. 2F5 was potent in neutralizing viruses in subtype B′ and CRF01_AE, while 2G12, could only neutralize a 6/9 of subtype B′ viruses and none of the CRF01_AE viruses. All 2F5-resistant viruses had K665S substitution.
Shang2011
(glycosylation, neutralization, subtype comparisons)
-
2F5: The long-term effect of broadly bNAbs on cell-free HIV particles and their capacity to irreversibly inactivate virus was studied. MPER-specific MAbs potently induced gp120 shedding upon prolonged contact with the virus, rendering neutralization irreversible. The kinetic and thermodynamic requirements of the shedding process were virtually identical to those of neutralization, identifying gp120 shedding as a key process associated with HIV neutralization by MPER bNAbs. Neutralizing and shedding capacity of 7 MPER-, CD4bs- and V3 loop-directed MAbs were assessed against 14 divergent strains. 2F5 induced potent shedding in 11/14 probed viruses.
Ruprecht2011
(neutralization, kinetics)
-
2F5: Unusually wide antigenic specificity of MAb 2F5 was explored. It was shown that when MAb 2F5 screens a pIII-type phage display 7-mer constrained peptide library for its epitope mimics, it demands an epitope sequence longer than DKW and does not tolerate substitutions in the epitope amino acid sequence. The 2F5 paratope flexibility was restricted and even inhibited when the epitope was presented to the paratope in the context of a 7-mer constrained peptide at either the amino-terminal (N-CDKWAxxxC-C) or carboxy-terminal (N-CxxLDKWAC-C) ends. Despite ample presence in the 7-mer constrained library of epitope amino acid substitution versions and peptides with a DKW and DRW core, these peptides were discarded by the antibody.
Palacios-Rodriguez2011
(antibody binding site)
-
2F5: Anti-MPER MAbs 4E10, 2F5 and Z13e1 were probed for binding to HIV-1 and SIV virions with protein A-conjugated gold (PAG) nanoparticles using negative-stain electron microscopy. The MAbs moderately associated with virions, including those devoid of MPER epitopes, and this interaction was strong enough to resist washout. MPER epitope-bearing virions liganded with CD4 showed a much higher association of anti-MPER antibodies compared to the unliganded virions. The results are consistent with a two-stage binding model where these anti-MPER MAbs bind first to the viral lipid bilayer and then to the MPER epitopes following spontaneous or induced exposure.
Rathinakumar2012
(binding affinity)
-
2F5: MPER antigenicity was analyzed in the context of the plasma membrane and a role for the gp41 transmembrane domain (TM) in exposing the epitopes of three bNt MAbs (2F5, 4E10, and Z13e1) was identified. Critical binding residues for the three Nt MAbs were identified using a panel of 24 MPER-TM1 mutants bearing single amino acid substitutions in the MPER; many were previously shown to affect MAb-mediated viral neutralization. Non-Nt mutants of MAbs 2F5 and 4E10 exhibited a reduction in binding to MPER-TM1 and yet maintained binding to synthetic MPER peptides, indicating that MPER-TM1 better approximates the MPER neutralization-competent structure (NCS) than peptides. Replacement of the gp41 TM and CT of MPER-TM1 with the platelet-derived growth factor receptor (PDGFR) TM reduced binding by MAb 4E10, but not 2F5, indicating that the gp41 TM plays a pivotal role in orienting the 4E10 epitope, and more globally, in affecting MPER exposure.
Montero2012
(antibody binding site)
-
2F5: A novel function for lentiviral Nef is reported: it renders the HIV-1 virion refractory to the broadly-neutralizing antibodies 2F5 and 4E10. Nef conferred 50-fold resistance to 2F5 and 4E10, but had no effect on HIV-1 neutralization by MPER-specific NAb Z13e1, by the peptide inhibitor T20, nor by a panel of nAbs and other reagents targeting gp120. Given the membrane-dependence of MPER-recognition by 2F5 and 4E10, in contrast to the membrane-independence of Z13e1, it is suggested that Nef alters MPER recognition in the context of the virion membrane.
Lai2011
(neutralization)
-
2F5: Anti-idiotypic Ab Ab2/3H6, directed against 2F5, was studied as a candidate for an HIV-1 vaccine, based on the induction of 2F5-like Abs.
Kunert2011
(anti-idiotype, vaccine antigen design)
-
2F5: A screening platform was developed that chemically mimics viral and host membrane lipids and replicated NAb membrane interactions. The assay is based on a surface plasmon resonance (SPR) spectroscopy and monitors antibody binding to thiol self-assembled monolayers (SAMs). By simply mimicking lipid chemistry, these thiol SAMs allowed to isolate and distinguish chemical groups that could potentially contribute to specific antibody–lipid interactions. Only 2F5 and 4E10 bound strongly to hydrophobic thiols, correlated with findings that suggest that 2F5 and 4E10 embed into the hydrophobic membrane core. This translates to vaccine design by suggesting that immunogens designed to elicit 2F5/4E10-like antibodies may require an accessible hydrophobic component available for B-cell receptor recognition.
Hardy2012
(assay or method development)
-
2F5: Epitope scaffolds (ES) prime:boosting was assessed by measuring epitope specific serum antibody titers by ELISA and B cell responses by ELISpot analysis using both free 2F5 peptide and an unrelated ES protein as probes. The heterologous ES prime:boosting immunization regimen elicited cross-reactive humoral responses to the structurally constrained 2F5 epitope target (EQELLELDKWASLW). Incorporating a promiscuous T cell helper epitope in the immunogens resulted in higher antibody titers against the 2F5 graft, but did not result in virus neutralization. Two epitope scaffolds (ES1 and ES2), which did not elicit a detectable 2F5 epitope-specific response on their own, boosted such responses when primed with the ES5.
Guenaga2011
(vaccine antigen design)
-
2F5: 2F5 and 4E10 molecular interactions with epitope cores in MPER and lipid bilayers were studied using combined atomic force and confocal microscopies. Both mAbs form lipid-segregated aggregates on supported lipid bilayers (SLBs) and do not induce other significant membrane perturbations. Furthermore, the affinity of MPER toward membranes is differently affected by both mAbs and correlates with the mAbs-epitope core lipid interactions. 2F5 is able to dock the MPER peptide on the membrane, whereas 4E10 extracts the MPER from the lipid bilayer.
Franquelim2011
(antibody binding site)
-
2F5: Study demonstrated that polyreactivity is common among human gp41 cluster II (98-6, 167-D and 126-6)but not cluster I (240D, 246D, 50-69D) antibodies. However, unlike 2F5, cluster II MAbs bind strongly to oligomeric forms of Env gp140 but not to gp41 peptide complexes, suggesting that polyreactivity is necessary but not sufficient for neutralization.
Dennison2011a
(antibody polyreactivity)
-
2F5: The study reports membrane bound forms of gp41 MPER peptides that can present epitopes in a conformation that induce serum antibodies that not only target the core 664DKW epitope of the neutralizing antibody 2F5, but also recognize a fusion intermediate construct of HIV-1 gp41 MPER as well as the 2F5 bound MPER conformation.
Dennison2011
(antibody binding site, polyclonal antibodies)
-
2F5: The sensitivity to PG9 and PG16 of pseudotyped viruses was analysed carrying envelope glycoproteins from the viral quasispecies of three HIV-1 clade CRF01_AE-infected patients. It was confirmed that an acidic residue or a basic residue at position 168 in the V2 loop is a key element determining the sensitivity to PG9 and PG16. In addition, evidence is provided of the involvement of a conserved residue at position 215 of the C2 region in the PG9/PG16 epitopes. Both wild-type and mutated clones of each subtype were found to be highly sensitive to 2F5. A trend towards a higher resistance of mutated clones compared to wild-type clones was nevertheless observed for 0377-I1, 0978-M1 and 1021-I1 CRF01-AE clones. However, the opposite was observed for 5008CL2, 11005CL3 and 11005CL7 clade B clones with a trend towards a higher sensitivity of the mutated counterparts. Collectively, comparing 2F5/4E10 IC50 toward wild-type or mutated clones did not reveal any significant difference.
Thenin2012a
(neutralization)
-
2F5: Given the potential importance of cell-associated virus during mucosal HIV-1 transmission, sensitivity of bNAbs targeting HIV-1 envelope surface unit gp120 (VRCO1, PG16, b12, and 2G12) and transmembrane domain gp41 (4E10 and 2F5) was examined for both cell-free and mDC-mediated infections of TZM-bl and CD4+ T cells. It was reported that higher gp120-bNAb concentrations, but not gp41-directed bNAb concentrations, are required to inhibit mDC-mediated virus spread, compared with cell-free transmission. Blocking the FcRs expressed on mDCs prior to antibody exposure had negligible impact on the ability of 2F5 to inhibit mDC-mediated trans-infection 4E10 and 2F5 bound a significantly greater percentage of mDCs, compared with b12. All abs bound a significantly greater percentage of mDCs, compared with the secondary antibody alone.
Sagar2012
(neutralization, binding affinity)
-
2F5: A way to produce conformationally intact, deglycosylated soluble, cleaved recombinant Env trimers by inhibition of the synthesis of complex N-glycans during Env production, followed by treatment with glycosidases under conditions that preserve Env trimer integrity is described to facilitate crystallography and immunogenicity studies. Deglycosylation had no apparent difference in the binding of the gp41-MPER directed MAb 2F5.
Depetris2012
(glycosylation, binding affinity)
-
2F5: Sensitivity to bNAbs of primary R5 HIV-1 isolates sequentially obtained before and after AIDS onset was studied. End-stage disease HIV R5 isolates were more sensitive to neutralization by TriMab, an equimolar mix of the IgGb12, 2F5 and 2G12 antibodies, than R5 isolates from the chronic phase. The increased sensitivity correlated with low CD4+ T cell count at time of virus isolation and augmented viral infectivity. Envs from end-stage R5 variants had increased positive surface charge and reduced numbers of potential N-linked glycosylation sites (PNGS).
Borggren2011
(glycosylation, neutralization)
-
2F5: 2 human MAbs m66 and m66.6 were identified from 2F5-like serum of HIV-1-infected patient. These new MAbs mimic 2F5 in terms of their MPER binding profiles and neutralize a subset of the viruses neutralized by 2F5, while being significantly less divergent than 2F5 from their germ line-encoded counterparts (8 amino acid changes for VH and 11 for VL genes respectively, compared to 25 amino acid changes for 2F5). m66.6 had higher neutralizing activity than m66, but weaker than 2F5 in a TZM-bl cell assay.
Zhu2011
(antibody lineage)
-
2F5: To test whether HIV-1 particle maturation alters the conformation of the Env proteins, a sensitive and quantitative imaging-based Ab-binding assay was used to probe the conformations of full-length and cytoplasmic tail (CT) truncated Env proteins on mature and immature HIV-1 particles. Slightly greater binding of MPER-specific MAb 2F5 to immature than mature particles was apparent, but the observed difference was not statistically significant.
Joyner2011
(binding affinity)
-
2F5: Humoral responses to specific, linear gp41 epitopes were that were already known to be the target of broadly neutralizing antibodies were compared in a cohort of sub-Saharan mother-child pairs. TriMab positive-control Abs (2F5, 2G12, and b12) neutralized all viruses tested: the subtype B laboratory strains SF162 (R5-B) and IIIB (X4-B), and the low-sensitivity subtype C strains, primary isolates DU172 and DU156 (both R5-C). The TriMab control inhibited strain DU156 when all neutralization assays were performed on the DU156 HIV isolate (C-R5) with cord blood specimens from EUN babies.
Diomede2012
(neutralization, mother-to-infant transmission, subtype comparisons)
-
2F5: 162 full-length envelope (env) clones were generated from plasma RNA obtained from 5 HIV-1 Clade B infected mother-infant pairs and their V1-V5 genotypes and phylogeny were extensively characterized. No infant or maternal clone was resistant to 2F5.
Kishko2011
(neutralization, mother-to-infant transmission)
-
2F5: Two HCDR2 allelic variants of the VH2-5 inferred unmutated ancestor germ line of the 2F5 bNAb (2F5 UAs) are described and it is showed that both variant putative germ line Abs bound to gp41 peptide and protein antigens and are thus capable of recognizing either linear or conformational gp41 epitopes. However, their binding affinities for the gp41-inter protein are an order of magnitude weaker than those of the mature 2F5 Ab. Neither of the two 2F5 UAs showed neutralization activity against pseudotyped viruses though both UAs show broader specificity than does the mature 2F5 Ab. The two 2F5 UA variants also bound to anionic phospholipid-containing liposomes equally well and gave binding responses higher than those of 2F5 MAb binding.
Alam2011
(neutralization, binding affinity, antibody lineage)
-
2F5: A series of immunogens that contain CTB (cholera toxin B subunit, a potent mucosal adjuvant) and tandem copies of ELDKWA were prepared using epitope vaccine strategy. ELDKWA epitope of neutralizing antibody 2F5 plays a crucial role in transcytosis. These immunogens are represented as CTB-nE (n is the number of ELDKWA epitopes fused to CTB). Binding of 2F5 to CTB-2, 4, 6E revealed that ELDKWA epitopes in these immunogens were exposed and retained their antigenicity. The increasing reactivity with MAb 2F5 in western-blot analysis reflected the increasing epitope numbers or epitope density in a single fusion protein. MF-2F5 (Mouse Fecal 2F5-like Abs) could significantly inhibit transcytosis of cell-free CNE3 with similar inhibition potency in both cell lines, but the inhibition potency of MAb 2F5 MAb 2F5 exhibited greater blocking potency in HT29 monolayer than in HEC-1 monolayer.
Wang2011
(neutralization, binding affinity)
-
2F5: Epitope accessibility of the gp41 neutralizing antibodies, 2F5 and 4E10, is explored either on the functional spike or during receptor-mediated entry and it is determined if these antibodies bind to the static spike on the surface of the HIV-1 or require target cell/receptor engagement to gain access to their MPER binding sites. The neutralization activity of 2F5 against lab-adapted viruses and sensitive and moderately resistant viruses was largely unaffected by relatively rapid antibody-virus washing, suggesting direct interaction with the “static” spike. However, for more neutralization-resistant viruses, the 2F5 could neutralize only under the “no antibody-virus wash” conditions, implying that the MPER epitopes were not accessible prior to receptor engagement.
Chakrabarti2011
(antibody binding site, neutralization)
-
2F5: HIV-1 adaptation to neutralization by MAbs VRC01, PG9, PG16 was studied using HIV-1 variants from historic (1985-1989) and contemporary (2003-2006) seroconverters. 2F5 was included for comparison. 2F5 neutralized 10% of contemporary viruses at IC50 < 1 μ g/ml and 70% at IC50 < 5 μ g/ml. TriMab construct, consisting of MAbs b12, 2F5 and 2G12 in equal concentrations, showed the highest neutralization correlation with 2F5.
Euler2011
(neutralization)
-
2F5: The neutralization potency of PG9, PG16, VRC01 and PGV04 was approximately 10-fold greater than that of MAbs b12, 2G12, 2F5 and 4E10.
Falkowska2012
(neutralization)
-
2F5: The characteristics of HIV-1-specific NAbs were evaluated in 100 breast-fed infants of HIV-1-positive mothers who were HIV-1 negative at birth and they were monitored until age 2. A panel of eight viruses that included variants representative of those in the study region as well as more diverse strains was used to determine the breadth of the infant NAbs. 2F5 had very low neutralization potency for 1 (Q842d16) out of 8 pseudoviruses in the panel, no neutralization potency for 3 (BF535.A1, THRO4156.18 and Du156.12) and high for the rest of them. For maternal variants, 2F5 had low neutralization potency for 5 (MF535.E2, MG505.A2, MJ613.A2, MJ613.C7 and ML274.A1) out of 12 variants and high for the rest of them.
Lynch2011
(neutralization, variant cross-reactivity, mother-to-infant transmission)
-
2F5: HIV-1 subtype C env genes from 19 mother-infant pairs: 10 transmitting in utero (IU) and 9 transmitting intrapartum (IP) were analyzed. A severe genetic bottleneck during transmission was confirmed in all pairs. Compared to the maternal viral population, viruses transmitted IP tended to have shorter variable loops and fewer putative N-linked glycosylation sites than viruses transmitted IU. The pseudotyped viruses displayed some sensitivity to 4E10 and soluble CD4 but were resistant to 2G12, 2F5, and IgG1b12.
Russell2011
(glycosylation, neutralization, mother-to-infant transmission)
-
2F5: The impact of specific changes at distal sites on antibody binding and neutralization was examined on Q461 variants. The changes at position 675 in conjunction with Thr to Ala at position 569 increased the 2F5 neutralization sensitivity by 6-fold compared to viruses with only mutation at position 675. There was detectable but modest neutralization by 2F5 with only T569A change. Weak binding is observed for 2F5 but the change at position 675 results in a modest increase in 2F5 binding.
Lovelace2011
(antibody binding site, neutralization, variant cross-reactivity, binding affinity)
-
2F5: The structure of a short fragment of the human HIV-1 membrane glycoprotein gp41 was examined to resolve conflicting reports on the solution state conformational bias in this membrane proximal domain spanning the epitope for 2F5. Study concluded that gp41 659-671 exhibits conformational plasticity in which competing folding propensities are present and can be influenced by loval microenvironment.
Tulip2010
(antibody binding site, structure)
-
2F5: A monostratified epithelium using HT-29 cells transduced to express CCR5 was constructed to model the transcytosis of HIV-1 across columnar epithelial cells because CCR5-tropic viruses are the dominant viruses transmitted in vivo and are preferentially transcytosed across intestinal epithelial cells in vitro. 2F5 IgG1 was the most potent inhibitor of transcytosis of NL4-3.Balecto among the mAbs tested. IgG1 and dIgA, but not pIgM, 2F5 Abs inhibited HIV-1 transcytosis through the epithelium in a dose-dependent manner. The efficiency with which a panel of viruses transcytose across HT-29 monolayers in the presence of 2F5 Abs was measured to determine whether 2F5 inhibition of HIV-1 transcytosis depended on the HIV-1 strain. Both IgG1 and dIgA 2F5 Abs potently inhibited SF162 and NL4-3.Balecto, R5 viruses. pIgM 2F5 had no inhibitory effect on epithelial cell transcytosis of these viruses. The ability of dIgA and mIgA 2F5 Abs to inhibit cell-free HIV-1 transcytosis was compared. Over a wide range of Ab concentrations, the mIgA 2F5 Abs inhibited NL4-3.Balecto transcytosis significantly more than dIgA 2F5 Abs. Also, compared with dIgA 2F5 anti-HIV-1 Abs, mIgA 2F5 Abs more potently reduced HIV-1 transcytosis across model epithelium. 2F5 isotype Abs, especially mIgA, inhibited HIV-1 transcytosis across rectal epithelium and thus entry into the subepithelial lamina propria.
Shen2010a
(binding affinity)
-
2F5: The development and characterization of a tier 1 R5 SHIV, termed SHIV-1157ipEL is reported. SHIV-1157ipEL is a chimera of the "early", neutralization-sensitive SHIV-1157ip envelope and the "late", neutralization-resistant engineered backbone of SHIV-1157ipd3N4. Molecular modeling revealed a possible mechanism for the increased neutralization resistance of SHIV-1157ipd3N4 Env: V2 loops hindering access to the CD4 binding site, shown experimentally with NAb b12. 2F5 only neutralized SHIV-SF162P4 (clade B) out of the 4 clade C and 2 clade B SHIV strains.
Siddappa2010
(neutralization, vaccine antigen design, subtype comparisons)
-
2F5: A high resolution gp41 structure, termed HR1-54Q was presented consisting of the N-terminal helical heptad repeat (HR1), the C-terminal helical heptad repeat (HR2), and the (membrane-proximal external region) MPER. HR1-54Q bound to 3 broadly neutralizing Abs that target gp41: 2F5, 4E10, Z13e1, as well as 98-6 MAb that recognizes the six-helix bundle. The MPER in HR1-54Q encompasses the complete 2F5 binding epitope and binds tightly to 2F5. HR1-54Q possesses several structural characteristics required for induction of 2F5 including the correct conformation and exposure to solvent that both triggers the immune system and generates Abs that appropriately recognize gp41.
Shi2010
(structure)
-
2F5: This review discusses current understanding of Env neutralization by antibodies in relation to epitope exposure and how this insight might benefit vaccine design strategies. This MAb is in the list of current MAbs with notable cross-neutralizing activity.
Pantophlet2010
(neutralization, variant cross-reactivity, review)
-
2F5: The two distinct and conflicting models of C-terminal tail (CTT) topology for HIV-1 gp41 were tested by characterizing the accessibility of KE (Kennedy epitope) sequences of gp41 to Ab binding on the surface of Env-expressing cells and intact mature virions. 2F5 binds effectively to KE in the context of intact virions.
Steckbeck2010
(binding affinity)
-
2F5: This review outlines the general structure of the gp160 viral envelope, the dynamics of viral entry, the evolution of humoral response, the mechanisms of viral escape and the characterization of broadly neutralizing Abs. It is noted that this MAb neutralizes a variety of strains from different subtypes but it displays low neutralizing activity for clade C viruses.
Gonzalez2010
(neutralization, variant cross-reactivity, escape, review)
-
2F5: This review discusses recent rational structure-based approaches in HIV vaccine design that helped in understanding the link between Env antigenicity and immunogenicity. This MAb was mentioned in the context of immunogens based on the epitopes recognized by bNAbs.
Walker2010a
(neutralization, review)
-
2F5: This review discusses the types of B-cell responses desired by HIV-1 vaccines and various methods used for eliciting HIV-1 inhibitory antibodies that include induction and characterization of vaccine-induces B-cell responses. 2F5 was mentioned when discussing virus-like particles and liposomes, as 2F5 requires lipid binding in addition to gp41 MPER recognition for neutralization breadth.
Tomaras2010
(neutralization, review)
-
2F5: 37 Indian clade C HIV-1 Env clones obtained at different time points from five patients with recent infection, were studied in neutralization assays for sensitivities to their autologous plasma antibodies and mAbs. None of the 37 Env clones were neutralized by 2F5 even when the minimum DKW motif was present in IVC3-3-9F1, IVC3-5-25F2, and all the Env clones obtained from IVC-11.
Ringe2010
(neutralization)
-
2F5: This review discusses strategies for design of neutralizing antibody-based vaccines against HIV-1 and recent major advances in the field regarding isolation of potent broadly neutralizing Abs.
Sattentau2010
(review)
-
2F5: 34 Env-pseudotyped viruses from HIV-1 CRF01_AE - infected plasma samples collected in China were susceptible to neutralization by 2F5 to varying extents. The neutralization susceptibility of these viruses to 2F5 could not be determined by the conservation of the core epitope nor the existence of PNLG site within core epitope regions.
Nie2010
(neutralization)
-
2F5: The effect of absence and presence of sCD4 on accessibility and binding of HIV-1 gp41 MPER-binding epitopes on CCR5-tropic pseudoviruses from five different clades to the mAbs was studied. 2F5 showed moderate to high binding affinity to pseudoviruses from clade A (epitope mutants:tWFDIs, NWFDIs) clade B (NWFDIT) and clade D (NWFsIT), poor binding to clade CRF01_AE (NWFDIT) and no binding to clade B (sWFsIT), clade C (sWFsIT) and clade CRF01_AE (NWFDIs). Pseudoviruses from clade A (tWFDIs, NWFDIs), clade B (NWFDIT, sWFsIT), clade D (NWFsIT) and clade CRF01_AE (NWFDIT) were neutralized by 2F5. The presence of sCD4 significantly increased the binding affinity of 2F5 to clade A and clade CRF01_AE. There was a trend towards significant increase in binding affinity of 2F5 to clade C (sWFsIT) with sCD4 present, although no significant increase in binding affinity was observed for the other pseudoviruses.
Peachman2010a
(antibody binding site, neutralization, variant cross-reactivity, binding affinity, subtype comparisons)
-
2F5: The binding affinity and neutralization potency of three murine IgM mAbs and human MAb 2F5 (IgG and IgM isotypes) to pseudoviruses from HIV-1 clades A, B, C, D and CRF01_AE was studied in the virus capture assay. 2F5 IgG isotype bound to viruses 93RW and KNH (clade A), BAL-PV (clade B), 57128 and A07412 (clade D), and CM235 (clade AE) with much higher affinity than 2F5 IgM isotype. All viruses that bound to 2F5 IgG isotype along with the virus US-1PV were neutralized by 2F5 IgG. 2F5 IgM isotype only neutralized viruses 93RW and KNH (clade A), and A07412 (clade D).
Peachman2010
(neutralization, variant cross-reactivity, binding affinity, subtype comparisons)
-
2F5: This review discusses the studies done on poly-reactive antibodies (binding to two different epitopes), and the importance of polyreactivity. Low polyreactivity has been reported for 2F5.
Pluckthun2010
(review, antibody polyreactivity)
-
2F5: This paper shows that a highly neutralization-resistant virus is converted to a neutralization sensitive virus with a rare single mutation D179N in the C-terminal portion of the V2 domain. A panel of mutants were tested to determine whether they can improve the neutralization sensitivity of an extremely neutralization-resistant clinical isolate. 2F5 neutralized wild-type sensitive clone and 12/17 mutants tested (D179N, N179D, D179E, D179Q, D179H, D179S, D179A, D179N-P182S, V1/V2_006, V1_006, V2_006 and V1_005).
ORourke2010
(neutralization, variant cross-reactivity)
-
2F5: 2F5 was used in this study to detect the quantity of gp41 incorporated into virions from six mother and infant pairs (MIPs). Different levels of gp41 were incorporated into chimeric viral particles from the MIPs, where in some instances poor Env incorporation correlated with low virion infectivity and replication deficits and in other instances no such correlation was observed.
Zhang2010a
(mother-to-infant transmission)
-
2F5: MAb m9 showed superior neutralization potency compared to 2F5 in a TZM-bl assay, where it neutralized all 15 isolates compared to 2F5 that neutralized only 60% of the isolates tested and did not neutralize any clade C isolates. When compared in an additional panel of isolates including subtypes A, B, C, D, AE and AG, 2F5 neutralized 37% of the isolates while m9 neutralized 89%. 2F5 also showed lower inhibition potency of cell-to-cell transmission of HIV-1 compared to m9.
Zhang2010
(neutralization, variant cross-reactivity)
-
2F5: This review focuses on recent vaccine design efforts and investigation of broadly neutralizing Abs and their epitopes to aid in the improvement of immunogen design. NAb epitopes, NAbs response to HIV-1, isolation of novel mAbs, and vaccine-elicited NAb responses in human clinical trials are discussed in this review.
Mascola2010
(review)
-
2F5: Naturally occurring human and experimentally induced murine and rabbit GBV-C E2 Abs were studied for their ability to neutralize diverse HIV-isolates and showed that broadly neutralizing HIV Abs were elicited on immunization with GBV-C E2. MAb 2F5 neutralized a dual-tropic R5-X4 HIV-1 isolate in primary human PBMCs. The TriMAb control including 2F5 did not neutralize the HIV-1 R5 isolate in TZM-bl cells but did in PBMCs. Ag interaction with Anti-GBV-C E2 Abs is similar to that of with 2F5, that reacts with HIV-1 gp41 peptides and permeabilized cells.
Mohr2010
(neutralization)
-
2F5: Four anti-idiotypic Ab2/3H6 variants against 2F5 were created using three different humanization approaches to be able to elicit 2F5 Ab response and were then compared to the chimeric Ab2/3H6. The binding affinity and neutralization potency for 2F5 Ab by the resurfaced Ab2/3H6 and conservative CDR-grafted Ab2/3H6 was similar to that of chimeric Ab2/3H6, while there was lower affinity for aggressive CDR-grafted Ab2/3H6 and no affinity for superhumazied Ab2/3H6.
Mader2010
(anti-idiotype, neutralization, binding affinity)
-
2F5: A mathematical framework is designed to determine the number of Abs required to neutralize a single trimer called the stoichiometry of trimer neutralization (N). 15 different virus antibody combinations divided into five groups based on antibody binding sites were used in the designed model. 2F5 was classified in a group by itself as it binds a linear gp41 epitope. The number of 2F5 Abs needed to neutralize a single trimer was determined to equal 1 but N=2 could not be excluded at a significance level of 0.05.
Magnus2010
-
2F5: Cross-reactive NAb responses were characterized in 39 acute and chronically HIV-1 infected individuals. Abs targeting the 4E10 epitope were found in three of the patients, and one of those also had Abs targeting the 2F5 epitope.
Sather2010
(variant cross-reactivity)
-
2F5: Four human anti-phospholipid mAbs were reported to inhibit HIV-1 infection of human PBMC's by binding to monocytes and releasing soluble chemokines. The ability of different anti-phospholid mAbs to inhibit pseudovirus infection was studied. Unlike the anti-phospholipid Abs, MAb 2F5 was able to inhibit fusion induced by Aldrithiol-2 inactivated HIV-1 in Sup-T1 T cells. Four out of nine anti-phospholid mAbs inhibited HIV-1 infectivity in PBMC-based virus infection inhibition assay where a mixture of mAbs 2F5, IgG1b12, and 2G12 (TriMab) was used as a positive control. Lipid binding of 2F5 was not dependent on the presence of β2GP1.
Moody2010
(neutralization, binding affinity)
-
2F5: Targeted neutralizing epitopes have been identified based on the change in sensitivity to neutralization due to variations in known immunoepitopes studied in 17 subjects. There was no neutralizing activity that targeted the 2F5 epitope in any of the patient sera when the K665N/W672 mutant was used for screening of neutralizing activity.
Nandi2010
(neutralization, escape)
-
2F5: The antigenic structure of Gag-Env pseudovirions was characterized and it was shown that these particles can recapitulate native HIV virion epitope structures. 2F5 bound to the BaL Gag-Env pseudovirions, indicating presence of native trimers. The Gag-Env pseudovirions were further used to identify a subset of antigen-specific B cells in chronically infected HIV subjects.
Hicar2010
(binding affinity, structure)
-
2F5: 2F5 was shown to capture virion particles completely devoid of HIV-1 Env. Virus capture assay was modified with added incubation of virions and MAbs in solution followed by removal of unbound MAbs, which nearly eliminated the Env-independent binding by this Ab. This modification also allowed for relative affinity of 2F5 for virions to be quantified. There was an overall reduction in the efficiency of capture of molecular clones (MC) relative to pseudotyped virions by 2F5. In addition, nontrimeric Envs from JR-CSF MC virus were more efficiently captured by 2F5 than trimeric JR-FL. It is suggested that the capture of virions by 2F5 is mostly mediated by nonfunctional Env.
Leaman2010
(assay or method development, binding affinity)
-
2F5: A combinatorial library of HRV:HIV chimeric viruses displaying the ELDKWA epitope was designed and the antigenic properties of virus chimera were analyzed both in vitro and in silico. A number of virus chimera able to bind to 2F5 with greater affinity than chimeric viruses produced to date. Binding affinities of chimeric viruses were estimated computationally and experimentally and agreed well. Molecular modeling identified energetic and structural factors affecting the ability of the inserted 2F5 epitope to assume conformations capable of binding to 2F5.
Lapelosa2010
(antibody binding site, kinetics, binding affinity)
-
2F5: The role of HIV-1 envelope spike density on the virion and the effect it has on MAb avidity, and neutralization potencies of MAbs presented as different isotypes, are reviewed. Engineering approaches and design of immunogens able to elicit intra-spike cross-linking Abs are discussed.
Klein2010
(review)
-
2F5: 18 unique Env clones of subtype C HIV-1 derived from six African countries and Scotland were tested for their neutralization susceptibility by MAbs. Five of the gp160 chimeras tested for their neutralization by 2F5 were resistant to neutralization by this Ab as they lacked the core DKW motif in the MPER.
Koh2010a
(neutralization)
-
2F5: Peptide ligands for CD4i epitopes on native dualtropic Envs were selected by phage display. MAb 2F5 bound to Fly-synGFP producer cells both in the presence or absence of sCD4.
Dervillez2010
(binding affinity)
-
2F5: The effect of presence and absence of V1 loop was assessed using two approaches: remove V1 loop from the soluble trimeric gp140 construct (ΔV1SF162gp140) and second, substitute the V1 loop on SF162gp140 construct with four different V1 loops from 89.6, YU2, JRFL, and HxB2 (heterologous HIV-1 viruses). Deletion or substitution of V1 loop did not affect neutralization by 2F5 and there was only a small change in binding affinity to 2F5. gp41 immunogenicity was increased by V1 loop deletion, although gp41 antibodies did not bind to the 2F5 epitope. D368R modification to SF162gp120 did not affect the binding and neutralization by 2F5.
Ching2010
(neutralization, binding affinity)
-
2F5: The effect of HIV-1 complement opsonization on 2F5 activity was evaluated in three instances: HIV-1 transcytosis through epithelial cells, HIV-1 attachment on immature monocyte derived dendritic cells (iMDDC), and infectivity of iMDDC. 2F5 was not able to inhibit HIV-1 transcytosis. 2F5 inhibited the attachment of both opsonized and of non-opsonized HIV to iMDDC. 2F5 was able to inhibit production of both opsonized and non-opsonized HIV-1 in iMDDCs.
Jenabian2010
(complement)
-
2F5: Clustering analysis was performed to find patterns of neutralization reactivity for the dataset of 103 patients sera against 20 viruses. The clustering by five MAbs (including 2F5) against the 20 isolates was less statistically robust than that with serum titers, resulting in three clusters for both cases. The membership in an isolate cluster defined by serum titers was compared with its sensitivity to every MAb to understand the relationship of serum and MAb reactivity. Membership in all the three clusters did not correlate with sensitivity to 2F5.
Doria-Rose2010
(neutralization)
-
2F5: The review describes several different methods that have been used to isolate and characterize HIV MAbs within the human Ab repertoire. Relative advantages and limitations of methods such as EBV transformation, human hybridoma, non-immortalized B cell culture, combinatorial libraries from B cells and clonal sorting are discussed.
Hammond2010
(review)
-
2F5: Addition of bacterial endotoxin (LPS) had no effect on the potency of 2F5 neutralization in TZM-bl assay but addition of LPS in PBMC assay increased neutralization potency of 2F5. Endotoxin contamination was shown to mediate release of antiviral chemokines in PBMCs and is thus suggested to be able to cause false-positive results in PBMC-based neutralization assays.
Geonnotti2010
(neutralization)
-
2F5: In order to overcome problems of the PBMC-based neutralization assay a novel approach was developed utilizing a platform based on Renilla luciferase (LucR) expressing HIV-1 proviral backbone. Env-IMC-LucR reporter viruses expressing HIV-1 envs from different virus strains were incubated with NAbs, such as 2F5, and used to infect donor PBMCs. The inhibition was assessed by measuring virus-encoded LucR activity in the cell lysates. Significant variation in sensitivity to 2F5 was observed among different donor PBMCs, and this high variability was suggested to be a real biological effect attributable to use of different donor PBMCs, rather than assay-to-assay variability.
Edmonds2010
(assay or method development, neutralization)
-
2F5: Crystal structure of the extracellular domain of gp41 has been solved including fusion peptide proximal region (FPPR) heptad repeat 1 and MPER to examine their influence on gp41 post fusion conformation. Their presence increased the melting temperature of gp41 complex greatly compared to the core structure of gp41. Comparison of the solved crystal structure with the MPER conformation in complex with 2F5 suggests that 2F5 blocks the refolding process of gp41 at early steps.
Buzon2010
(antibody binding site, structure)
-
2F5: 21c binding, autoreactivity, polyreactivity and protective benefits are discussed and compared to other autoreactive MAbs, such as 2F5 and 4E10. Regulation of CD4i MAbs, such as 21c and 17b, by tolerance mechanisms is discussed.
Haynes2010
(autoantibody or autoimmunity, antibody polyreactivity)
-
2F5: Subtype B HIV-1 variants from historical seroconverters (individuals that seroconverted between 1985 and 1989) were equally sensitive to neutralization by 2F5 as variants isolated from contemporary seroconverters (ndividuals that seroconverted between 2003 and 2006).
Bunnik2010a
(neutralization, dynamics)
-
2F5: 17b was linked with sCD4 and the construct was tested for its neutralization breadth and potency. sCD4-17b showed significantly greater neutralization breadth and potency compared to 2F5, neutralizing 100% of HIV-1 primary isolates of subtypes A, B, C, D, F, CRF01_AE and CRF02_AG, while 2F5 neutralized some isolates of subtypes A, B, C and D, and all isolates of the CRF01_AE and CRF02_AG. Unlike sCD4-17b, 2F5 was not equivalently active against virus particles generated from different producer cell types.
Lagenaur2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
2F5: A set of Env variants with deletions in V1/V2 was constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Sensitivity of the evolved ΔV1V2 viruses was evaluated to study accessibility of their neutralization epitopes. 2F5 neutralized ΔV1V2 variants more potently than the full-length virus. 2F5 bound more efficiently to all uncleaved ΔV1V2 variant trimers compared to the full-length trimer, although the differences were minor.
Bontjer2010
(neutralization, binding affinity)
-
2F5: Optimized peptide mimetics of gp41 prehairpin intermediates were constructed to induce neutralizing responses in vaccinated guinea pigs and rabbits. Neutralization potency of sera from animals immunized with covalent trimeric immunogens was greater than the potency of sera from animals immunized with noncovalent trimers. Sera from animals immunized with longer constructs was more neutralizing than antisera from shorter constructs. Sera from immunized guinea pigs, but not from rabbits, neutralized half of the Tier 1 viruses tested. For the analyses, a mutant virus (HXB2-V570A) was used, which is hypersensitive to Abs binding to the pre-hairpin intermediate but not to mAbs that bind elsewhere. 2F5 neutralized HXB2-V570A slightly more than HXB2 wild type, probably because it targets a g41 region near the prehairpin intermediate.
Bianchi2010
(mimics, neutralization)
-
2F5: Review discusses the recent research done to improve the production, quality, and cross-reactivity of binding Abs, neutralizing Abs, monoclonal Abs with broad neutralizing activity, ADCC, and ADCVI Abs, and catalytic Abs. Studies focusing on several aspects of BNAb roles in vaccine development, and studies done to better understand the broad binding capacity and the exposure of epitopes of BNAbs are reviewed.
Baum2010
(effector function, neutralization, binding affinity, review)
-
2F5: Neutralizing activities of 2F5 were similar against parent and GnTI (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps) viruses, and the N301Q mutant virus (glycan at position 301 is removed). This suggests that the antennae of the complex glycans of gp120 and the upper part pf gp41 have little or no influence on 2F5 access to MPER.
Binley2010
(glycosylation, neutralization)
-
2F5: Confocal microscopy of giant unilamellar vesicles (GUVs) was used to visualize 2F5 interactions with lipid bilayers mimicking the conditions existing at the plasma membrane. 2F5 was only found in contact with GUVs bearing surface-bound 2F5-MPER peptide and was unable to directly react with GUV phospholipids. Enhancement of 2F5 binding to membrane-inserted epitope in vesicles displaying fluid phase co-existence was observed, consistent with the increase in surface concentration of the MPER peptide.
Apellaniz2010
(antibody interactions)
-
2F5: Insertion of an artificial 2F5 epitope into the V4 region of gp120 resulted in bivalent binding of 2F5 to both V4 and MPER regions of Env at the same time. Binding bivalency resulted in higher binding avidity compared to 2F5 MPER or 2F5 V4 alone, and in greatly enhanced neutralization efficiency. 2F5 was shown to be able to bind bivalently only in trans configuration, i.e. bridging the V4 region and the MPER in two gp120/gp41 subunits within one Env trimer. 2F5 bivalency was not achieved for 2F5 binding to V3 and MPER within a single gp120/gp41 subunit (cis-transfiguration).
Wang2010
(neutralization, binding affinity)
-
2F5: L669S substitution in gp41 dramatically increased (>250-fold) neutralization sensitivity of mutant virus to 2F5. Binding affinity of 2F5 to linear peptide with the L669S mutation did not differ from its binding affinity to the wild type peptide. In contrast, 2F5 binding affinity was increased for L669S mutation in peptide-lipid complex compared to the wild type. The lifetime of 2F5 neutralization was shown to be ∼3 fold longer for the L669S virus compared to wild type, indicating that the L669S mutation altered the MPER structure such that 2F5 epitope was exposed for a longer time.
Shen2010
(antibody binding site, neutralization, kinetics)
-
2F5: Neutralization potency of 2F5 was compared to that of HK20 scFv in TZM-based assay using 45 Tier 1 and Tier 2 HIV isolates. 2F5 neutralized 22/45 isolates. In addition, 2F5 was used in TriMab, together with 2G12 and b12, to examine neutralization of 9 clade A, B, C, D and E isolates in PBMC assay. Here, TriMab neutralized 7 isolates with 2 not determined.
Sabin2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
2F5: Crystal structure of the non-neutralizing 13H11 MAb in complex with a 20-mer gp41 MPER peptide was obtained and compared to that of neutralizing 2F5 MAb. The primary structural difference between the two MAbs was shown to be a large groove on the 13H11 idiotope between CDRs L1 and L2, and H1 and H2. Unlike 2F5, 13H11 did not bind to trimeric gp41-inter construct. 2F5 neutralization was not blocked by 13H11.
Nicely2010
(structure)
-
2F5: Two 2F5 mutants, F100B(H)A (phenylalanine at the tip of the CDR H3 loop is replaced with alanine) and delta CDR H3 (TLFGVPI residues are replaced with a Ser-Gly dipeptide linker) showed similar high affinity for linear peptide epitope binding as wild type 2F5, indicating that 2F5 CDR H3 apex residues are not involved in core epitope binding. Neutralization assays showed complete loss of neutralization by delta CDR H3 mutant and reduction of neutralization by F100B(H)A mutant, indicating that these residues are essential for neutralization. Differences in mutant and wild type 2F5 binding affinities were observed only when residues WFNITNWLWYIK were added to the gp41 MPER C terminus, and when this extended peptide was placed in a membrane bilayer. It is suggested that the role of the apex of the CDR H3 loop for neutralization is due to secondary interactions to either C-terminal MPER residues or/and components of membrane lipid bilayer.
Julien2010
(antibody binding site, neutralization, binding affinity)
-
2F5: Prefusion (gp140), prehairpin intermediate (gp41-inter) and postfusion (gp41-post) constructs were developed to define conformational states recognized by non-neutralizing cluster II Abs. gp41-inter was re-constructed replacing the six helix bundle with GCN4. 2F5 bound to, and showed the same kinetic profile, for both gp41-inter and GCN4-gp41-inter constructs, suggesting identical MPER conformation of the two constructs.
Frey2010
(binding affinity, structure)
-
2F5: Unlike for b12, decreasing neutralization sensitivity during the course of infection was not observed for 2F5 in 15 patients studied.
Bunnik2010
(neutralization)
-
2F5: 2F5 epitope was transplanted into 5 select protein scaffolds by computational techniques. The five resultant 2F5-epitope scaffolds (ES1-ES5) showed high affinity for 2F5MAb. Guinea pigs immunized with the 2F5-epitope scaffolds developed polyclonal sera that mimicked binding of 2F5 to the gp41 MPER region. Mice immunized with two of the 2F5-epitope scaffolds, ES2 or ES5, developed monoclonal Abs that bound to the 2F5 epitope with high affinity, induced a conformation similar to that induced by 2F5, and showed similar angles of epitope approach. In addition, the study showed that the flexibility of the engrafted epitope positively correlated with its immunogenicity.
Ofek2010a
(vaccine antigen design, vaccine-induced immune responses, binding affinity, structure)
-
2F5: 2F5 was used in competition assays with gp41 Abs cloned from B cells from patients with broadly neutralizing sera. None of the Abs from these patients competed for binding with 2F5. 2F5 competed for binding with MAbs 4E10, D17 and D50.
Pietzsch2010
(antibody interactions, binding affinity)
-
2F5: Chimeric human/mouse 2F5 Abs were generated in knock-in mice where the Ig heavy chain (HC) VhDJh from human 2F5 was targeted into mouse Igh locus. In vivo, the 2F5 VhDJh knock-in mouse line demonstrated that the great majority of B-lineage cells expressing the 2F5 VhDJh rearrangement were halted in their development at the transition from small pre-B to immature B cells. Homozygous knock-in mice showed reduced numbers of residual splenic B cells with low surface IgM density and severely diminished serum IgM levels. However, serum IgG levels were normal and did not react with autoantigens. The results suggest that 2F5 Vh is sufficiently autoreactive to invoke tolerance control of 2F5 Vh expression.
Verkoczy2010
(autoantibody or autoimmunity)
-
2F5: A dimerization domain is described in the C-terminal domain of gp41 (C54), where two C54 monomers form an asymmetric, antiparallel coiled coil. 2F5 and 4E10 bind to C54 with higher affinity compared to linear MPER peptides, and the interaction is biphasic described by a two-step conformational change model. 2F5 formed a more stable complex with C54 than 4E10. A conformational change accompanied the interaction of 2F5 and 4E10 with C54. It is suggested that the conformation of C54 dimer is a potential intermediate, capable of interacting with 2F5 and 4E10.
Liu2010
(antibody binding site, binding affinity)
-
2F5: The specificities of 2F5 binding to MPER peptides and phospholipids on the viral membrane are reviewed. Implications of 2F5 anti-host cell activity are discussed. This review also summarizes data on the evolution of HIV neutralizing Abs, principles of Env immunogen design to elicit broadly neutralizing Abs, and future critical areas of research for development of an Ab-based HIV vaccine.
Hoxie2010
(vaccine antigen design, review)
-
2F5: 6 male Indian rhesus macaques were given a dose of 2F5 one day prior and one day after challenge with SHIVBa-L, which was chosen because it was reasonably neutralization sensitive to both 2F5 and 4E10. All animals but one showed the absence of viral replication. Sera of all animals showed no gp120-specific responses, and no cellular immune responses were observed in any animals. The one animal in which presence of viral replication could not be excluded showed low-level viremia at day 35. A re-challenge of this animal conducted at month 6 after the initial challenge failed to induce productive infection, while the other 5 animals became infected at this time point. A second re-challenge 12 months later led to a regular infection course. 2F5 serum half-life was estimated as 4.6 days. 2F5 displayed significant antibody-dependent cell-mediated virus inhibition (ADCVI) activity, but only at high concentrations.
Hessell2010
(immunoprophylaxis)
-
2F5: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 2F5 neutralization activity was compared to the three new broadly neutralizing mAbs. 2F5 did not compete for binding to gp41 with any of the new mAbs. 2F5 neutralized 67% of Tier 1 and 36% of Tier 2 viruses, the neutralization of Tier 2 viruses being comparable to that of the new MAb HJ16. 2F5 rarely neutralized clade C isolates.
Corti2010
(neutralization, variant cross-reactivity)
-
2F5: 433 Abs were cloned from HIV envelope-binding memory B cells from 6 patients with broadly neutralizing sera. The Abs had neutralizing activity directed against several epitopes on gp120 and the majority neutralized Tier 1 viruses. Tier-2 neutralization was observed only with mixtures of MAbs, but only at high concentrations. 2F5 was used as a control and it neutralized 3/5 Tier 1 and 3/5 Tier 2 viruses.
Scheid2009
(neutralization)
-
2F5: Exogenous epitope tags were introduced in different parts of three variable regions, V1, V2 and V4, of two HIV isolates, SF162 and SF33. In the majority of the cases, tags did not have any effect on the susceptibility of the isolates to neutralization by 2F5. Only two viruses with tags in their V1 and V2 regions were more sensitive to neutralization by 2F5 compared to wild type.
Wallace2009
(antibody binding site, neutralization)
-
2F5: This review discusses obstacles to elicitation of protective NAbs, recent data on viral epitopes vulnerable to broadly NAbs, qualitative and quantitative implications of NAb response for vaccine development, and possible future areas of investigation to improve understanding of Env structure and stimulation of appropriate B cell responses.
Stamatatos2009
(review)
-
2F5: The structure and dynamic of the virion spike and the MPERe are discussed. Data revealing MPER steric barriers to Ab access, and recent results on the model for the structure and accessibility of the MPER on the native spike and the mechanisms of action for 2F5 are reviewed. Implications of the data for immunogen design is discussed.
Schief2009
(antibody binding site, review)
-
2F5: TZM-bl and PBMC systems were compared to investigate the influence of target cell environment on HIV entry inhibition. The sensitivity of TZM-bl system was confirmed by inhibitory capacity of 2G12, 2F5 and b12. 2F5 was shown to be significantly less active on TZM-bl cells, where it failed to inhibit 4 viruses with mutations in the 2F5 epitope, while 3/4 viruses were sensitive in the PBMC assay. HIV isolates were less sensitive to inhibition by 2G12, 2F5 and 4E10, with up to 100-fold lower sensitivity in the TZM-bl assay.
Rusert2009
(assay or method development, neutralization)
-
2F5: This review summarizes targets of autologous neutralizing Abs (AnAbs) in early and chronic infections. V1V2 is a frequent target of AnAbs, while V4 and V5 have marginal role and anti-V3 Abs do not contribute to autologous neutralization. In addition to variable regions, C3 is a neutralization target in subtype C viruses, and is thought to interact with V4. gp41 is thought to have marginal effect as a target of AnAbs, with only one study showing 4E10-resistant variants suggesting escape from AnAbs targeting this region. AnAb specificities and sequential development, and their role in preventing superinfection is also reviewed. The relatively high Ab titer required for prevention of superinfection and control of viremia, and the low inhibitory potential of b12, 2F5, 4E10 and 2G12 compared to antiretroviral drugs is discussed.
Moore2009
(autologous responses, review)
-
2F5: This review describes obstacles that have been encountered in the development of an HIV-1 vaccine that induces broadly neutralizing Abs, and unusual features of existing broadly neutralizing Abs, such as 2F5. Importance of identification and characterization of new epitopes, and of B-cell stimulation, is discussed.
Montefiori2009
(review)
-
2F5: IgG form of 2F5 neutralized SF162 Env very strongly while the IgM form neutralized the virus at much lower levels, barely reaching 50% neutralization. 2F5 IgM neutralization potency was compared and was lower than that of WR320 IgM murine MAb.
Matyas2009a
(isotype switch, neutralization)
-
2F5: An overview of the different expression strategies to over produce HIV neutralizing Abs, including 2F5, in plants. The attention is specially focused on expression strategies of Nef protein.
Marusic2009
(review)
-
2F5: Env clones of 2 out of 12 viruses were shown to be highly sensitive to neutralization by 2F5 in PBMC assay but were not inhibited by 2F5 in TZM-bl assay. Both envelopes carried a mutation in the core epitope of 2F5. The study suggests that TZM-bl assay can fail to detect neutralizing activity of in vivo relevance but may be more prone to detect epitope mismatches. Causes of the observed differences between the PBMC and TZM-bl assays were due to virus producer cells and target cells, that could influence virus entry inhibition.
Mann2009
(assay or method development, neutralization)
-
2F5: Ab specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. To test sera for presence of 2F5-like Abs, MPER peptides overlapping the core epitopes of 2F5 and 4E10 were used. Neutralization of HXB2 and SF162 by sera was not inhibited by the 2F5 peptide, indicating lack of 2F5-like Abs. Sera with limited neutralizing activity were mapped to V3. In some of the broadly neutralizing sera, the gp120-directed neutralization was mapped to CD4bs. Some sera were positive for NAbs against coreceptor binding region.
Li2009c
(assay or method development)
-
2F5: 2F5 membrane-binding mode of epitope recognition is reviewed in detail. The review also summarizes on how different modes of Ab binding and recognition are used to overcome viral evasion tactics and how this knowledge may be used to re-elicit responses in vivo.
Kwong2009a
(antibody binding site, review)
-
2F5: The review discusses the implications of HIV-1 diversity on vaccine design and induction of neutralizing Abs, and possible novel approaches for rational vaccine design that can enhance coverage of HIV diversity. Patterns of within-clade and between-clade diversity in core epitopes of known potent neutralizing Abs, including 2F5, is displayed.
Korber2009
(review)
-
2F5: HA-gp41, an antigen representing the trimeric fusion-intermediate conformation of gp41, was constructed and shown to bind to 2F5 with high nanomolar affinity. Rabbits immunized with HA-gp41 produced gp41-specific Abs that recognized epitopes overlapping with 2F5. Sera from immunized animals lacked neutralizing activity.
Hinz2009
(vaccine-induced immune responses, kinetics, binding affinity)
-
2F5: 2F5 alone or in combination with other Abs was not able to trigger complement-mediated lysis (CML) of 93BR020 and 92UG037 HIV strains.
Hildgartner2009
(complement)
-
2F5: FcγR-mediated inhibition and neutralization of HIV by 2F5 and other MAbs is reviewed. The review also summarizes the role of ADCC and ADCVI Abs on HIV infection inhibition and neutralization.
Forthal2009
(review)
-
2F5: Stimulation of platelets with gp41 peptides led to a significant reduction of RANTES release which could be restored if platelet cultures with gp41 peptides were performed in the presence of 2F5.
Cognasse2009
-
2F5: This review summarizes novel approaches to mapping broad neutralizing activities in sera and novel technologies for targeted MAb retrieval.
Binley2009
(assay or method development, review)
-
2F5: A significant fraction of splenic B cells from BALB/c mice was shown to bind a MPER peptide that included the 2F5 epitope. The binding was concentrated in IgM subsets. However, IgM interactions with MPER peptide included residues distinct from those involved in 2F5 binding, indicating that low avidity, non-paratopic interactions between MPER and B cells may interfere with or divert 2F5 bNAb responses.
Verkoczy2009
(binding affinity)
-
2F5: 2F5 reacted poorly with trimeric and dimeric forms of cross-linked sgp140(-) Env glycoprotein and precipitated only a trace amount of monomeric forms. This suggested that 2F5 epitope is occluded or disrupted in soluble oligomeric forms of Env.
Yuan2009
(antibody binding site)
-
2F5: The crystal structure for VRC01 in complex with an HIV-1 gp120 core from a clade A/E recombinant strain was analyzed to understand the structural basis for its neutralization breadth and potency. The number of mutations from the germline and the number of mutated contact residues for 2F5 were smaller than those for VRC01.
Zhou2010
(neutralization, structure)
-
2F5: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 did not show binding to 2F5.
Wu2010
(binding affinity)
-
2F5: Unlike PG9 and PG16, 2F5 neutralized kifunensine-treated pseudoviruses with similar potency as wild type pseudoviruses.
Walker2010
(neutralization)
-
2F5: Ab gene divergence analyses found that 2F5 Ab was significantly more divergent from the closest germline Abs than were hmAbs against other viruses. Germline-like 2F5 was constructed in a scFv format. It was shown that germline-like 2F5 did not bind to recombinant gp140 although the corresponding mature 2F5 showed binding.
Xiao2009
(binding affinity, antibody sequence)
-
2F5: EPR and NMR were used to define 2F5-induced MPER conformational changes. Large conformational changes of the MPER were observed upon binding of 2F5, where residues L669 and W670 were lifted out and exposed. It is suggested that 2F5 initially reacts with surface-exposed residues E662 and D664, followed by extraction of buried residues into its binding pocket, resulting in lifting up of the entire MPER N helix.
Song2009
(antibody binding site)
-
2F5: Patient sera from 13 HIV controllers and 75 chronic viremic patients were tested for the ability to block binding of 2F5 to Env JRFL gp140 oligomers. There was no difference observed between the controllers and chronic viremic patients. HIV controllers had the same levels of direct binding Abs to 2F5 peptide epitopes as viremic HIV-1 infected individuals. There was a higher level of binding to the 2F5 peptide than the 4E10 peptide. The NAb response was significantly lower in controllers, while ADCC was detected in all controllers but in only 40% of viremic patients.
Lambotte2009
(elite controllers and/or long-term non-progressors, neutralization)
-
2F5: One functional Env clone from each of 10 HIV-1 infected seroconverting individuals from India were analyzed for their sensitivity to MAbs and plasma pools of subtypes B, C and D. Only one of ten Indian Envs was sensitive to 2F5, and was the only Env that contained a DKW motif required for 2F5 recognition. HIVIG neutralized all 10 Envs, and the Envs were most sensitive to neutralization by subtype C pool, followed by subtype D and B pools, respectively. Amino acid signature patterns that associated with neutralization clusters were found. One signature position (667) was located within the 2F5 epitope.
Kulkarni2009
(neutralization, acute/early infection)
-
2F5: This MAb was shown to bind to the E2 (656-670) peptide, containing the MAb epitope, but not to E1 (532-546) peptide derived from the FPPR of gp41. However, peptide E1 (AASMTLTVQARQLLS) enhanced binding of 2F5 to the ELDKWA epitope and enhanced the effect of peptide E2 (NEQELLELDKWASLW) in a neutralization assay. E1 and E2 together inhibited binding of 2F5 to gp41 more efficiently than E2 alone, leading to a 25% greater reduction of neutralization. Core epitope of 2F5 was shown to be DKWAS.
Fiebig2009
(neutralization, kinetics, binding affinity)
-
2F5: A review about the in vivo efficacy of 2F5 and other MAbs against HIV-1, and about inhibition of HIV-1 infection by Ab fragments Fab, scFv and engineered human Ab variable domains or "domain antibodies" (dAbs).
Chen2009b
(neutralization, immunotherapy, review)
-
2F5: 2F5 neutralization breadth and potency was compared to that of two broadly neutralizing Abs PG9 and PG16 in a panel of 162 multi-clade viruses. 2F5 exhibited lower neutralization potency than PG9 and PG16.
Walker2009a
(neutralization, variant cross-reactivity)
-
2F5: 2F5 recognition of model cell or viral membranes with or without the presence of the peptide containing the MAb epitope was examined. 2F5 bound to both membranes with low affinity, suggesting that involvement of the antigen-binding site is absent. Binding of 2F5 increased significantly and exhibited almost irreversible binding in the presence of the membrane bound peptide epitope complex. It is suggested that 2F5 does not bind specifically to the membrane but that membrane involvement is important to the secondary structure of the 2F5 epitope.
Veiga2009
(antibody binding site, kinetics, binding affinity)
-
2F5: Four IgA MAb were isolated from Cambodian exposed but uninfected women through a construction of phage libraries and selection by gp41-ΔMPR and P1. These MAbs were correlated to protection from HIV-1 infection in HEPS. 2F5 could not compete with IgA Fab 43 for binding to P1. Three IgA Fabs showed a neutralizing activity similar to that of 2F5, while IgA 177 was much more potent than 2F5. When converted to IgG, Fab 177 displayed neutralization activity similar to that of 2F5.
Tudor2009
(neutralization)
-
2F5: An analytical selection algorithm and a reduced virus screening panel were created for assessment of serum neutralizing activity. It is suggested that selection of pseudoviruses for neutralization assays should focus on the overall resistance profile of the pseudovirus and against MAbs b12, 4E10, 2F5 and 2G12. Neutralization profiles of all viruses used for screenings were determined for 2F5.
Simek2009
(neutralization)
-
2F5: In one out of 311 HIV-1 infected patients, neutralizing Abs reacting with an epitope overlapping with that of 2F5 were found. These 2F5-like Abs were responsible for the neutralization breadth of the patient serum. The Abs arose in the patient 12-27 months after infection, coinciding with the development of autoantibodies against dsDNA and Jo-1. Patient sera were also positive for anti-cardiolipin autoantibodies. There was no evidence of development of 2F5 escape mutants.
Shen2009
(autoantibody or autoimmunity, neutralization)
-
2F5: Substantial increase in neutralization potency (∼5000-fold) of 2F5 was observed in cells expressing FcγRI, and a moderate increase in cells expressing FcγRIIb. Both receptors affected IgG1 and IgG3 versions of 2F5 equally. Cells expressing FcγRIIa and FcγRIIIa did not have any effect on the neutralization potency of this Ab. The effect of the FcγRs was observed only for MPER-specific Abs. FcγRI and FcγRIIb facilitated antibody-mediated neutralization of HIV-1 that was dependent on the Fc region, IgG subclass, and Ab epitope specificity.
Perez2009
(isotype switch, neutralization)
-
2F5: Mutations that decreased hydrophobicity of the CDR H3 loop of 2F5 had little effect on the affinity of the Ab to gp41 but strongly decreased and even completely disrupted 2F5 neutralization of HIV-1 isolates. On the other hand, mutations that increased hydrophobicity, such as tryptophan substitutions, were able to increase 2F5 neutralization potency. The effect of CDR H3 hydrophobicity on neutralization was independent of isolate sensitivity to 2F5.
Ofek2010
(neutralization)
-
2F5: Swarm analysis of viruses from one patient resulted in isolation of several different clones with different neutralization sensitivities against four HIV-1 positive sera. Comparison of sequences from two clones, one neutralization resistant and the other one not, revealed seven amino acid differences of which only Q655R showed increase in neutralization sensitivity to 2F5. This mutation disrupted a ring of hydrogen bonds in gp41 trimer and favored prehairpin intermediate structure. When 655R was introduced into two other neutralization resistant, unrelated viruses it also significantly increased sensitivity to neutralization by 2F5.
ORourke2009
(neutralization, acute/early infection)
-
2F5: Binding of 2F5 to lipid antigens was studied. 2F5 bound to a variety of phospholipids, a sulfated glycolipid, sulfogalactosyl ceramide, and to two neutral glycolipids. 2F5 also bound to squalene. Unlike 4E10, 2F5 did not bind to cardiolipin, cholesterol, and lipid A derived from Gram-negative bacteria.
Matyas2009
(binding affinity)
-
2F5: Unlike b12, 2F5 was not able to inhibit formation of virological synapses, it did not block the transfer of HIV particles from infected to target cells, and it did not block the trogocytic transfer of CD4 molecules from target to infected cells. Analysis of late events of HIV transmission showed, however, that 2F5 was able to block infection of target cells, indicating that HIV infection is transmitted by a neutralization-sensitive mechanism.
Massanella2009
-
2F5: There was an association between 2F5 Abs and anticardiolipin in serum samples from slow progressors.
Martinez2009
(autoantibody or autoimmunity)
-
2F5: By manipulation of the glycosylation machinery of S. cerevisiae a heavily glycosylated yeast protein, Pst1, was identified, that bound 2G12 with high affinity and was able to inhibit 2G12 neutralization of HxB and SF162 Env. Pst1 did not inhibit 2F5 neutralization of HxB viruses.
Luallen2009
(neutralization)
-
2F5: Crystal structure of a MPER subdomain was determined. The structure suggests that the four hydrophobic residues critical for the neutralization activity of 2F5 are buried within the MPER trimer interface. In experiments, 2F5 was able to bind to monomeric MPER but failed to bind to trimeric MPER.
Liu2009
(antibody binding site)
-
2F5: A highly efficient strategy for rapid expression of Ig genes was designed by combining isolation of Ig Vh and Vl genes from single cells, with novel linear Ig gene expression cassettes. The method was used to produce 2F5 from synthetic Vh and Vl genes. The recombinant 2F5 neutralized HIV-1 isolates with similar potency as MAb 2F5.
Liao2009
(assay or method development)
-
2F5: REMD analyses of the 2F5 epitope peptide in solution indicated that the 7-mere structure interconverts between α-helical and type I β-turn conformations. Insertion of the peptide into the VP2 puff of the HRV14 virus indicated a structure likely to be recognized by 2F5. A REMD solution simulation of a 21-amino acid MPER peptide including both 2F5 and 4E10 epitopes showed increased epitope exposure upon reduction of hydrophobic character of the peptide. The 21-aa peptide adopted a favorable conformation for Ab binding in solution, but when inserted into the VP2 puff of the HRV14 it adopted a less favorable conformation.
Lapelosa2009
(computational prediction)
-
2F5: 2F5 was active against subtype A KNH1144 virus and against KNH1144 SOS in both post CD4 and post-CD4/CCR5 assays.
Kang2009
-
2F5: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:2-5*10, IGHD:nd, D-RF:nd, IGHJ:6. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner.
Gorny2009
(antibody sequence)
-
2F5: Three plasmas with broadly cross-neutralizing activities and high titers of MPER Abs were identified among 156 chronically infected patients. JR-FL virus was better neutralized by these MPER plasmas than by 2F5, 4E10 and Z13e1.
Gray2009a
(neutralization)
-
2F5: Ten new non-neutralizing, cross-reactive mAbs were found in immunized mice. 2F5 only reacted with a subset of different Env subtypes tested due to amino acid substitutions in the epitopes. Binding of 2F5 to B_JRFL oligomer was not blocked by any of the newly detected mAbs.
Gao2009
(variant cross-reactivity)
-
2F5: An international collaboration (NeutNet) was organized to compare the performance of a wide variety of HIV-1 neutralization assays performed in different laboratories. Four neutralizing agents were evaluated: 4E10, 447-52D, sCD4 and TriMab (equal mixture of 2F5, 2G12 and b12). For TriMab, the mean IC50 values were always lower in the pseudovirus assays than in virus infectivity assays. In general, there were clear differences in assay sensitivities that were dependent on both the neutralizing agent and the virus. No single assay was capable of detecting the entire spectrum of neutralizing activities.
Fenyo2009
(assay or method development, neutralization)
-
2F5: Gene encoding gp140 was fused with three trimerization motifs, T4F, GCN and ATC. gp140, gp140(-)(with mutations in the furin-cleavage site), gp140(-)T4F and gp140(-)GCN bound 2F5 similarly, while gp140(-)ATC bound 2F5 less strongly.
Du2009
(binding affinity)
-
2F5: Four groups of Abs were detected in a patient directed against mimotopes of MPER, V3, C1 and LLP2. The MPER mimotope shared key amino acid residues with the 4E10 epitope. There were two different 2F5 epitope sequences observed in the patient virus over time. One was wildype and the other one displayed the D664N mutation consistent with resistance to 2F5 neutralization. Indeed, the earliest virus from the patient as very sensitive to neutralization by 2F5, while the second time point isolate showed 50-fold decrease in sensitivity, and the late viruses demonstrated complete resistance to 2F5 neutralization..
Dieltjens2009
(neutralization, escape)
-
2F5: Binding of 2F5 to its nominal epitope, and to a longer biepitope peptide-liposome conjugate was best described by a two step encounter-docking model. More efficient docking of 2F5 to its nominal epitope compared to 4E10 correlated with the more exposed nature of 2F5 nominal epitope on the membrane surface. Both 2F5 and 4E10 showed a more efficient docking to the biepitope peptide-liposome structures than to nominal epitopes, indicating that the conjugate provides a more favorable MPER orientation. 2F5 nominal epitope also had lower helical content than the biepitope conjugate.
Dennison2009
(antibody binding site, kinetics)
-
2F5: Structural characterization of the 2F5 epitope revealed that the FP (fusion protein) interactions stabilize MPER native-like structures in proximity to membrane surface. The structural constraints of the FP on the 2F5 epitope varied by medium polarity and temperature, where conformations accessible to 2F5 consisting of α helices and β turns were favored below 20 degrees C, and that β turns accumulated above this temperature and arose from the existing 310-helix structures. Presence of helices resulted in a more efficient Fab'-peptide interaction. The correct FP sequence caused the creation of a carboxy-terminal α helix following β turn in the native gp41 structure that is recognized by 2F5. Thus, recreating FP-induced interactions and structures is important for vaccine design.
delaArada2009
(antibody binding site, structure)
-
2F5: Two chimeras were constructed from a new HIV-2KR.X7 proviral scaffold where the V3 region was substituted with the V3 from HIV-1 YU2 and Ccon, generating subtype B and C HIV-2 V3 chimera. Both chimera, and the wildtype HIV-2KR and its derivatives HIV-2KR.X4 and HIV-2KR.X7 were resistant to neutralization by 2F5.
Davis2009
(neutralization)
-
2F5: Neutralization profiles of cloned Envs derived from recent heterosexual infections by subtypes A, C, D, and A/D from Kenya were determined. 2F5 was the most broadly neutralizing MAb among these transmitted env variants, neutralizing 15/31 viruses from 8/14 subjects. Some 2F5 resistant variants had mutations within the 2F5 epitope while other resistant viruses did not.
Blish2009
(neutralization, acute/early infection)
-
2F5: Conserved 2F5 epitope was displayed in various ways on the immunogenic human rhinovirus. 2F5 was used to capture chimeric viruses form a combinatorial library that presented the 2F5 epitope in antigenically relevant ways. Guinea pigs were immunized with chimeric viruses and immune responses were elicited with Abs capable of modestly neutralizing HIV-1 pseudoviruses of clades A, B, A/E, D and even C. The neutralizing responses correlated with the presence of ELDKWA-directed Abs. Viruses that were capable of eliciting broadly neutralizing Abs were benefited by the nonrandom occurrence of linker residues that promoted the formation of β-turns.
Arnold2009
(neutralization, vaccine antigen design, vaccine-induced immune responses)
-
2F5: Three 2F5 mutants, with Ala substitutions in their CDR H3 loops, bound to gp41 with somewhat reduced affinity compared to wildtype, indicating that CD3 loop does not make major contribution to contact with gp41. However, the three 2F5 mutants did not bind, or bound weakly, to lipid bilayers, indicating that the hydrophobic residues of CDR H3 loop are necessary for 2F5 interaction with viral membrane. The three 2F5 mutants also failed to neutralize BG1168 and SF162 strains, both which are neutralized by wildtype Ab. These results indicate a two-step mechanism of 2F5 binding and neutralization: 1) 2F5 attaches to the viral membrane through CDR H3 loops. 2) 2F5 binds to the MPER after gp41 has undergone conformational changes and assumes its prehairpin intermediate conformation. The results also indicate the importance of the HIV-1 membrane in binding and neutralization by 2F5 and that a lipid component may be required for an immunogen to induce 2F5-like Ab responses.
Alam2009
(antibody binding site, neutralization, kinetics, binding affinity)
-
2F5: HIV-1 variants derived from 5 patients at different timepoints during chronic infection were analysed for their sensitivity to neutralization by b12, 2G12, 2F5 and 4E10. In four of the patients, the earliest virus variants were highly sensitive to neutralization by 2F5 and the majority remained so during the course of infection. Sensitivity to 2F5 correlated with the absence of mutations in the 2F5 epitope, although in one of the patients, the variants did have mutations in the 2F5 epitope but not in the core DKW sequence. There were a small amount of variants found that were resistant to 2F5 neutralization although no mutations in the 2F5 epitope were observed, indicating that the epitope may not be equally exposed in all viruses. Virus variants from the fifth patient from the early infection all had a mutation in the core of the 2F5 epitope (DQW), and were all resistant to 2F5 neutralization. Later on, this mutation reverted to wildtype which coincided with increased sensitivity to 2F5.
Bunnik2009
(neutralization, escape)
-
2F5: 35 7-mer peptides corresponding to the primary 2F5 epitope with most commonly occurring substitutions in this MPER region were tested for crystal complex formation with 2F5 Fab'. The structural analyses revealed the importance of the correct positioning of residues 664 and 666 in the DKW core of the 2F5 epitope, from which 2F5 gets most of its neutralization potency and breadth. Also, positions 665 and 667 were identified as determinants of 2F5 neutralization potency and of neutralization escape. A buried surface area analysis of gp41 revealed that core epitope residues of 2F5 and 4E10 MAbs are more conserved than those of Z13, explaining the greater neutralization breadth of 2F5 and 4E10. It is suggested that evolving 2F5 to rely on the conserved residues of MPER might be a better way to increase its neutralization breadth and potency.
Bryson2009
(escape, structure)
-
2F5: 2F5 neutralized infection of PBLs with various HIV-1 strains with high potency. However, 2F5 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including 2F5, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs.
Chomont2008
(neutralization)
-
2F5: The lipid binding properties of 2F5, and the similarity to binding properties of anti-lipid mAbs, are discussed. Potential role of liposomes containing lipid A for induction of NAbs to lipids of HIV-1 is reviewed.
Alving2008
(autoantibody or autoimmunity, review)
-
2F5: A reference panel of recently transmitted Tier 2 HIV-1 subtype B envelope viruses was developed representing a broad spectrum of genetic diversity and neutralization sensitivity. The panel includes viruses derived from male-to-male, female-to-male, and male-to-female sexual transmissions, and CCR5 as well as CXCR4 using viruses. The envelopes displayed varying degrees of neutralization sensitivity to 2F5, with 14 of 19 envelopes sensitive to neutralization by this Ab.
Schweighardt2007
(assay or method development, neutralization)
-
2F5: This review summarizes data on possible vaccine targets for elicitation of neutralizing Abs and discusses whether it is more practical to design a clade-specific than a clade-generic HIV-1 vaccine. Development of a neutralizing Ab response in HIV-1 infected individuals is reviewed, including data that show no apparent division of different HIV-1 subtypes into clade-related neutralization groups. Also, a summary of the neutralizing activity of MAb 2F5 in different HIV-1 clades is provided.
McKnight2007
(variant cross-reactivity, review)
-
2F5: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 2F5 structure and binding to HIV-1 envelope and current strategies to develop versions of the Env spike with functional trimer properties for elicitation of broadly neutralizing Abs, such as 2F5, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed.
Phogat2007
(review)
-
2F5: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including 2F5 MAb, in vivo and in vitro activity of neutralizing Abs, the importance and downfalls of non-neutralizing Abs and antibodies that mediate antibody-dependent cellular cytotoxicity and the complement system, and summarizes data on areas that need future investigation on Ab-mediated immune control.
Huber2007
(review)
-
2F5: A new high throughput method was developed for neutralization analyses of HIV-1 env genes by adding cytomegalovirus (CMV) immediate enhancer/promoter to the 5' end of the HIV-1 rev/env gene PCR products. The PCR method eliminates cloning, transformation, and plasmid DNA preparation steps in the generation of HIV-1 pseudovirions and allows for sufficient amounts of pseudovirions to be obtained for a large number of neutralization assays. Pseudovirions generated with the PCR method showed similar sensitivity to 2F5 Ab, indicating that the neutralization properties are not altered by the new method.
Kirchherr2007
(assay or method development, neutralization)
-
2F5: 2F5 structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit anti-gp41 Abs, are reviewed in detail. The effect of the autoreactivity of 2F5 on vaccine antigen design is discussed.
Lin2007
(vaccine antigen design, review, structure)
-
2F5: This review summarizes 2F5 Ab epitope, properties and neutralization activity. 2F5 use in passive immunization studies in primates and possible mechanisms explaining protection against infection are discussed. Also, 2F5 autoreactivity and its implications for active immunizations are discussed.
Kramer2007
(immunotherapy, review)
-
2F5: The various effects that neutralizing and non-neutralizing anti-envelope Abs have on HIV infection are reviewed, such as Ab-mediated complement activation and Fc-receptor mediated activities, that both can, through various mechanisms, increase and decrease the infectivity of the virus. The importance of these mechanisms in vaccine design is discussed. The unusual features of the 2F5 MAb, and its neutralizing activities, are described.
Willey2008
(neutralization, review)
-
2F5: Current insights into CTLs and NAbs, and their possible protective mechanisms against establishment of persistent HIV/SIV infection are discussed. Pre- and post-infection sterile and non-sterile protection of NAbs against viral challenge, and potential role of NAbs in antibody-mediated antigen presentation in modification of cellular immunity, are reviewed. Use of 2F5 in immunization experiments and its in vivo anti-viral activity in suppression of viral rebound in HIV-1 infected humans undergoing structured treatment interruptions are described.
Yamamoto2008
(immunotherapy, supervised treatment interruptions (STI), review)
-
2F5: A mathematical model was developed and used to derive transmitted or founder Env sequences from individuals with acute HIV-1 subtype B infection. All of the transmitted or early founder Envs were sensitive to neutralization by 2F5, but there was a modest heightened resistance of acute Envs compared to chronic Envs to neutralization by 2F5.
Keele2008
(neutralization, acute/early infection)
-
2F5: Similarity level of the 2F5 binding site pentapeptide LDKWA to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 1 time, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome.
Kanduc2008
-
2F5: This review summarizes the obstacles that stand in the way of making a successful preventive HIV-1 vaccine, such as masked or transiently expressed Ab epitopes, polyclonal B-cell class switching, and inefficient, late, and not sufficiently robust mucosal IgA and IgG responses. Possible reasons why HIV-1 envelope constructs expressing 2F5 epitope fail to induce broadly neutralizing Abs are discussed.
Haynes2008
(vaccine antigen design, review)
-
2F5: Transmission of HIV-1 by immature and mature DCs to CD4+ T lymphocytes was significantly higher for CXCR4- than for CCR5-tropic strains. In addition, 2F5 inhibited transmission of CCR5-tropic viruses while transmission of 2F5-neutralized X4 variants increased, indicating that X4 HIV-1 has an advantage over R5 in transmission when neutralized with 2F5. The increase in transmission of X4 viruses is probably mediated by increase in capture, as X4 HIV-1 capture increased twofold upon 2F5 neutralization, while neutralization by 2F5 had no effect on capture of R5 viruses. Capture analysis of different HIV-1 molecular clones showed that neutralization by 2F5 increased transmission of only X4 and late R5X4 variants with a higher V3 charge.
vanMontfort2008
(co-receptor, neutralization, dendritic cells)
-
2F5: The newly detected MAb m44 was shown to neutralize a subtype C SHIV strain more potently than 2F5. In binding assays, 2F5 did not bind to 5Hb region. 2F5 did not compete with m44 for binding. A fusion protein of gp41 constructed for alanine-scanning mutagenesis bound to 2F5, indicating that its antigenic structure was intact. Five alanine mutations in the C-HR region (M94, W96, M97, R101, and I103) affected binding of 2F5 to gp41. 2F5 bound to self antigens in lipid binding assays.
Zhang2008
(neutralization, binding affinity)
-
2F5: The MPER region was shown to have an L-shaped structure, with the conserved C-terminal residues immersed in the membrane and the variable N-terminal residues exposed to the aqueous phase. The specific binding of 2F5 to the MPER was comparable to that of 4E10, with little or no binding to the membrane alone. It is suggested that 2F5, like 4E10, extracts its epitope from the viral membrane, and that the key requirement for neutralization is induction of structural rearrangement of the MPER hinge by the Ab. It is also suggested that exposure of the membrane-embedded residues of the MPER region to the immune system in their native L-shaped form may elicit neutralizing Abs.
Sun2008
(antibody binding site)
-
2F5: Trimeric envelope glycoproteins with a partial deletion of the V2 loop derived from subtype B SF162 and subtype C TV1 were compared. 2F5 recognized both B and C trimers, indicating that the 2F5 epitope was exposed and preserved in the subtype C trimers. Subtype C trimer had many biophysical, biochemical, and immunological characteristics similar to subtype B trimer, except for a difference in the three binding sites for CD4, which showed cooperativity of CD4 binding in subtype C but not in subtype B.
Srivastava2008
(binding affinity, subtype comparisons)
-
2F5: Quaternary structure of gp41 helical domains N-HR and C-HR was mimicked by 3α N-HR and 3α C-HR mimetic proteins consisting of covalently linked trimeric coiled-coil bundle, which is a truncated version of the gp41 prehairpin. The 3α mimetics were immunogenic and elicited Abs in guinea pigs specific for gp41. The sera from immunized animals neutralized viral R5 and X4-tropic viruses at 31.5 degrees C, but not under standard assay conditions, in which 2F5 blocked HIV-1 infection.
Sadler2008
(neutralization)
-
2F5: In order to assess whether small molecule CCR5 inhibitor resistant viruses were more sensitive to neutralization by NAbs, two escape mutant viruses, CC101.19 and D1/85.16, were tested for their sensitivity to 2F5, compared to the sensitivity of CC1/85 parental isolate and the CCcon.19 control isolate. The CC101.19 escape mutant has 4 sequence changes in V3 while the D1/85.16 has no sequence changes in V3 and relies on other sequence changes for its resistance. D1/85.16 isolate was moderately (6-fold) more sensitive to 2F5 neutralization than the parental isolate, while CC101.19 was not. As D1/85.16 escape mutant had a polymorphism in the first position of the 2F5 epitope (Aldkwas), this sequence change might be responsible for its modest increase in the 2F5 neutralization sensitivity. Overall, the study suggests that CCR5 inhibitor-resistant viruses are likely to be somewhat more sensitive to neutralization than their parental viruses.
Pugach2008
(co-receptor, neutralization, escape)
-
2F5: This minireview summarizes data on differences in neutralizing activities of MAbs and pooled human sera using a traditional primary cell neutralization assay and the more standardized TZM-bl reporter cell line assay. Also, suggestions are made on how to improve and standardize neutralization assays for comparable use in different laboratories. 2F5 neutralization was tested against a panel of 60 HIV-1 primary isolates (10 each from clades A-D, CRF01_AE and CRF02_AG) in the two assays. 13 viruses from the PBMC assay and 9 viruses from the TZM-assay were not neutralized by this Ab (including subtype C in both assays). In total, the assay discordances were shown to be bi-directional and not attributable to assay sensitivity.
Polonis2008
(assay or method development, neutralization, review, subtype comparisons)
-
2F5: The sensitivity of R5 envelopes derived from several patients and several tissue sites, including brain tissue, lymph nodes, blood, and semen, was tested to a range of inhibitors and Abs targeting CD4, CCR5, and various sites on the HIV envelope. All but one envelope from brain tissue were macrophage-tropic while none of the envelopes from the lymph nodes were macrophage-tropic. Macrophage-tropic envelopes were also less frequent in blood and semen. There was no clear correlation between macrophage-tropism and neutralization sensitivity to 2F5, indicating that variation in macrophage tropism is not caused by variation in the membrane proximal region of Env.
Peters2008a
(brain/CSF, neutralization)
-
2F5: For assessment of gp41 immunogenic properties, five soluble GST-fusion proteins encompassing C-terminal 30, 64, 100, 142, or 172 (full-length) amino acids of gp41 ectodomain were generated from M group consensus Env sequence. All five protein fragments were equally recognized by 2F5 indicating that the 2F5 epitope is conformationally similar and equally exposed. Patients considered as slow progressors generally exhibited greater Ab reactivity against the 30aa fragment, indicating that these Abs target MPER region and exhibit 2F5- and 4E10-like properties. Plasma from these patients also exhibited broader and more potent neutralizing activity against several HIV-1 isolates. Plasma from 8 of 44 patients reacted with peptides that bind 2F5, indicating that these patients mounted 2F5-like Ab response.
Penn-Nicholson2008
(rate of progression)
-
2F5: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 2F5 was used as control in neutralization assays, and was able to neutralize JR-FL isolate, and with lower potency, SF162. A chimeric SF162 variant with a JR-FL-like V3 sequence was hypersensitive to neutralization by this Ab.
Patel2008
(neutralization)
-
2F5: Contemporaneous biological clones of HIV-1 were isolated from plasma of chronically infected patients and tested for their functional properties. The clones showed striking functional diversity both within and among patients, including differences in infectivity and sensitivity to inhibition by 2F5. There was no correlation between clonal virus infectivity and sensitivity to 2F5 inhibition, indicating that these properties are dissociable. The sensitivity to 2F5 inhibition was, however, a property shared by viruses from a given patient, suggesting that the genetic determinants that define this sensitivity may lie in regions that are not necessarily subject to extensive diversity.
Nora2008
(neutralization)
-
2F5: 2F5 was shown to bind to Envs used in typical epitope binding assays, unlike the neutralizing Abs 8K8, DN9, and D5 used in this study.
Nelson2008
-
4E10: The study compared the in-membrane recognition and blocking activity of the 2F5 and 4E10 MAbs, using solution-diffusing, unstressed phospholipid vesicles with sizes that approximate to that of the HIV virion, and an MPER-derived sequences that combines the full length 2F5 and 4E10 epitopes. 2F5 MAb had lower affinity for membrane-bound species than 4E10 MAb, as defined by inhibition data together with direct electron microscopy and flow cytometry determination of the vesicle-antibody association.
Huarte2008a
-
2F5: 2F5 reacted with maltose-binding proteins MBP30 and MBP32, containing both HR1 and HR2 domains of gp41, and with MBP37 and MBP44, containing only the HR2 domain, but not with MBP-HR1, containing only the HR1 domain.
Vincent2008
(antibody binding site)
-
2F5: Neutralization susceptibility of CRF01_AE Env-recombinant viruses, derived from blood samples of Thai HIV-1 infected patients in 2006, was tested to 2F5. Approximately 40% of viruses tested showed high susceptibility to 2F5, including viruses with and without conserved 2F5 epitopes, suggesting that the susceptibility of CRF01_AE to 2F5 is not determined by the conservation of the core epitope sequence. Several X4R5 viruses were less susceptible to 2F5 compared with X4 or R5 viruses. There was no correlation observed between virus neutralization susceptibility to 2F5 and viral infectivity, the length of the gp120 variable regions, or the number of PNLG sites.
Utachee2009
(co-receptor, neutralization, subtype comparisons)
-
2F5: CTB-MPR649-684 (cholera toxin subunit B and residues 649-684 of gp41 MPER region) peptide was developed for vaccine studies in rabbits. 2F5 affinity to the CTB-MPR peptide was equivalent to 2F5 affinity toward an MPR peptide, indicating that the fusion peptide presented antigenically competent MPR. Sera from immunized rabbits displayed no neutralizing activity, but could inhibit epithelial transcytosis of virus, indicating elicitation of non-neutralizing Abs capable of stopping mucosal transmission and infection of target cells.
Matoba2008
(binding affinity)
-
2F5: A MPER peptide, AISpreTM, overlapping 2F5 and 4E10 epitope sequences, was capable of breaching the permeability barrier of lipid vesicles. 2F5 blocked the peptide bilayer-destabilizing activity, whether the lipid composition contained cholesterol or sphingomyelin raft-lipids, indicating that the lipid composition of the membrane has a less pronounced effect on the 2F5 inhibitory activity. The 2F5 epitope appears to remain anchored to the water-membrane interface and is more accessible for Ab binding under different membrane lipid conditions.
Huarte2008
(antibody binding site)
-
2F5: Synergy of 2F5 with MAbs 2G12, D5, and peptide C34 was examined. 2F5 exhibited synergy in inhibition of HIV-1 89.6 with MAb 2G12, D5 and peptide C34. In combination with a matured D5 variant (2-75), the synergistic effect was increased. D5 and 2F5 contributed equally to the observed synergy. It is suggested that 2F5 and D5 have complementary roles, binding to distinct but adjacent Env trimers on the same virion, thereby synergistically preventing formation of fusion pores.
Hrin2008
(antibody interactions)
-
2F5: Neutralization of HIV-1 BAL by 2F5 Ab was compared to neutralization capabilities of immunoprecipitated IgG and IgA Abs from the colostrum of two goats immunized with HIV-1 MPR 649-684 peptide. Immunoprecipitated IgG and IgA showed varying and low level neutralization of free virus, while the highest percent neutralization achieved by 2F5 was 24.9%.
Dorosko2008
(neutralization)
-
2F5: Three constructs of the outer domain (OD) of gp120 of subtype C, fused with Fc, were generated for immunization of mice: OD(DL3)-Fc (has 29 residues from the center of the V3 loop removed), OD(2F5)-Fc (has the same deletion reconstructed to contain the sequence of 2F5 epitope), and the parental OD-Fc molecule. Only OD(2F5)-Fc construct reacted with 2F5. Sera from mice immunized with OD(2F5)-Fc showed low Ab titers, and no significant neutralization activity.
Chen2008a
(neutralization, vaccine antigen design)
-
2F5: The goal of the study was to measure NAb responses in patients infected with HIV-1 prevalent subtypes in China. g160 genes from plasma samples were used to establish a pseudovirus-based neutralization assay. 2F5 neutralized 67% of subtype B clones and all subtype AE clones, but not subtype BC clones.
Chong2008
(neutralization, subtype comparisons)
-
2F5: The study examined whether elastin-like peptide (ELP) fusion technology is compatible with the production of MAb 2F5, which is a complex heteromultimeric pharmaceutical protein. ELP fusion to the light chain, heavy chain of both chains of a plant-derived antibody had no adverse effects on protein quality, but had a positive impact on the yield.
Floss2008
-
2F5: To investigate B-cell responses immediately following HIV-1 transmission, env-specific Ab responses to autologous and consensus Envs in plasma donors were determined. Broadly neutralizing Abs with specificity similar to 2F5 did not appear during the first 40 days after plasma virus detection.
Tomaras2008
(acute/early infection)
-
2F5: The neutralization profile of early R5, intermediate R5X4, and late X4 viruses from a rhesus macaque infected with SHIV-SF162P3N was assessed. 2F5 neutralized the late X4 virus, and to some extent the parental R5 virus, but did not neutralize the R5X4 intermediate. A K to N mutation within the 2F5 epitope in the R5X4 intermediate accounted for its neutralization resistance.
Tasca2008
(co-receptor, neutralization, escape)
-
C2F5: Neutralization of HIV-1 IIIB LAV isolate by 2F5 was within the same range as the neutralization of the virus by natural antibodies from human sera against the gal(α1,3)gal disaccaride linked to CD4 gp120-binding peptides, indicating that the activity of natural antibodies can be re-directed to neutralize HIV-1.
Perdomo2008
(neutralization)
-
2F5: Two HIV-1 isolates, NL4-3 and KB9, were adapted to replicate in cells using the common marmoset receptors CD4 and CXCR4. The adaptation resulted in a small number of changes of env sequences in both isolates. The adapted NL4-3 variants were equally sensitive to neutralization by 2F5 as the adapted KB9 variants. Some of the NL4-3 and KB9 variants exhibited increased sensitivity to neutralization by 2F5 compared to the wildtype isolates.
Pacheco2008
(neutralization)
-
2F5: Eight 2F5 Fab' crystal structures, free and in complex with various gp41 peptide epitopes, revealed several key features of Ab-antigen interaction. The extended complementarity-determining region (CDR) H3 loop is mobile, both in ligand-free and epitope-bound forms. The interaction between 2F5 and the ELDKWA epitope core is critical, and there are also close and specific contacts with residues located N-terminal to the core, while the residues located at the C-terminus of the core do not interact as tightly with the Ab. In the presence of a larger peptide, these C-terminus residues adopt a conformation consistent with the start of an α helix. At the base of the CDR H3, a sulfate ion is present near residue Arg100H, that might be mimicking the negatively charged phosphate of a lipid headgroup representing a possible site of interaction between 2F5 and the phospholipid bilayer.
Julien2008
(antibody binding site, structure)
-
2F5: The IC50 for 2F5 in a standard neutralization assay is 3.8nM but is increased 20-fold in the postattachment neutralization assay to 72nM. The neutralization half-life for 2F5 is 15 minutes but is increased 3-fold to 44 minutes in the presence of N36Mut(e,g), peptide, which is a class 3 inhibitor that prolongates temporal window of neutralization by disrupting trimerization of the N-heptad repeat (N-HR) in the prehairpin intermediate by sequestering the N-HR into N-HR/N36Mut(e,g) heterodimers. HXB2 was neutralized synergistically by 2F5 and N36Mut(e,g), where the formation of N-HR/N36Mut(e,g) heterodimers enhances the probability of 2F5 binding and the binding of 2F5 enhances the probability of N-HR/N36Mut(e,g) heterodimer formation, greatly diminishing the probability of 6-helix bundle formation.
Gustchina2008
(antibody binding site, neutralization, kinetics)
-
2F5: NMR structure of P1, a minimal MPER region that permits interaction with the mucosal galactosyl ceramide HIV-receptor, was analyzed in interaction with 2F5 at different pH. The best fit between NMR P1 and crystal structures of the Ab was at pH 6 and 5. The binding of 2F5 to P1 inserted into the liposomes of different compositions mimicking various biological membranes revealed 5- to 10-fold higher affinity of 2F5 to P1 in the lipid environment compared to aqueous environment, suggesting that specific lipid environment stabilizes the appropriate structure of the HIV-1 peptide.
Coutant2008
(kinetics, binding affinity, structure)
-
2F5: Crystal structure of the heterodimeric complex of Ab2/3H6 Fab, an anti-idiotypic Ab, and 2F5 Fab, showed that the contacts between the Abs are predominantly made between the heavy chains of the two molecules. Mainly CDR-H3 of Ab2/3H6 forms contacts to 2F5 although residues from all three heavy-chain loops contribute to binding, interacting with a single linear ten amino acid sequence on the surface of 2F5. There is only a limited overlap between the parts of 2F5 recognized by Ab2/3H6 and those interacting with peptides derived from the linear gp41 epitope, but this overlap is sufficient to lead to steric competition between Ab2/3H6 and gp41. The results indicate that Ab2/3H6 is an anti-idiotypic Ab of the Ab2γ class, an Ab that does not carry the internal image of the linear primary gp41 2F5 epitope.
Bryson2008
(anti-idiotype, structure)
-
2F5: 24 broadly neutralizing plasmas from HIV-1 subtype B and C infected individuals were investigated using a series of mapping methods to identify viral epitopes targeted by NAbs. Three different assays were used to analyze gp41-directed neutralizing activity. MAb 2F5 was shown to neutralize equivalently in the standard and post-CD4/CCR5 assay. Weak post-CD4/CCR5 neutralization was detected in five subtype B and two subtype C plasmas. 2F5 was shown to neutralize two of the MPER-engrafted mutant viruses, but the subtype B plasmas did not exactly recapitulate this activity. Neutralization of four subtype B plasmas was not inhibited by a 2F5 peptide. These results indicated that the anti-gp41 activity of the plasmas was probably not due to the presence of 2F5-like Abs.
Binley2008
(neutralization, subtype comparisons)
-
2F5: An anti-idiotypic mouse Ab (Ab2/3H6) against MAb 2F5 was partially humanized, expressed and characterized for its interactions with 2F5. The recombinantly expressed variants of Ab2/3H6 were able to bind to the paratope of 2F5 and also significantly inhibit binding of 2F5 to its epitope. All recombinant Ab2/3H6 were also able to inhibit the neutralization of HIV-1 isolate RF by 2F5.
Gach2007a
(anti-idiotype, neutralization, binding affinity)
-
2F5: HIV-1 env clones resistant to cyanovirin (CV-N), a carbohydrate binding agent, showed amino acid changes that resulted in deglycosylation of high-mannose type residues in the C2-C4 region of gp120. Compared to their parental virus HIV-1 IIIB, these resistant viruses maintained similar sensitivity to 2F5.
Hu2007
(neutralization, escape)
-
2F5: The ability of 2F5 to neutralize recently transmitted viruses was examined in four homosexual and two parenteral transmission pairs. The vast majority of recently transmitted viruses from 3/4 homosexual recipients were sensitive to neutralization by 2F5, although viruses isolated later in the course of infection showed increased sensitivity to 2F5 in the patient with early viruses resistant to 2F5 neutralization. In the parenteral transmission, one of the recipients had early viruses resistant to 2F5 neutralization, and one had viruses sensitive to 2F5 neutralization. The neutralization sensitivity patterns of recipient viruses to 2F5 did not correlate to the neutralization sensitivity patterns of their donors in the homosexual couples, while the HIV-1 variants from the parenteral pairs were similarly resistant/sensitive to neutralization by 2F5. Despite variations in 2F5 sensitivity, none of the viruses had mutations in the crucial DKW residues of the 2F5 epitope.
Quakkelaar2007a
(neutralization, acute/early infection, mother-to-infant transmission)
-
2F5: Three MAbs, 2G12, 4E10 and 2F5, were administered to ten HIV-1 infected individuals treated with ART during acute and early infection, in order to prevent viral rebound after interruption of ART. MAb infusions were well tolerated with essentially no toxicity. Viral rebound was not prevented, but was significantly delayed in 8/10 patients. 2G12 activity was dominant among the MAbs used. Antiviral activity of 2F5 was not clearly demonstrated. Development of resistance to 2F5 was not observed despite ongoing viral replication. Plasma HIV-1 RNA levels did not increase following cessation of Ab infusion. Plasma viremia was essentially identical between patients not receiving MAb therapy and patients receiving 4E10 and 2F5 in the face of 2G12 resistance. 2F5 also failed to accumulate with repeated infusions in patient plasma. Long-term suppression of viremia was achieved in 3/10 patients.
Mehandru2007
(escape, immunotherapy, supervised treatment interruptions (STI))
-
2F5: The study compared Ab neutralization against the JR-FL primary isolate and trimer binding affinities judged by native PAGE. There was direct quantitative relationship between monovalent Fab-trimer binding and neutralization, implying that neutralization begins as each trimer is occupied by one Ab. In BN-PAGE, neutralizing Fabs, 2F5 in particular, and sCD4 were able to shift JR-FL trimers, In contrast, most non-neutralizing Fabs bound to monomer, but their epitopes were conformationally occluded on trimers, confirming the exclusive relationship of trimer binding and neutralization.
Crooks2008
(antibody binding site, neutralization, binding affinity)
-
2F5: Five amino acids in the gp41 N-terminal region that promote gp140 trimerization (I535, Q543, S553, K567 and R588) were considered. Their influence on the function and antigenic properties of JR-FL Env expressed on the surfaces of pseudoviruses and Env-transfected cells was studied. Various non-neutralizing antibodies bind less strongly to the Env mutant, but neutralizing antibody binding is unaffected. There was no difference in 2F5 binding to wild type and mutant JR-FL, and 2F5 inhibited infection of the two pseudoviruses with comparable potencies.
Dey2008
(binding affinity)
-
2F5: This study explored features of Env that would enhance exposure of conserved HIV-1 epitopes. The changes in neutralization susceptibility, mediated by two mutations, T569A (in the HR1) and I675V (in the MPER), were unparalleled in their magnitude and breadth on diverse HIV-1 Env proteins. The variant with both TA and IV mutations was 2.8-fold more susceptible to b12, >180-fold more susceptible to 4E10, >780-fold more susceptible to sCD4 and resulted in 18-fold enhanced susceptibility to autologous plasma and >35-fold enhanced susceptibility to the plasma pool. It was also >360-fold more susceptible to 2F5. Mutant with only one IV mutation was >27-fold more susceptible to 2F5.
Blish2008
(antibody binding site, neutralization)
-
2F5: Molecular mechanism of neutralization by MPER antibodies, 2F5 and 4E10, was studied. Preparations of trimeric HIV-1 Env protein in the prefusion, the prehairpin intermediate and postfusion conformations were used. The epitopes for 2F5 and 4E10 were found to be exposed only on a form designed to mimic an prehairpin intermediate state during viral entry, which helps to explain the rarity of 2F5- and 2E10-like antibody responses.
Frey2008
(antibody binding site, binding affinity)
-
2F5: This study describes the molecular features of murine anti-idiotypic MAb Ab2/3H6, which mimics the antigen recognition site of 2F5. Mice immunization with AB2/3H6 Fab variants elicited a specific 2F5-like humoral immune response.
Gach2008a
(anti-idiotype, mimics, vaccine antigen design, structure)
-
2F5: This study describes an expression, purification and in vivo administration in guinea pigs of an anti-idiotypic HIV-1 vaccine based on murine anti-idiotypic MAb Ab2/3H6, which mimics the antigen recognition site of 2F5.
Gach2008
(anti-idiotype, mimics, vaccine antigen design)
-
2F5: 2F5 binding to gp41 was partially blocked by murine MAbs 5A9 and 13H11. 13H11 and the three cluster II human MAbs 98-6, 126-6 and 167-D blocked 2F5 binding to gp41 epitopes to variable degrees; the combination of 98-6 and 13H11 completely blocked 2F5 binding. MAb 2F5 showed strong binding to HIV-1-positive infected cells.
Alam2008
(antibody interactions, kinetics, binding affinity)
-
2F5: The potency of 2F5 was 25-fold higher than the potency of new neutralizing Fab 3674 in neutralization of laboratory and primary strains of HIV-1 subtypes A, B and C.
Gustchina2007
(neutralization, subtype comparisons)
-
2F5: A D386N change in the V4 region, which results in restoration of N-glycosylation at this site, did not have any impact on the neutralization of a mutant virus by 2F5 compared to wildtype. Also, there was no association between increased sensitivity to 2F5 neutralization and enhanced macrophage tropism.
Dunfee2007
(neutralization)
-
2F5: This review summarizes data on the development of HIV-1 centralized genes (consensus and ancestral) for induction of neutralizing antibody responses. Functionality and conformation of native epitopes in proteins based on the centralized genes was tested and confirmed by binding to 2F5 and other MAbs. Antibodies induced by immunization with these centralized proteins did not, however, have the breadth and potency compared to that of 2F5 and other broadly neutralizing MAbs. 2F5 physical characteristics of autoantibodies as a possible reason for lack of 2F5 broad production is also discussed.
Gao2007
(antibody binding site, neutralization, vaccine antigen design, review)
-
2F5: 2F5 bound with slower on-rates and faster off-rates to the SF162gp140 and ΔV2gp140 proteins than the anti-gp41MAbs P4A3 and P4C2, but in contrast to the anti-gp41 MAbs, it neutralized the SF162 virus. Thus, differences in neutralization potency could not be explained by differing kinetics.
Derby2007
(neutralization, kinetics, binding affinity)
-
2F5: Competition of free gp120 89.6 with immobilized gp140 89.6 for binding to 2F5 was assessed. The binding of this Ab to coated gp140 was not affected by an increase in the gp120 concentration.
Zhang2006a
(binding affinity)
-
2F5: The epitope recognition sequence for this Ab was introduced into the corresponding region of SIVmac239 but the replication of this viral variant (SIVmac239/2F5) was delayed in comparison to the parental virus. SIVmac239/2F5 was specifically neutralized by MAb 2F5.
Yuste2006
(neutralization, SIV)
-
2F5: Significant levels of 2F5 were shown to bind to HA/gp41 expressed on cell surfaces and this Ab did stain cells expressing HA/gp41 in a fluorescence assay. However, a much smaller percentage of the HIV 89.6 Env expressing cells were stained with this Ab than with 2G12, indicating that this Ab recognition site on gp41 is masked by the gp120 subunit in the HIV Env protein and that it is more easily accessible on the HA/gp41 chimeric protein.
Ye2006
(antibody binding site, binding affinity)
-
2F5: Viruses with wild-type HIV-1JR-FL Envs and HIV-1 hXBc2 Envs were neutralized by this Ab at much lower concentrations than HIV-1 YU2 Env viruses. Viruses bearing inserted artificial epitopes of FLAG in the V4 region were as sensitive to neutralization by this Ab as the parental viruses. A clear relationship between neutralization potency and the affinity of the anti-FLAG antibody for its cognate epitope was observed.
Yang2006
(neutralization, binding affinity)
-
2F5: SHIV SF162p4 virus used as challenge in ISCOM vaccinated macaques was shown to be highly sensitive to neutralization by this Ab.
Pahar2006
(neutralization)
-
2F5: 2 of 18 subtype C env-pseudotyped clones derived from individuals in acute/early stage of HIV-1 infection were neutralized by this Ab, both of them had a DKW motif reported to be a requirement for 2F5recognition. The sensitivity of clones to a mix of Abs IgG1b12, 2G12 and 2F5 was tracked to IgG1b12.
Li2006a
(neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
-
2F5: This Ab was used as a positive control in the neutralization assay. At the highest Ab concentrations, 2F5 was able to neutralize several primary isolates but not all, with a neutralization pattern similar to that of rabbit sera immunized with monovalent and polyvalent DNA-prime/protein-boost Env from different HIV-1 subtypes. At a reduced concentrations, 2F5 showed much weaker neutralizing activities.
Wang2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
2F5: Interaction of this Ab with membrane model systems revealed that 2F5 does not significantly interact with model viral or target cell membranes indicating that it does not use membrane interaction prior to gp41 docking.
Veiga2006
(antibody binding site)
-
2F5: The capacity of different soluble lysoderivatives to inhibit 2F5 binding to immobilized HIV-1 peptide epitope were compared and it was shown that only dilysocardiolipin resulted in effective blocking. Dilysocardiolipin was also shown to compete with native-functional gp41 for 2F5 recognition indicating that specific cardiolipin recognition by 2F5 involves the epitope-binding site.
Sanchez-Martinez2006a
(antibody binding site)
-
2F5: This Ab is shown to have the capacity to penetrate into the membrane interfaces and recognize isolated peptide-epitope sequence embedded into the membrane, however, 2F5 recognizes its epitope with lower affinity when immersed into the membrane interface. This lower affinity is suggested to result from a differently oriented epitope residues in the membrane-bound state.
Sanchez-Martinez2006
(antibody binding site)
-
2F5: The effect of epitope position on 2F5 neutralization was examined by inserting the 2F5 epitope into MLV proline rich region Env surface protein (SU) or into MLV Env TM comparable to its natural position. 2F5 was shown to block cell fusion and virus infection with the SU-located 2F5 epitope while MLV with HA epitope at the same position was not neutralized by anti-HA. 2F5 was shown to block Env-mediated cell fusion in MLV with TM-located 2F5 epitope. Epitope position was also shown to have effect on neutralization by 2F5, where inhibition of cell fusion was more than 10-fold lower when the 2F5 epitope was in SU than in TM.
Ou2006
(antibody binding site, neutralization)
-
2F5: This Ab recognized AIS (amphipathic-at-interface sequence)-FP (fusion peptide) hybrid sequence with higher affinity than the linear AIS, indicating that the hybrid sequence better emulates the native gp41 2F5 epitope.
Lorizate2006a
(antibody binding site, binding affinity)
-
2F5: PreTM peptide lacks the complete epitope sequence required for efficient recognition of this Ab. Thus, 2F5 was not able to arrest the leakage process and pore-formation at the viral membrane surface indicating that blocking of membrane destabilization depends on specific 4E10 epitope recognition.
Lorizate2006
-
2F5: Novel approaches based on sequential (SAP) and competitive (CAP) antigen panning methodologies, and use of antigens with increased exposure of conserved epitopes, for enhanced identification of broadly cross-reactive neutralizing Abs are reviewed. Previously known broadly neutralizing human mAbs are compared to Abs identified by these methods.
Zhang2007
(review)
-
2F5: Spread of HIV-1 through formation of virological synapses (VS) between infected and uninfected T-cells was shown to require Env-CD4 receptor interactions. Treatment of cells with 2F5 did not block VS-mediated transfer, indicating that VS-mediated transfer is not dependent on activation of viral membrane fusion. 2F5 at the same or lower concentrations blocked cell-free infection.
Chen2007
(neutralization)
-
2F5: Pseudoviruses derived from gp120 env variants that evolved in multiple macaques infected with SHIV 89.6P displayed a range of degrees of virion-associated Env cleavage. Pseudoviruses with higher amount of cleaved Env were more resistant to neutralization by 2F5. The gp41 sequence was the same in all pseudoviruses, indicating that changes in gp120 can mediate sensitivity of gp41 to neutralization.
Blay2007
(neutralization)
-
2F5: To test the immunogenicity of three molecularly engineered gp41 variants on the cell surface their reactivity with 2F5 was assessed. The reactivity of 4cSSL24 variant was comparable to gp160 while the other two variants showed somewhat lower expression levels. When guinea pigs were immunized with the three variants, the level of the specific anti-gp41 Ab responses was low with the anti-gp41 response preferentially directed to the C-helical domain, away from the MPER region.
Kim2007
(vaccine antigen design, binding affinity)
-
2F5: No differences in neutralization sensitivity between (R5)X4 and R5 viruses obtained early and late after X4 emergence were observed.
Bunnik2007
(co-receptor, neutralization)
-
2F5: HIV-1 neutralized with 2F5 was shown to be more efficiently captured by immature monocyte-derived DCs (iMDDCs) and DC-SIGN-expressing Raji cells than nonneutralized virus. 2F5-neutralized virus captured by these cells was successfully released and transferred to CD4+ T lymphocytes. The released virus could be re-neutralized by 2F5 before infecting CD4+ T cells, indicating that Ab-HIV-1 complex is separated upon capture by DC-SIGN cells. Capture of 2F5-neutralized virus was inhibited by blocking Fc receptors and DC-SIGN on iMDDCs, indicating significant role of DC-SIGN, and a partial role of Fc receptors, in the Ab-enhanced capture of HIV-1.
vanMontfort2007
(enhancing activity, neutralization, dendritic cells)
-
2F5: Infusion of a MAb cocktail (4E10, 2G12 and 2F5) into HIV-1 infected subjects was shown to be associated with increased levels of serum anti-cardiolipin and anti-phosphatidylserine Ab titers, and increased coagulation times. In the absence or in the presence of adult and neonate plasma, 2F5 exhibited low binding to phosphatidylserine, did not bind to cardiolipin, and did not induce significant prolongations of clotting times in human plasma, indicating that infusion of 2F5 was not responsible for autoreactivity and prolonged clotting times.
Vcelar2007
(antibody interactions, autoantibody or autoimmunity, binding affinity, immunotherapy)
-
2F5: The major infectivity and neutralization differences between a PBMC-derived HIV-1 W61D strain and its T-cell line adapted counterpart were conferred by the interactions of three Env amino acid substitutions, E440G, D457G and H564N. Chimeric Env-pseudotyped virus Ch5, containing all three of the mutations, was only marginally more neutralization sensitive to 2F5 than Ch2, which did not contain any of these mutations. Env-pseudotyped viruses containing D457G mutation alone, or in combination with E440G or H564N, were also more sensitive to neutralization by 2F5 than Ch2.
Beddows2005a
(neutralization)
-
2F5: Four primary isolates (PIs), Bx08, Bx17, 11105C and Kon, were tested for binding and neutralization by 2F5. 2F5 was able to neutralize Bx08, Bx17 and 11105C with various efficiencies, but bound inefficiently to all four PIs. There was no direct correlation between binding and neutralization of the four PIs by 2F5. CD4-induced gp120 shedding had no effect on binding of 2F5 to Bx08.
Burrer2005
(neutralization, binding affinity)
-
2F5: A panel of 60 HIV-1 isolates, with complete genome sequences available, was formed for neutralization assay standardization. It comprises of 10 isolates from each of the subtypes A, B, C, D, CRF01_AE and CRF02AG, with majority of the viruses being of R5 phenotype and few of X4 phenotype. Neutralization profile of each isolate was assessed by measuring neutralization by sCD4, a cocktail of MAbs including 2G12, 2F5 and IgG1b12, and a large pool of sera collected from HIV-1 positive patients. The MAb cocktail neutralized with >50% a large portion of the isolates (51/60) including: 10 subtype A isolates, 8 subtype B isolates, 8 subtype C isolates, 9 subtype D isolates, 7 CRF-01_AE isolates, and 9 CRF_02AG isolates.
Brown2005a
(assay or method development, neutralization, subtype comparisons)
-
2F5: The structure of the 2F5 MAb, particularly its CDRH3 region's binding mechanisms to the MPER region of gp41, and possibly the cellular membrane as well, are reviewed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed.
Burton2005
(antibody binding site, review, structure)
-
2F5: Trimeric gp140CF protein synthesized from an artificial group M consensus Env gene (CON6) bound well to 2F5, indicating correct exposure of the 2F5 epitope.
Gao2005a
(antibody binding site)
-
2F5: 2F5 neutralized viral isolates HXBc2, SF162, 89.6, BaL, ADA, and YU2. Neutralization was concentration dependent, as higher MAb concentration resulted in higher % of neutralization.
Grundner2005
(neutralization)
-
2F5: Furin co-transfection did not have an effect on the reactivity of Δ140ct HXBc2 and 3.2P pseudoviruses with 2F5, or on their neutralization sensitivity. Presence or absence of sialic acid residues did not affect Env reactivity with 2F5. A cleavage-competent form of 3.2P reacted poorly with 2F5, while its cleavage-defective counterpart showed higher level of MAb reactivity. Both cleavage-competent and cleavage-defective HXBc2 showed higher levels of reactivity to 2F5. DDT-induced dissociation of SOS gp140 and the estimate of cleavage was scored higher when 2F5 was used as detection Ab than when B13 MAb was used.
Herrera2005
(antibody binding site, neutralization, binding affinity)
-
2F5: Why broadly neutralizing Abs, such as 2G12, 2F5 and 4E10, are extremely rare, and their protective abilities and potential role in immunotherapy are discussed.
Julg2005
(neutralization, immunotherapy, review)
-
2F5: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alternations of both gp41 and gp120. The alternations did not affect virus CD4 binding, coreceptor binding site exposure, or infectivity of the virus, but did result in decreased binding of certain MAbs and increased neutralization resistance to MAbs as well as to human polyclonal HIV-Ig and pooled human sera. 2F5 MAb, however, effectively neutralized both the LLP-2 mutant and wildtype viruses, and also exhibited similar levels of binding to both the LLP-2 mutant and the wildtype virus.
Kalia2005
(antibody binding site, neutralization, binding affinity)
-
2F5: A series of genetically modified Env proteins were generated and expressed in both insect and animal cells to be monitored for their antigenic characteristics. For 2F5, most of the modified proteins expressed in insect cells containing the 3G mutation (mutations in 3 glycosylation sites) showed higher levels of binding to the MAb than the wildtype did. Additional presence of a glycosylation mutation 1G, close to the 2F5 epitope, increased binding of 2F5 compared to the binding to Env without the mutation. The highest binding to 2F5 was observed for the dV1V2 mutant. When expressed in animal cells, the 3G mutant was the one that displayed increased binding to 2F5 compared to other mutants.
Kang2005
(antibody binding site, binding affinity)
-
2F5: A trimeric recombinant gp140 construct was developed for immunization studies. Its structural integrity was assessed by a panel of MAbs. The trimeric recombinant gp140 lacked the membrane proximal ectodomain segment of gp41, but the 2F5 Ab did bind efficiently to the gp140 trimers containing the entire gp41 ectodomain.
Kim2005
(antibody binding site)
-
2F5: A trimeric gp41 construct comprising the env transmembrane domain and the extracellular C-terminal region (gp41ctm) was incorporated into liposomes. 2F5 bound to the liposome-incorporated gp41ctm, indicating that its extracellular region is accessible to this Ab. Sera from mice immunized with either gp41ctm alone or with gp41ctm-liposome did not show any significant neutralization activity, indicating that the construct might not properly expose its 2F5 epitope.
Lenz2005
(antibody binding site, neutralization)
-
2F5: Full-length gp160 clones were derived from acute and early human HIV-1 infections and used as env-pseudotyped viruses in neutralization assays for their characterization as neutralization reference agents. 13 out of 19 pseudoviruses were neutralized by 2F5, but few required higher concentration of the Ab for neutralization. MN, SF162.LS and IIIB strains were highly sensitive for neutralization by 2F5. Resistance to neutralization by 2F5 was associated with mutations in the DKW motif, or elsewhere in the 2F5 epitope. A mixture of IgG1b12, 2F5 and 2G12 (TriMab) exhibited potent neutralizing activity against all Env-pseudotyped viruses except one. 8 out of 12 Env-pseudotyped viruses were more sensitive to neutralization by 2F5 than their uncloned parental PBMC-grown viruses.
Li2005a
(assay or method development, neutralization)
-
2F5: Pseudoviruses expressing HIV-1 envelope glycoproteins from BL01, BR07 and 89.6 strains were compared in neutralization assays to replication competent clone derived from transfection of 293T cells (IMC-293T) and to the IMC-293T derived from a single passage through PBMC (IMC-PBMC). The neutralization responses of pseudoviruses and corresponding IMC-293T to 2F5 were similar, while a significant decrease in viral neutralization sensitivity to 2F5 was observed for all three IMC-PBMC viruses. The decrease was associated with an increase in average virion envelope glycoprotein content on the PBMC-derived virus.
Louder2005
(assay or method development, neutralization)
-
2F5: A short review of studies on 2F5 interaction with autoantigens, epitope accessibility, structure, and neutralizing capability. The reasons why 2F5 appears infrequently in nature are discussed.
Nabel2005
(antibody binding site, neutralization, immunotherapy, review)
-
2F5: Viruses containing substitutions at either L568 or K574 of the gp41 hydrophobic pocket were resistant to D5-IgG1 but were as sensitive to 2F5 as the wildtype virus. 2F5 neutralized more isolates than D5-IgG1 and was shown to be more potent. 2F5 did not, however, neutralize some of the isolates neutralized by D5-IgG1.
Miller2005
(neutralization)
-
2F5: This short review summarizes recent findings of the role of neutralizing Abs in controlling HIV-1 infection. Certain neutralizing MAbs and their potential role in immunotherapy and vaccination, as well as the reasons for their poor immunogenicity, are discussed.
Montefiori2005
(antibody binding site, therapeutic vaccine, escape, immunotherapy)
-
2F5: Escape mutations in HR1 of gp41 that confer resistance to Enfuvirtide reduced infection and fusion efficiency and also delayed fusion kinetics of HIV-1. The mutations also conferred increased neutralization sensitivity of virus to 2F5. Enhanced neutralization correlated with reduced fusion kinetics, indicating that the mutations result in Env proteins remaining in the CD4-triggered state for a longer period of time.
Reeves2005
(antibody binding site, drug resistance, neutralization, escape, HAART, ART)
-
2F5: More that 90% of viruses from both acutely and chronically infected HIV-1 patients were inhibited by this Ab, however, viruses from acute patients were significantly more sensitive to 2F5 than viruses from chronic patients. The epitope of this Ab was highly conserved among all isolates tested suggesting that the higher susceptibility of acute viruses may be due to better epitope accessibility. The sensitivity of viruses to 2F5 was also highly correlated to their sensitivities to 4E10.
Rusert2005
(antibody binding site, antibody interactions, autologous responses, neutralization, acute/early infection)
-
2F5: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed.
Srivastava2005
(antibody binding site, neutralization, vaccine antigen design, binding affinity, immunotherapy, mother-to-infant transmission, review, structure)
-
2F5: Six acutely and eight chronically infected patients were passively immunized with a mix of 2G12, 2F5 and 4E10 neutralizing Abs during treatment interruption. Two chronically and four acutely infected individuals showed evidence of a delay in viral rebound during Ab treatment suggesting that NAbs can contain viremia in HIV-1 infected individuals. All subjects with virus sensitive to 2G12 developed Ab escape mutants resulting in loss of viremia and failure to treatment while no escape was observed for 4E10 and 2F5. Plasma levels of 2G12 were substantially higher than those of 2F5 and 4E10, and the 2G12 levels exceeded the in vitro required 90% inhibitory doses by two orders of magnitude in subjects that responded to Ab treatment. No such differences were observed for 2F5 or 4E10, suggesting that high levels of NAbs are required for inhibition in vivo, and that the in vivo concentrations of 4E10 and 2F5 might have been too low to control viremia and exert a selective pressure.
Trkola2005
(acute/early infection, escape, immunotherapy, HAART, ART, supervised treatment interruptions (STI))
-
2F5: Ab neutralization of viruses with mixtures of neutralization-sensitive and neutralization-resistant envelope glycoproteins was measured. It was concluded that binding of a single Ab molecule is sufficient to inactivate function of an HIV-1 glycoprotein trimer. The inhibitory effect of the Ab was similar for neutralization-resistant and -sensitive viruses indicating that the major determinant of neutralization potency of an Ab is the efficiency with which it binds to the trimer. It was also indicated that each functional trimer on the virus surface supports HIV-1 entry independently, meaning that every trimer on the viral surface must be bound by an Ab for neutralization of the virus to be achieved.
Yang2005b
(neutralization)
-
2F5: A substantial fraction of soluble envelope glycoprotein trimers contained inter-subunit disulfide bonds. Reduction of these disulfide bonds had little effect on binding of the 2F5 to the glycoprotein, indicating that the inter-S-S bonds had no impact on the exposure of 2F5 epitope.
Yuan2005
(antibody binding site)
-
2F5: This Ab recognized the gp41 epitope ALDKWQ from the 92/BR/025.9 strain. HIV-1 infected patients treated with T20 showed decreased reactivity of their sera to a peptide containing the 2F5 epitope. The Ab titer to this peptide recovered after cessation of T20 therapy. It is indicated that 2F5 may interfere with the T20-HR1 interaction.
Vincent2005
(antibody interactions)
-
2F5: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1.
McCann2005
(antibody binding site, antibody interactions, neutralization, vaccine antigen design, variant cross-reactivity, immunotherapy, review)
-
Two ELDKWA-specific MAbs were obtained from mice immunized with four copies of ELDKWA-epitope with spacers between the epitopes. The two Abs inhibited syncytium formation less efficiently than 2F5 but were as potent as 2F5 in neutralization of primary isolate 92US657. The two murine MAbs were ineffective against the laboratory-adapted HIV-1 IIIB strain while 2F5 neutralized successfully. Neither 2F5 nor the two new MAbs neutralized group O primary isolate BCF02.
Zhang2005
(antibody binding site, neutralization, vaccine antigen design)
-
2F5: 2F5 was investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. 2F5 showed modest neutralization in the standard format, which was increased with the gp41 tail truncation and/or addition of a disulfide bridge linking gp120 and gp41. 2F5 was also able to neutralize in all the other neutralization formats analyzed, suggesting that it binds Env trimers at various stages of infection. None of the analyzed HIV-1+ human plasmas neutralized in the post-CD4/CCR5 format indicating absence of 2F5 and 4E10 - like Abs.
Crooks2005
(antibody binding site, assay or method development, neutralization)
-
2F5: This review summarizes data on the polyspecific reactivities to host antigens by the broadly neutralizing MAbs IgG1b12, 2G12, 2F5 and 4E10. It also hypothesizes that some broadly reactive Abs might not be routinely made because they are derived from B cell populations that frequently make polyspecific Abs and are thus subjected to B cell negative selection.
Haynes2005a
(antibody interactions, review, antibody polyreactivity)
-
2F5: This review summarizes data on 447-52D and 2219 crystallographic structures when bound to V3 peptides and their corresponding neutralization capabilities. 2F5, like 447-52D and like other HIV-1 neutralizing Abs, was shown to have long CDR H3 loop, which is suggested to help Abs access recessed binding sites on the virus.
Stanfield2005
(antibody binding site, review, structure)
-
2F5: In addition to gp120-gp41 trimers, HIV-1 particles were shown to bear nonfunctional gp120-gp41 monomers and gp120-depleted gp41 stumps on their surface. 2F5 effectively neutralized wildype virus particles, however, it did not capture virus efficiently. 2F5 was found to bind to both nonfunctional monomers and to gp120-gp41 trimers. Binding of 2F5 to trimers correlated with its neutralization of wildtype virus particles. Monomer binding did not correlate with neutralization, but it did correlate with virus capture. It is hypothesized that the nonfunctional monomers on the HIV-1 surface serve to divert the Ab response, helping the virus to avoid neutralization.
Moore2006
(antibody binding site, neutralization, binding affinity)
-
2F5: Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). 2F5 recognized all four gp140 proteins equally. 2F5 was found to equally neutralize SF162 and Δ2F5.4E10, which is a virus with mutations in the 2F5 and 4E10 epitopes and is resistant to neutralization by 2F5 and 4E10. This indicates that 2F5-like Abs were not present in sera from the gp140-immunized animals nor in the SHIV-infected and in the HIVIG sera.
Derby2006
(antibody binding site, neutralization)
-
2F5:A fusion protein (FLSC R/T-IgG1) that targets CCR5 was expressed from a synthetic gene linking a single chain gp120-CD4 complex containing an R5 gp120 sequence with the hinge-Ch2-Ch3 portion of human IgG1. The fusion protein did not activate the co-receptor by binding. In PBMC assays, FLSC R/T-IgG1 neutralized primary R5 HIV-1 isolates more potently than 2F5, while in cell-line based assays they were comparable.
Vu2006
(neutralization)
-
2F5: Sera from rabbits immunized with either monomeric gp120, trimeric cleavage-defective gp140 or disulfide-stabilized soluble trimeric gp140 were tested for neutralization of chimeric SIVmac239 viruses expressing epitope for this Ab. Little or no neutralization was observed indicating that little or no Ab activity in these rabbit sera was directed against the gp41 region.
Beddows2007
(neutralization, vaccine antigen design)
-
2F5: Env-pseudotyped viruses were constructed from the gp160 envelope genes from seven children infected with subtype C HIV-1. 2F5 failed to neutralize any of the seven viruses, correlating with the replacement of the crucial lysine at the position 665 of the 2F5 epitope on these viruses. When this Ab was mixed with IgG1b12 and 2G12, the neutralization was similar as to IgGb12 alone, indicating that the majority of the pool activity was due to IgG1b12. When 4E10 was added to this mix, all isolates were neutralized.
Gray2006
(neutralization, variant cross-reactivity, responses in children, mother-to-infant transmission)
-
2F5: Pharmacokinetic properties of this Ab were studied in HIV infected patients infused with high doses of 2G12. The Ab did not elicit an endogenous immune response and had distribution and systemic clearance values similar to other Abs. The elimination half-life was measured to 4.3 days.
Joos2006
(kinetics, immunotherapy)
-
2F5: Inhibition of 2F5 binding to gp160 by 2F5-like Abs in sera from long-term non-progressors (LTNP) was determined. 2F5-like Abs were present in almost all sera from LTNPs but at a lower levels than b12. No statistically significant correlation was found for the specificity of this Ab comparing sera able to neutralize all four HIV-1 strains and sera that could not.
Braibant2006
(enhancing activity, neutralization, variant cross-reactivity, subtype comparisons)
-
2F5: Neutralization rates and rate constants for the neutralization of clade B primary isolates SF33, SF162 and 89.6 by this Ab were determined. Statistically significant neutralization was not observed for isolates SF162 and 89.6. It was shown that neutralization sensitivity is not associated with neutralization of cell-associated or free virus.
Davis2006
(neutralization, variant cross-reactivity, kinetics)
-
2F5: The majority of broadly cross-reactive neutralizing (BCN) Envs were neutralized at lower concentrations of 2F5 than the non-BCN Envs. Amino acid variability of the 2F5 epitope was examined. The presence of T at position 662 was associated with increased sensitivity to neutralization by 2F5 while the K665N mutation resulted in resistance to 2F5
Cham2006
(neutralization, variant cross-reactivity, escape, subtype comparisons)
-
2F5: Neutralization of HIV-1 primary isolates of different HIV-1 clades (A, B, C, D, E) by 2F5 was determined in cells expressing high or low surface concentrations of CD4 and CCR5 receptors. CD4 cell surface concentration had no effect on the inhibitory activity of this Ab while the CCR5 surface concentration had a significant effect decreasing the 50% inhibitory concentration of 2F5 in cell lines with low CCR5.
Choudhry2006
(co-receptor, neutralization, variant cross-reactivity)
-
2F5: Genetic variability and co-variation of the MAb 2F5, 4E10 and Z13 epitopes in B and non B clades was investigated. A significant shift in the predominant sequence patterns over time was observed for all three epitopes. Also, significant inter-subtype genetic variability of the three epitopes was detected. However, the 4E10 epitope displayed a more similar variability within B clade and non-B clades, concurring with the cross-clade neutralizing activity of this MAb. Epitope co-variation was also noted, as one third of the recently isolated HIV-1 strains displayed simultaneous epitope variants.
Dong2006
(antibody binding site, subtype comparisons)
-
2F5: The ability of this Ab to inhibit viral growth was increased when macrophages and immature dendritic cells (iDCs) were used as target cells instead of PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication by this Ab for macrophages and iDCs can occur by two distinct mechanisms, neutralization of infectivity involving only the Fab part of the IgG, and, an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles.
Holl2006
(dendritic cells)
-
2F5: 2F5 was shown to interact with cells transiently transfected by VSV-gp120 expressing vector and stained with sera from mice immunized intranasally with VSV vector expressing HIV-1 HXB2 gp120, indicating that VSV-HXB2 immunization produced anti-HIV-1 Abs.
Jiang2006
(vaccine antigen design)
-
2F5: Viruses with cleavage-competent 2G12-knockout Env and cleavage-defective Env able to bind 2G12 were constructed. 2F5 was shown to bind more to the cleavage-defective Envs than to the cleavage-competent Envs. More 2F5 binding was detected to cells co-expressing wildtype and leavage-defective Env than to a mixture of cells expressing either, suggesting that uncleaved Env proteins have an enhancing effect of the binding of 2F5 to the heterotrimer or that fewer than three Abs can bind per trimer and that 2F5 has a higher affinity for the uncleaved Env. Env pseudotyped virions bearing either Wt3.2P(+)gp140δct Env or a mixture of the wildtype and cleavage-defective Env had similar sensitivities to neutralization by 2F5.
Herrera2006
(neutralization, binding affinity)
-
2F5: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The neutralizing activity of 2F5 was observed to be higher in iMDDCs than in PBLs and PHA-stimulated PBMCs. Furthermore, the kinetics of Ab addition showed that this MAb interferred with the first events of HIV-1 entry in iMDDCs. High concentrations of 2F5 triggered a non-HIV-related maturation of target cells. Blockade of FcγRII on iMDDCs decreased the anti-HIV activity of 2F5 while increased expression of FcγRI increased inhibition of HIV by 2F5, suggesting the involvement of these receptors in the HIV-inhibitory activity of this Ab.
Holl2006a
(neutralization, kinetics, dendritic cells)
-
2F5: 2F5 was produced in transgenic tobacco BY2 suspension cell cultures. The plant derived antibody was efficiently assembled and intact. When compared to CHO-derived 2F5, the plant derived 2F5 showed similar kinetic properties and 89% of the binding capacity of the CHO-derived Ab. However, it was only 33% as efficient in HIV-1 RF neutralization assay.
Sack2007
(neutralization, binding affinity)
-
2F5: This study found that, contrary to expectations, the viruses resistant to b12, 4E10, 2G12 and 2F5 neutralization did not have lower replication kinetics than viruses sensitive to neutralization. Viruses from early infection tended to have relatively low replications rates.
Quakkelaar2007
(viral fitness and/or reversion, acute/early infection, escape)
-
2F5: Z13e1, a high affinity variant of Fab Z13, was identified through targeted mutagenesis and affinity selection against gp41 and an MPER peptide. Z13e1 showed 100-fold improvement in binding affinity for MPER antigens over Z13, but was still less potent than 4E10 at neutralizing several pseudotyped Envs. Neutralization assays of HIV-1 JR2 MPER alanine mutants showed that mutants W666A and W672A were completely resistant to neutralization by 2F5.
Nelson2007
(antibody binding site)
-
2F5: High levels of gp120-specific Abs were elicited when mice and rabbits were immunized by DNA priming and protein boosting with G1 and G2 grafts, consisting of 2F5 and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120. A consistent NAb response against the homologous JR-FL virus was detected in rabbits but not in mice. 4E10 bound to the engrafted construct, but embedding the MPER epitopes in the immunogenic V1/V2 region did not result in eliciting anti-MPER antibodies in mice or rabbits. 2F5 bound to the Graft1 antigen consisting of 2F5 and 4E10 epitopes engrafted into the immunogenic V1/V2 region of gp120 much more weakly than to gp41 suggesting that the 2F5 epitope might be hidden or folded incorrectly in this construct.
Law2007
(vaccine antigen design)
-
2F5: This review describes the effectiveness of the current HIV-1 immunogens in eliciting neutralizing antibody responses to different clades of HIV-1. It also summarizes different evasion and antibody escape mechanisms, as well as the most potent neutralizing MAbs and their properties. MAbs reviewed in this article are: 2G12, IgG1b12, 2F5, 4E10, A32, 447-52D and, briefly, D50. Novel immunogen design strategies are also discussed.
Haynes2006a
(antibody binding site, neutralization, escape, review, subtype comparisons, structure)
-
2F5: This review summarizes current knowledge of HIV-1 lipid-protein interactions and antibodies to liposomal phospholipids and cholesterol. A potential use of Abs to lipids to neutralize HIV-1 and a potential role of the broadly neutralizing HIV-1 Abs, mainly 2F5 and 4E10, in binding to phospholipids is discussed.
Alving2006
(antibody binding site, neutralization, review)
-
2F5: The gp140δCFI protein of CON-S M group consensus protein and gp140CFI and gp140CF proteins of CON6 and WT viruses from HIV-1 subtypes A, B and C were expressed in recombinant vaccinia viruses and tested as immunogens in guinea pigs. 2F5 was shown to bind specifically to CON6, CON-S and subtype B recombinant proteins but not to subtype A and C recombinant proteins or to the two subtype B gp120 proteins. The specific binding of 2F5 to CON-S indicated that its conformational epitope was intact.
Liao2006
(antibody binding site, vaccine antigen design, subtype comparisons)
-
2F5: Viruses from 304 days and at 643 days (time of death) post-infection of a macaque infected with SHIV SF162P4 were resistant to contemporaneous serum that had broadly reactive NAbs. While resistance to anti-V3, b12, and anti-V1 MAbs developed over time, viruses remained sensitive to 2F5 and 2G12.
Kraft2007
(neutralization, escape)
-
2F5: Binding of 2F5 to gp41 was not significantly affected by the small molecule HIV-1 entry inhibitor IC9564. IC9564 induces conformational change of gp120 to allow CD4i antibody 17b to bind, but inhibits CD4-induced gp41 conformational changes.
Huang2007
(antibody binding site)
-
2F5: Using synchronously infected cell cultures, the binding of b12, 2F5 and 2G12 to the cell-free virus interferes with a step of infection subsequent to cell attachment. HIV escape from b12 occurred 30 and 10 min before escape from 2F5 for IIIB infection of HeLa cells and JRFL infection of Cf2Th-CD4/CCR5 cells, respectively, indicating that neutralization efficiency is determined by the time frames during which Ab can bind to the receptor-activated envelope proteins during the entry phase. 2F5 neutralization was enhanced by a decreasing the rate of coreceptor CXCR4 engagement, presumably by increasing the time the CD4 bound Env was available and slowing viral entry kinetics.
Haim2007
(co-receptor, kinetics)
-
2F5: Kinetics experiments of 2F5 binding to MPER region during viral fusion showed that the 2F5 kinetics resembled those of the six-helix bundle formation and fusion blocker C34, indicating that the function of MPER in the fusion cascade is still in effect at a late stage in the fusion reaction. Binding of 2F5 was shown to decrease upon triggering HIV-1 Env-expressing cells with appropriate target cells and addition of C34 did not counteract this loss, suggesting that changes in exposure of MPER occur independently of the six-helix bundle formation.
Dimitrov2007
(antibody binding site, neutralization, kinetics, binding affinity)
-
2F5: Chimeric SIV viruses containing 2F5 and 4E10 epitopes were not neutralized by broadly neutralizing sera from two clade B and one clade A infected asymptomatic individuals, indicating that MPER NAb epitopes did not account for the broad neutralizing activity observed.
Dhillon2007
(antibody binding site, neutralization)
-
2F5: SOSIP Env proteins are modified by the introduction of a disulfide bond between gp120 and gp41 (SOS), and an I559P (IP) substitution in gp41, and form trimers. The KNH1144 subtype A virus formed more stable trimers than did the prototype subtype B SOSIP Env, JRFL. The stability of gp140 trimers was increased for JR-FL and Ba-L SOSIP proteins by substituting the five amino acid residues in the N-terminal region of gp41 with corresponding residues from KNH1144 virus. b12, 2G12, 2F5, 4E10 and CD4-IgG2 all bound similarly to the WT and to the stabilized JRFL SOSIP timers, suggesting that the trimer-stabilizing substitutions do not impair the overall antigenic structure of gp140 trimers.
Dey2007
(vaccine antigen design)
-
2F5: 2F5, 4E10, and m46 neutralization was more potent when tested in a HeLa cell line expressing low CCR5 than in a HeLa cell line expressing high CCR5 levels. PBMC tend to have low CCR5 expression.
Choudhry2007
(assay or method development, co-receptor, neutralization)
-
2F5: 7/15 and 9/15 subtype A HIV-1 envelopes from samples taken early in infection were neutralized by MAbs 4E10 and 2F5, respectively, and the potency was generally modest. Mutational patterns in the MAb binding sites did not readily explain the observed patterns of sensitivity and resistance.
Blish2007
(neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
-
2F5: The autoantibody nature of the two membrane proximal HIV-1 neutralizing antibodies, 2F5 and 4E10, was evaluated by comparison to human anti-cardiolipin MAbs derived from a primary antiphospholipid syndrome patient. Both 2F5 and 4E10 bound specifically to cardiolipin. CDR3 sequence similarities between 2F5, 4E10 and anti-cardiolipin MAbs were observed. Both 2F5 and 4E10 binding to the peptide-lipid conjugate was best fit by a two-step conformational change model. These results suggest that these MAbs share binding and structural similarities with human autoantibodies and their induction by vaccines or natural infection therefore might be limited by immune tolerance mechanisms.
Alam2007
(antibody sequence)
-
2F5: Four consensus B Env constructs: full length gp160, uncleaved gp160, truncated gp145, and N-linked glycosylation-site deleted (gp160-201N/S) were compared. All were packaged into virions, and all but the fusion defective uncleaved version mediated infection using the CCR5 co-receptor. Primary isolate Envs varied between completely resistant or somewhat sensitive to neutralization by membrane proximal Nabs 4E10 and 2F5. The most sensitive Con B construct was the truncated version of Con B Env with a stop codon immediately following the membrane spanning domain, suggesting that truncation of the gp41 cytoplasmic domain facilitates greater accessibility of the MPER region. The Con B gp160 was quite resistant, and the gp160-201N/S more sensitive, to 4E10 and 2F5.
Kothe2007
(vaccine antigen design, variant cross-reactivity)
-
2F5: Newborn macaques were challenged orally with the highly pathogenic SHIV89.6P and then treated intravenously with a combination of IgG1b12, 2G12, 2F5 and 4E10 one and 12 hours post-virus exposure. All control animals became highly viremic and developed AIDS. In the group treated with mAbs 1 hour post-virus exposure, 3/4 animals were protected from persistent systemic infection and one was protected from disease. In the group treated with mAbs 12 hour post-virus exposure, one animal was protected from persistent systemic infection and disease was prevented or delayed in two animals. IgG1b12, 2G12, and 4E10 were also given 24 hours after exposure in a separate study; 4/4 treated animals become viremic, but with delayed and lower peak viremia relative to controls. 3/4 treated animals did not get AIDS during the follow up period, and 1 showed a delayed progression to AIDS, while the 4 untreated animals died of AIDS. Thus the success of passive immunization with NAbs depends on the time window between virus exposure and the start of immunoprophylaxis.
Ferrantelli2007
(immunoprophylaxis)
-
2F5: Ab titers to the 2F5 binding peptide ELDKWA were tested by peptide ELISA in sera from Thais infected with CRF01 virus who were asymptomatic versus those who had AIDS, and antibody titers were found to be significantly lower in AIDS patients. The frequency of recognition of this peptide was low overall (15-35%) in CRF01 infections, as well as infections with clades A-G.
Srisurapanon2005
(variant cross-reactivity, subtype comparisons, rate of progression)
-
2F5: A peptide FLAG tag was inserted into the V4 loop of YU-2, a neutralization resistant variant with a short V4 loop. IgG1b12 and 2F5 could neutralize both the WT YU-2 and the modified variant. The high diversity of V4 suggests it does not play a direct role in receptor binding or viral entry, yet M2, an anti-FLAG antibody, neutralized the modified virus, demonstrating that neutralizing activity doesn't have to block functionality of the virus.
Ren2005
(neutralization)
-
2F5: A multi-epitope ELDKWA/ELDEWA string in a glutathione S-transferase (GST) backbone elicited Abs in mice and rabbits that could bind to gp41 carrying either the 2F5 susceptible ELDKWA variant, or the ELDEWA escape variant. Vaccinations with only the ELDKWA epitope or the ELDEWA embedded-peptide constructs yielded type specific Abs.
Wang2005
(vaccine antigen design, vaccine-induced immune responses, escape)
-
2F5: Alanine scanning mutations of the 21 amino acid region between positions 660-680 showed that only Ala substitutions in the DKW at the core of the epitope reduced binding, positions llelDKWanlwnwfdisnwlw. No single Ala mutation was resistant to both 2F4 and 4E10. Ala substitutions in 12 of the 20 positions enhanced neutralization sensitivity, LLeLdkwanLWNWFdIsnWLW.2F5 inhibits the neutralization activity of peptide T20.
Zwick2005
(antibody binding site, escape)
-
2F5: Passive immunization of 8 HIV-1 infected patients with 4E10, 2F5 and 2G12 (day 0, 4E10; days 7, 14 and 21 4E10+2G12+2F5; virus isolated on days 0 and 77) resulted in 0/8 patients with virus that escaped all three NAbs. No viruses fully escaped 2F5, although 5/8 developed a more than 2-fold increase in 2F5 IC50 concentrations at day 77. No changes in the 2F5 epitope were observed in the 77 day study period, although 3 patients had unusual 2F5 epitope sequences to start with (not A/ELDKWA but SLNNWN, ALDTWE, or KFDNWA); all viruses were susceptible to 2F5 neutralization, although to varying degrees. In a companion in vitro study, resistance to a single MAb emerged in 3-22 weeks, but triple combination resistance was slower and characterized by decreased viral fitness. In the core of the 2F5 epitope, LDKW, the L and W were completely conserved in the in vitro study, but 9/13 cases had a D->N change, 1/13 a K->N, and 1/13 a K->Q. The lack of resistance to the combination of MAbs in vivo and the reduced fitness of the escape mutants selected in vitro suggests passive immunotherapy may be of value in HIV infection.
Nakowitsch2005
(escape, immunotherapy)
-
2F5: Nine anti-gp41 bivalent Fabs that interacted with either or both of the 6-helix bundle and the internal coiled-coil of N-helices of gp41 were selected from a non-immune human phage display library. The IC50 range for the inhibition of LAV ENV-mediated cell-fusion was 6-61 ug/ml. For context, 2F5 and 2G12 (IC50s of 0.5-1.5 ug/ml) were about an order of magnitude more potent in this assay than the best Fabs generated here.
Louis2005
(neutralization)
-
2F5: This study is about the V2 MAb C108g, that is type-specific and neutralizes BaL and HXB2. JR-FL is a neutralization resistant strain; modification of JRFL at V2 positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The modification in V2 also increased neutralization sensitivity to V3 MABs 4117c, 2219, 2191, and 447-52D, but only had minor effects on neutralization by CD4BS MAb 5145A, and broadly neutralizing MAbs IgG1b12, 2G12, and 2F5.
Pinter2005
(antibody binding site)
-
2F5: gp41 and p15E of the porcine endogenous retrovirus (PERV) share structural and functional similarities, and epitopes in the membrane proximal region of p15E are able to elicit NAbs upon immunization with soluble p15E. Rabbits immunized with a VSV recombinant expressing an HIV-1 membrane-proximal external region (MPER) fused to PERV p15E, with a fusion p15E-HIV MPER protein boost, elicited HIV specific NAbs. The MPER contains the 2F5 epitope, and the 2F5 MAb was used as a positive control for neutralization in this study, and could bind to the vaccine construct.
Luo2006
(vaccine antigen design)
-
2F5: A peptide containing eight copies of the ELDKWA-epitope separated by aa spacers GSGGGGS, RS, and GS was used to test the impact of spacers on eliciting antibody responses to peptides. Both GSGGGGS and GS induced high titers of ELDKWA peptide-specific Abs in BALB/c mice, which reacted with rsgp41. 2F5 served as a positive control in a Western Blot to determine whether epitope-specific Abs bound to recombinant protein rsgp41.
Liu2005a
(vaccine antigen design, vaccine-induced immune responses)
-
2F5: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B V3s. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. Neutralization by Cameroonian sera MAbs was blocked by Clade A and B V3 loop fusion proteins, while NAbs to non-V3 epitopes, 2F5, 2G12, and b12, were not blocked.
Krachmarov2005
(antibody binding site, variant cross-reactivity, subtype comparisons)
-
2F5: In an attempt to elicit 2F5-like antibodies, the 2F5 epitope ELDKWAS was constrained in the beta-turn sites of the immunoglobulin heavy chain, or alternatively was attached at the C-terminal ends of the immunoglobulin light chain. The constrained heavy chain inserted epitopes bound to 2F5 with 10-fold higher affinity than the light chain unconstrained versions, and when used as an immunogen, elicited epitope-specific antibodies in rabbits, but these antibodies could not neutralize the virus.
Ho2005
(vaccine antigen design, vaccine-induced immune responses)
-
2F5:2F5 and 4E10 both bind to membrane proximal regions of gp41, and have long hydrophobic CDR3 regions characteristic of polyspecific autoreactive antibodies. Of 35 Env-specific MAbs tested, only 2F5 and 4E10 were reactive with phospholipid cardiolipin. Vaccine induction of antibodies that react with these gp41 membrane proximal regions may be rare because of elimination due to autoantigen mimicry. 2F5 also reacted with centromere B and histone autoantigens, and both 4E10 and 2F5 reacted with HEp-2 cells with diffuse cytoplasmic and nuclear patterns indicating polyspecific autoreactivity.
Haynes2005
(antibody binding site)
-
2F5: Guinea pigs were immunized with a hybrid HXB2/BaL Env (HIV HXB/BaL gp140δCFI, clade B) in which the tip of the V3 loop (GPGRA) was replaced with the 2F5 epitope LELDKWAS. 2F5 bound to the Env that carried the V3-replacement 2F5 epitope, but antibodies against this construct only neutralized the X4-tropic lab adapted HIV strain IIIB, and not CCR5-HIV BaL or SF162 isolates.
Chakrabarti2005
(vaccine antigen design, variant cross-reactivity)
-
2F5: 2F5 recognizes the epitope ELDKWA, but does not neutralize viruses carrying the commonly found mutated epitope variants: ELDeWA, ELDsWA, ELDnWA, ELDqWA, ELDtWA, or ELnKWA. Peptide cocktails containing ELDKWA, ELnKWA, ELDeWk, and ELeKWA elicit polyclonal antibodies in rabbits that can bind to all of the natural variants that are escape variants for 2F5 expressed in gp41 via Western blotting, as well as ELDrWA.
Dong2005
(vaccine antigen design, variant cross-reactivity, escape)
-
2F5: Circular dichroism and NMR were used to analyze the structure of the HIV-1 inhibitor peptide T-20 (gp41 HXB2 aa 638-673) that contains the full 2F5 and partial 4E10 epitope. T-20 was unstructured towards the N terminus, and helical in the central and C-terminal regions. The 2F5 epitope sequence (gp41 HXB2 657-670) forms an intrinsic helical structure, which is stable in water.
Biron2005
(structure)
-
2F5: This review summarizes properties of 2F5 and its binding to the prefusogenic membrane proximal region of gp41. The linear core epitope does not stimulate cross-reactive NAbs when placed outside the context of gp41, suggesting its presentation in a highly specific molecular framework is critical.
McGaughey2004
(vaccine antigen design, review)
-
2F5: Infusions of 2F5 and 2G12 intravenously administered 24h prior to vaginal SHIV-89.P challenge are able to protect macaques from infections. Animals that receive a IL-2 adjuvanted DNA immunization SIV Gag and HIV Env have T-cell responses and lower viral loads, but were not protected. Suboptimal levels of 2F5 and 2G12 were not able to confer sterile protection in combination with the T-cell responses stimulated by DNA immunizations.
Mascola2003
(adjuvant comparison, vaccine-induced immune responses)
-
2F5: Nabs against HIV-1 M group isolates were tested for their ability to neutralize 6 randomly selected HIV-1 O group strains. IgG1b12 could neutralize some O group strains when used on its own, and quadruple combination of b12, 2F5, 2G12, and 4E10, could neutralize the six Group O viruses tested between 62-97%. The 2F5 epitope in the O group viruses was : ELDEWA.
Ferrantelli2004a
(variant cross-reactivity)
-
2F5: Neonatal rhesus macaques were exposed orally to a pathogenic SHIV, 89.6P. 4/8 were given an intramuscular, passive immunization consisting of NAbs 2G12, 2F5 and 4E10, each given at a different body sites at 40 mg/kg per Ab, at one hour and again at 8 days after exposure to 89.6P. The four animals that were untreated all died with a mean survival time of 5.5 weeks, the four animals that got the NAb combination were protected from infection. This model suggests antibodies may be protective against mother-to-infant transmission of HIV.
Ferrantelli2004
(mother-to-infant transmission)
-
2F5: Env sequences were derived from 4 men at primary infection and four years later; the antigenicity in terms of the ability to bind to 2G12, 2F5 and IgG1b12 was determined. 2G12 bound primarily to late clones in 3 of the 4 patients, and to both early and late in the other patient. Neither 2F5 nor IgG1b12 showed a difference in binding affinity to early or late envelopes.
Dacheux2004
(antibody binding site, acute/early infection, kinetics)
-
2F5: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. 2F5 was cross-reactive with A, B, and E subtype viruses, some D, and no C clade viruses. DKW was defined as the core motif, and was found in only 25% of C clade sequences in the database. It was found in C clade viruses in a country specific manner -- common in Burundi, Brazil and Ethiopia, rare in Botswana, India, and S. Africa. The potency of the neutralizing activity was somewhat context-dependent. DQW is a common D clade variant from Uganda, and all D viruses in this study were Ugandan.
Binley2004
(variant cross-reactivity, subtype comparisons)
-
2F5: 2F5 was used for screening of phage-displayed peptide libraries. 2F5 requires the DKW core for synthetic and phage-displayed peptide recognition, but is multispecific for amino acid residues flanking C-terminally the DKW core epitope. Three clones from the AADKW-X12 library had high affinity for 2F5, but did not share obvious homology with gp41 or each other; Ala substitution showed each bound to 2F5 with a different mechanism.
Menendez2004
(antibody binding site, mimotopes)
-
2F5: This review discusses research presented at the Ghent Workshop of prevention of breast milk transmission and immunoprophylaxis for HIV-1 in pediatrics (Seattle, Oct. 2002), and makes the case for developing passive or active immunoprophylaxis in neonates to prevent mother-to-infant transmission. Macaque studies have shown that passive transfer of NAb combinations (for example, IgG1b12, 2G12, 2F5, and 4E10; or 2G12 and 2F5) can confer partial or complete protection to infant macaques from subsequent oral SHIV challenge.
Safrit2004
(immunoprophylaxis, mother-to-infant transmission)
-
2F5: A primary isolate, CC1/85, was passaged 19 times in PBMC and gradually acquired increased sensitivity to FAb b12 and sCD4 that was attributed to changes in the V1V2 loop region, in particular the loss of a potential glycosylation site. The affinity for sCD4 was unchanged in the monomer, suggesting that the structural impact of the change was manifested at the level of the trimer. The passaged virus, CCcon19, retained an R5 phenotype and its neutralization susceptibility to other Abs was essentially the same as CC1/85. The IC50 for 2F5 was greater than 50 for CC1/85, and was 35 for CCcon19, so the passaged virus was weakly neutralized by 2F5.
Pugach2004
(variant cross-reactivity, viral fitness and/or reversion)
-
2F5: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neutralization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype.
Pinter2004
(variant cross-reactivity)
-
2F5: An antigen panel representing different regions of gp41 was generated, and sera from 23 individuals were screened. Anti-gp41 titers were very high, and sera bound to many regions of gp41, there were no immunologically silent regions. Many individuals had broad responses to diverse regions. High titer responses tended to focus on the N-heptad, C-heptad and 2F5-4E10 regions, but there was no correlation between neutralization capacity of sera and the particular peptides recognized. 2F5 responded to the four antigens that carried the minimal EDLKWA epitope. 2F5 did not bind to the minimal epitope embedded in an alpha helix, supporting that the 2F5 conformation of EDLKWA is embedded in a beta sheet. 2F5 bound better to a synthetic peptide containing the proximal regions than to the native gp41.
Opalka2004
(assay or method development)
-
2F5: A set of HIV-1 chimeras that altered V3 net charge and glycosylation patterns in V1V2 and V3, involving inserting V1V2 loops from a late stage primary isolate taken after the R5 to X4 switch, were studied with regard to phenotype, co-receptor usage, and MAb neutralization. The loops were cloned into a HXB2 envelope with a LAI viral backbone. It was observed that the addition of the late-stage isolate V1V2 region and the loss of V3-linked glycosylation site in the context of high positive charge gave an X4 phenotype. R5X4, R5, and X4 viruses were generated, and sCD4, 2G12 and b12 neutralization resistance patterns were modified by addition of the late stage V1V2, glycosylation changes, and charge in concert, while neutralization by 2F5 was unaffected.
Nabatov2004
(antibody binding site, co-receptor)
-
2F5: Sera from two HIV+ people and a panel of MAbs were used to explore susceptibility to neutralization in the presence or absence of glycans within or adjacent to the V3 loop and within the C2, C4 and V5 regions of HIV-1 SF162 env gp120. The loss of the glycan within the V3 loop (GM299 V3) and adjacent to the C-terminal end of the V3 loop (GM329 C3) did not alter neutralization susceptibility to 2F5, but the loss of glycans in C2 (GM292 C2), C4 (GM438 C4), or V5 (GM454 V5) increased 2F5 neutralization susceptibility. V3 glycans tended to shield V3 loop, CD4 and co-receptor MAb binding sites, while C4 and V5 glycans shielded V3 loop, CD4, gp41 but not co-receptor MAb binding sites. Selective removal of glycans from a vaccine candidate may enable greater access to neutralization susceptible epitopes.
McCaffrey2004
(antibody binding site, vaccine antigen design)
-
2F5: Mice susceptible to MV infection were intraperitoneally immunized with native HIV-1 89.6 env gp160 and gp140 and δV3 HIV-1 89.6 mutants expressed in live attenuated Schwarz measles vector (MV). The gp160ΔV3 construct raised more cross-reactive NAbs to primary isolates. The constructs had an additional 2F5 MAb epitope, ELDKWAS, but responses were not directed towards this epitope. A HIVIG/2F5/2G12 combination was used as a positive control and could neutralize all isolates.
Lorin2004
(vaccine antigen design)
-
2F5: The role of serine proteases on HIV infection was explored. Trypsin decreased the binding of most Env MAb tested and diminished cell fusion of H9 cells infected with HIV-1 LAI virus (H9/IIIB) to MAGI cells. In contrast, thrombin increased the binding of MAbs to gp120 epitopes near the CD4 and CCR5 binding sites, and increased cell fusion. Binding of 17b and F105 was decreased by trypsin, but increased by thrombin. gp41 MAbs 246D, 98.6, 50-69, were decreased by trypsin, unaltered by thrombin, while NAb 2F5 binding was increased by thrombin. Thrombin may increase HIV-induced cell fusion in blood by causing a conformational activating shift in gp120.
Ling2004
(antibody binding site)
-
2F5: 2F5 was used as a positive control in a study that showed that A32-rgp120 complexes open up the CCR5 co-receptor binding site, but did not induce neutralizing antibodies with greater breadth among B subtype isolates than did uncomplexed rgp120 in vaccinated guinea pigs.
Liao2004
-
2F5: A set of oligomeric envelope proteins were made from six primary isolates for potential use as vaccine antigens: 92/UG/037 (clade A), HAN2/2 (clade B), 92/BR25/025 (clade C), 92/UG/021 (clade D), 93/BR/029 (clade F) and MVP5180 (clade O). This was one of a panel of MAbs used to explore folding and exposure of well characterized epitopes. The clade C isolate BR25 is apparently misfolded, as conformation-dependent antibodies did not bind to it. 2F5 bound to clade A, B, D and F HIV-1 primary isolates. Polyclonal sera raised in rabbits against these antigens cross-bound the other antigens, but none of the sera had neutralizing activity.
Jeffs2004
-
2F5: This paper reviews MAbs that bind to HIV-1 Env. 2F5 binds to a region of gp41 proximal to cluster II (aa 662-676), neighboring the binding site of the broadly neutralizing MAb 4E10 and of neutralizing Fab Z13. 2F5 is broadly neutralizing.
Gorny2003
(review)
-
2F5: The MAb 2F5 binds to the C-heptad and is neutralizing, but the MAb D50 binds to the C-heptad and is not neutralizing. 2F5 binds preferentially to native gp41 prior to receptor activation. D50 prefers the triggered form after receptor activation. Trapped fusion-intermediates suggest 2F5 remains present shortly after gp120 triggering by CD4, but may be lost by the time the six-helix bundle is formed. D50 binds equally to the fusion-intermediate and six-helix bundle. 2F5 neutralization seems to block a later step of the fusion process, but it does not inhibit binding of NC-1, a MAb specific for the six-helix bundle, so it does not prevent formation of the six-helix bundle. The results are most consistent with 2F5 inhibiting a post-fusion-intermediate step.
deRosny2004
(antibody binding site, antibody interactions)
-
2F5: The broadly neutralizing antibodies 2F5 and 2G12 were class-switched from IgG to IgA and IgM isotypes. Neutralizing potency was increased with valence for 2G12 so the IgM form was most potent, but for 2F5 the IgG form was most potent. Eight primary isolates were tested including two subtype A isolates. The polymeric IgM and IgA Abs, but not the corresponding IgGs, could interfere with HIV-1 entry across a mucosal epithelial layer, although they were limited in a standard neutralization assay. All isotypes could interact with activated human sera, presumably through complement, to inhibit HIV replication.
Wolbank2003
(complement, genital and mucosal immunity, isotype switch, variant cross-reactivity, subtype comparisons)
-
2F5: The antiviral response to intravenously administered MAbs 2F5 and 2G12 was evaluated in 7 HAART-naive asymptomatic HIV-1 infected patients during a treatment period of 28 days. MAb therapy reduced plasma HIV RNA in 3/7 patients during the treatment period, and transiently reduced viral load in two more. CD4 counts were up in 3/7 through day 28, and transiently increased in three more. Vigorous complement activation was observed after 48/56 Ab infusions. Before treatment, 2F5 neutralized isolates from five patients and no escape was observed during treatment.
Stiegler2002
(complement, variant cross-reactivity, escape, immunotherapy)
-
2F5: Env genes derived from uncultured brain biopsy samples from four HIV-1 infected patients with late-stage AIDS were compared to env genes from PBMC samples. Brain isolates did not differ in the total number or positions of N-glycosylation sites, patterns of coreceptor usage, or ability to be recognized by gp160 and gp41 MAbs. 2F5 recognized most variants from 3/4 individuals by gp41 WB; the 4th individual had the ELDKWA variant Aldkwa in all three isolates. The other single Env that was not recognized carried eldRwa.
Ohagen2003
(brain/CSF, escape)
-
2F5: AC10 is a subject who was given treatment early after infection, and had a viral rebound after cessation of therapy, which then declined to a low level. The polyclonal sera from AC10 could potently neutralize the rebound virus, and NAb escape followed with a neutralizing response against the escape variant and subsequent escape from that response. Viral loads remained low in this subject despite escape. The rebound isolate that was potently neutralized by autologous sera was not particularly neutralization sensitive, as it resisted neutralization by sCD4 and MAbs IgG1b12, 2G12 and 2F5, and was only moderately sensitive to sera from other HIV+ individuals that had high titers of NAbs to TCLA strains.
Montefiori2003
(acute/early infection, escape)
-
2F5: Cyclic peptides ELLELDKWASLW that adopt constrained beta-turn conformation of the 2F5 epitope beta-turn in the complexed crystal structure were synthesized and optimize 2F5 binding affinity. This peptide elicits high titer peptide-specific immune responses in guinea pigs that do not neutralize; the authors propose this may be the result of a short CDR3 loop in guinea pigs.
McGaughey2003
(antibody binding site, vaccine antigen design, binding affinity, structure)
-
2F5: A polyepitope vaccine was designed based on three repeats of the 2F5 core epitope ELDKWA combined with the V3 region peptide GPGRAFY. Abs raised in mice could recognize the peptides, sgp41, and CHO-WT cells that expressed HIV-1 Env on their surface.
Li2002
(vaccine antigen design)
-
2F5: MAbs IgG1b12, 2G12, 2F5 and 4E10 were tested for their ability to neutralize two primary HIV-1 clade A isolates (UG/92/031 and UG/92/037) and two primary HIV-1 clade D isolates (UG/92/001 and UG/92/005). 4E10 demonstrated the most potent cross-neutralization activity. Quadruple administration of MAbs IgG1b12, 2G12, 2F5, and 4E10 induced strong synergistic neutralization of 4 clade A isolates (UG/92/031, UG/92/037, RW/92/020 and RW/92/025) as well as 5 clade D isolates (UG/92/001,UG/9/005, /93/086/RUG/94/108, UG/94/114). The authors note this combination of 4 MAbs neutralizes primary HIV A, B, C, and D isolates.
Kitabwalla2003
(antibody interactions, immunoprophylaxis, variant cross-reactivity, mother-to-infant transmission, subtype comparisons)
-
2F5: A mouse MAb was raised against a variant of ELDKWA core epitope of the NAb 2F5, eldEwa, derived from the 2F5 neutralization resistant variant MVP5180. 2F5 does not bind to the variants eldEwa, elNkwa (B.TH.TH936705) or elEkwa, while 14D9 binds only to eldEwa and not ELDKWA. The eldEwa variant is common in the HIV-1 O group.
Huang2002
(variant cross-reactivity, subtype comparisons)
-
2F5: Review of current neutralizing antibody-based HIV vaccine candidates and strategies of vaccine design. Strategies for targeting of the epitopes for NAbs 2F5, 2G12, 4E10, b12, and Z13 are described.
Wang2003
(vaccine antigen design, review)
-
2F5: Most plasma samples of patients from early infection had NAb responses to early autologous viruses, and NAbs against heterologous strains tended to be delayed. Serial plasma samples were tested against serial isolates, and neutralization escape was shown to be rapid and continuous throughout infection. Autologous neutralization-susceptible and resistant viruses from four patients were tested for susceptibility to neutralizing Ab responses using MAbs 2G12, IgG1b12 and 2F5. No correlation was established, all viruses tested were susceptible to at least one of the neutralizing MAbs. Two patients that did not have an autologous NAb response also did not evolve changes in susceptibility to these MAbs, while one patient with a pattern of autologous neutralization and escape acquired a 2G12 sensitive virus at month 6, and lost IgG1b12 sensitivity at month 21.
Richman2003
(autologous responses, acute/early infection, escape)
-
2F5: A sCD4-17b single chain chimera was made that can bind to the CD4 binding site, then bind and block co-receptor interaction. This chimeric protein is a very potent neutralizing agent, more potent than IgG1b12, 2G12 or 2F5 against Ba-L infection of CCR5-MAGI cells. It has potential for prophylaxis or therapy.
Dey2003
-
2F5: UK1-br and MACS2-br are R5 isolates derived from brain tissue samples from AIDS patients with dementia and HIV-1 encephalitis; both are neurotropic, but only UK1-br induced neuronal apoptosis and high levels of syncytium formation in macrophages. UK1-br Env had a greater affinity for CCR5 than MACS-br, and required low levels of CCR5 and CD4 for cell-to-cell fusion and single round infection. PBMC infected with UK1-br and MACS2-br virus isolates were resistant to neutralization by MAb 2G12. UK1-br was more sensitive than MACS2-br to IgG1b12, 2F5 and CD4-IgG2 neutralization. This pattern of Ab reactivity was similar to the CD4-independent variant ADA197N/K, and thought to result from conformational changes which better expose the CCR5 binding regions, although the loss of the particular N-linked glycosylation site in the V1V2 stem region of ADA was experimentally shown to not be responsible for the CD4-independent phenotype of UK1-br.
Gorry2002
(brain/CSF, co-receptor)
-
2F5: Anti-gp41 MAbs were tested in a cell-cell fusion system to investigate the antigenic changes in gp41 during binding and fusion. Cluster I and Cluster II MAbs required CD4 expression on HIV HXB2 Env expressing HeLa target cells, but not the CXCR4 co-receptor, binding to a fusion intermediate. 2F5 behaved very differently than these non-neutralizing antibodies: it bound to Env in the absence of target cells, and it was distributed evenly all over the cell surface, not localized in fusion domains. It did not interact with cells that exhibited cytoplasmic mixing. 2F5 was unusual in that it exhibited temperature dependence, and did not interact below 19 degrees C, in contrast to 2G12, M77 98-6 and IgG1b12 which bound strongly at temperatures ranging between 4-37 degrees. The authors suggest the temperature dependence of 2F5 may be due to increased flexibility of the Envelope spike at warmer temperatures facilitating epitope exposure.
Finnegan2002
(antibody binding site, kinetics)
-
2F5: A complex of the epitope peptide ELDKWAS bound to 2F5 was crystalized, and the peptide was found to interact with amino acids near the base of the very long (22 residue) CDR 3H region of the Ab. Ala substitution of the CDR H3 region confirmed the importance of these sites near the base of the H3 loop for interaction with the epitope in the context of intact gp41 as well as the peptide. A Phe at the apex of the loop was not located directly in the binding site, however binding of 2F5 to the epitope was very sensitive to non-conservative substitutions in this position (F100G, F100H, and F100R); these diminished both binding affinity and 2F5 neutralization, suggesting a role for the very long CDR 3H region. The authors suggest that particularly long CDR H3 regions may be a common feature of HIV-1 NAbs, based on the 22 residues in H3 of 2F5, the 18 H3 residues in b12, and the 22 H3 residues in X5. They express concern that because small animals like mice are unable to elicit Ab responses with such long H3s, they may be poor model systems for HIV vaccine studies.
Zwick2004a
(antibody binding site, antibody interactions, antibody sequence, structure)
-
2F5: This review discusses the importance and function of protective antibody responses in animal model studies in the context of effective vaccine development. SHIV models have shown protection using high levels of MAbs can prevent infection, and partial protection that can influence disease course can be obtained from modest levels of NAbs. SHIV challenges studies conducted with infusions of combinations of MAbs b12, 2G12, and 2F5 are reviewed.
Mascola2003a
(immunoprophylaxis, review)
-
2F5: This study investigates the effects of glycosylation inhibitors on the binding between HIV-1 gp120 and mannose-binding lectin (MBL). Mannosidase I inhibitor deoxymannojirimycin (dMM) inhibits formation of complex and hybrid N-linked saccharides and yields virus with more mannose residues. dMM added during viral production significantly enhanced the binding 2F5 and 2G12, but not IgG1b12 in a viral capture assay.
Hart2003
(antibody binding site)
-
2F5: Four newborn macaques were challenged with pathogenic SHIV 89.6 and given post exposure prophylaxis using a combination of NAbs 2F5, 2G12, 4E10 and IgG1b12. 2/4 treated animals did not show signs of infection, and 2/4 macaques maintained normal CD4+ T cell counts and had a lower delayed peak viremia compared to the controls.
Ferrantelli2003
(antibody interactions, immunoprophylaxis, mother-to-infant transmission)
-
2F5: This study examined antibody interactions, binding and neutralization with a B clade R5 isolate (92US660) and R5X4 isolate (92HT593). Abs generally bound and neutralized the R5X4 isolate better than the R5 isolate, with the exception of F240 which bound both equally well, which captured more virus than any other human MAb tested, and didn't neutralize either isolate. F240 enhanced the binding of CD4BS MAbs IgG1b12 and F105 and the gp41 MAb 2F5 for both R5X4 and R5 isolates. F240 also enhanced neutralization of the R5X4 isolate by 2F5, but had no effect on R5 virus. Anti-V3 MAb B4a1 did not impact 2F5 neutralization.
Cavacini2002
(antibody binding site, antibody interactions, co-receptor)
-
2F5: Alanine mutations were introduced into the N- and C-terminal alpha-helices of gp41 to destabilize interhelical packing interactions in order to study their inhibitory effect on viral infectivity. These mutations were shown to inhibit viral replication though affecting the conformational transition to the fusion-active form of gp41, and allow increased inhibition by gp41 peptides. 2F5 sensitivity is increased in the mutated viruses, presumably because 2F5s neutralization activity is focused on the transition to the fusion active state. No other MAb against gp41 tested, including NC-1, 50-69D, 1281, 98-6D, 246-D and F240, neutralized the parental or the fusion-deficient mutated viruses.
Follis2002
(antibody binding site)
-
2F5: The SOS mutant envelope protein introduces a covalent disulfide bond between gp120 surface and gp41 transmembrane proteins into the R5 isolate JR-FL by adding cysteines at residues 501 and 605. Pseudovirions bearing this protein bind to CD4 and co-receptor bearing cells, but do not fuse until treatment with a reducing agent, and are arrested prior to fusion after CD4 and co-receptor engagement. gp41 NAbs 2F5 and 4E10 are able to potently neutralize the SOS pseudovirion post-attachment, although 2F5 performed relatively poorly in the pre-attachment assay, a further support for previous studies that indicated it does not bind well to native Env, and may bind best after the virus is attached to cells.
Binley2003
(vaccine antigen design)
-
2F5: IgG1b12 neutralized many South African (5/8) and Malawian (4/8) clade C primary HIV-1 isolates, being more effective than 2F5 which neutralized only two Malawian and no South African isolates. 2G12 did not neutralize any of the 16 isolates.
Bures2002
(subtype comparisons)
-
2F5: NIH AIDS Research and Reference Reagent Program: 1475.
-
2F5: UK Medical Research Council AIDS reagent: ARP3063.
-
2F5: Review of NAbs that discusses mechanisms of neutralization, passive transfer of NAbs and protection in animal studies, and vaccine strategies.
Liu2002
(immunoprophylaxis, vaccine antigen design, review)
-
2F5: Review of NAbs that notes that 2F5 alone or in combination with other MAbs can protect some macaques against SHIV infection, that it is safe and well tolerated in humans, and that illustrates gp41's conformational change and exposure of the 2F5 epitope in the transient pre-hairpin form.
Ferrantelli2002
(immunoprophylaxis, review)
-
2F5: A 2F5 anti-idiotype murine MAb Ab2/3H6 was developed that blocks 2F5 binding to a synthetic epitope peptide and to gp160 in an ELISA competition assay -- Ab2/3H6 diminished the neutralizing potency of 2F5 -- Ab2/3H6 Fab fragments were capable of inducing neutralizing Abs and 2F5-epitope specific responses in immunized B6D2F1 mice.
Kunert2002
(vaccine antigen design)
-
2F5: Rhesus macaques were better protected from vaginal challenge with SHIV89.6D (MAb 2G12, 2/4; MAbs 2F5/2G12, 2/5; and HIVIG/2F5/2G12, 4/5 infected) than from intravenous challenge (MAb 2G12, 0/3; MAbs 2F5/2G12, 1/3; and HIVIG/2F5/2G12, 3/6 infected)-- the animals that were infected by vaginal challenge after Ab infusion had low or undetectable viral RNA levels and modest CD4 T-cell decline.
Mascola2002
(immunoprophylaxis)
-
2F5: HIV-1 gp160ΔCT (cytoplasmic tail-deleted) proteoliposomes (PLs) containing native, trimeric envelope glycoproteins from R5 strains YU2 and JRFL, and X4 strain HXBc2, were made in a physiologic membrane setting as candidate immunogens for HIV vaccines---2F5 bound to gp160ΔCT with a reconstituted membrane ten-fold better than the same protein on beads (except for the YU2 form that doesn't bind 2F5)---anti-CD4BS MAbs IgG1b12 and F105, A32 (C1-C4), C11 (C1-C5), and 39F (V3) MAbs bound gp160ΔCT PLs indistinguishably from gp160ΔCT expressed on the cell surface.
Grundner2002
(vaccine antigen design)
-
2F5: A series of mutational changes were introduced into the YU2 gp120 that favored different conformations -- 375 S/W seems to favor a conformation of gp120 closer to the CD4-bound state, and is readily bound by sCD4 and CD4i MAbs (17b, 48d, 49e, 21c and 23e) but binding of anti-CD4BS MAbs (F105, 15e, IgG1b12, 21h and F91 was markedly reduced -- IgG1b12 failed to neutralize this mutant, while neutralization by 2G12 was enhanced -- 2F5 did not neutralize either WT or mutant, probably due to polymorphism in the YU2 epitope -- another mutant, 423 I/P, disrupted the gp120 bridging sheet, favored a different conformation and did not bind CD4, CCR5, or CD4i antibodies, but did bind to CD4BS MAbs.
Xiang2002
-
2F5: A combination of MAbs 2F5 and 2G12 given in multiple infusions was found to be safe and well tolerated even in high doses in a phase I study of seven HIV-1 infected healthy volunteers---the median elimination half-life was 7.94 days for 2F5, and 16.48 for 2G12---no anti-2F5 or anti-2G12 IgM or IgG responses were detected---although there was some transient increases, overall plasma viral RNA levels decreased in 6/7 volunteers, by a median of 0.62 log10.
Armbruster2002
(immunotherapy)
-
2F5: Six sera from HIV-exposed uninfected individuals(EU) had IgA neutralizing activity dominated by recognition of a distinctive epitope within gp41, QARILAV -- sera of QAFILAV-immunized BALB/c mice was neutralizing with the dose-dependent behavior similar to 2F5.
Clerici2002
(HIV exposed persistently seronegative (HEPS))
-
2F5: DP178 is a peptide derived from the C-term heptad repeat of gp41 that is a potent inhibitor of viral-mediated fusion---it contains the 2F5 epitope but fails to stimulate 2F5-like NAbs upon immunization---the peptide was extended to force an increase in helicity, and the modified peptide had an increase in affinity for 2F5, but upon guinea pig immunization although high peptide-specific Ab titers were achieved the sera were incapable of viral neutralization---the authors propose that 2F5 may bind with low affinity to a maturation intermediate, which may account for its breadth and why it is hard to recreate the epitope, but also suggests that the high concentrations required for neutralization are not relevant in vivo.
Joyce2002
(antibody binding site)
-
2F5: A modified gp140 (gp140deltaCFI), with C-term mutations intended to mimic a fusion intermediate and stabilize trimer formation, retained antigenic conformational determinants as defined by binding to CD4 and to MAbs 2F5, 2G12, F105, and b12, and enhanced humoral immunity without diminishing the CTL response in mice injected with a DNA vaccine.
Chakrabarti2002
(vaccine antigen design)
-
2F5: Passive immunization of neonate macaques with a combination of F105+2G12+2F5 conferred complete protection against oral challenge with SHIV-vpu+ or -- the combination b12+2G12+2F5 conferred partial protection against SHIV89.6 -- such combinations may be useful for prophylaxis at birth and against milk born transmission -- the synergistic combination of IgG1b12, 2G12, 2F5, and 4E10 neutralized a collection of HIV clade C primary isolates.
Xu2002
(antibody interactions, immunoprophylaxis, subtype comparisons)
-
2F5: ELDKWAS was embedded into a beta-turn-like conformational site on a framework of an antibody specific for human leukocyte antigen HLA-DR -- this construct was recognized by 2F5, and is suggested as an adjuvant-independent vaccine candidate.
Ho2002
(vaccine antigen design)
-
2F5: Expanding the minimal epitope ELDKWA to an end-capped, linear nonapeptide, Ac-LELDKWASL-amide attained maximal affinity within a set of native gp41-sequence peptides -- scanning single residue substitutions confirmed that essential recognition requirements were the central DKW core sequence and the importance of the terminal Leu residues for high-affinity binding -- high specificity binding pockets at central Lys and Trp side-chains and an absolute requirement for the carboxylate group of the Asp side chain were found -- the nine residue fragment flanked by pairs of Ser and constrained by a disulfide bridge had high affinity for 2F5.
Tian2002
(antibody binding site)
-
2F5: Ab binding characteristics of SOS gp140 were tested using SPR and RIPA -- SOS gp140 is gp120-gp41 bound by a disulfide bond -- NAbs 2G12, 2F5, IgG1b12, CD4 inducible 17b, and 19b bound to SOS gp140 better than uncleaved gp140 (gp140unc) and gp120 -- non-neutralizing MAbs 2.2B (binds to gp41 in gp140unc) and 23A (binds gp120) did not bind SOS gp140 -- SOS gp140-2F5-IgG1b12 formed multiple ring structures composed of two SOS gp140 proteins bridged by two Ab molecules, while 2F5 and 2G12 formed extended chains rather than closed rings.
Schulke2002
(vaccine antigen design)
-
2F5: The fusion process was slowed by using a suboptimal temperature (31.5 C) to re-evaluate the potential of Abs targeting fusion intermediates to block HIV entry -- preincubation of E/T cells at 31.5 C enabled polyclonal anti-N-HR Ab and anti-six-helix bundle Abs to inhibit fusion, indicating six-helix bundles form prior to fusion -- the preincubation 31.5 C step did not alter the inhibitory activity of neutralizing Abs anti-gp41 2F5, or anti-gp120 2G12, IG1b12, 48d, and 17b.
GoldingH2002
-
2F5: Oligomeric gp140 (o-gp140) derived from R5 primary isolate US4 was characterized for use as a vaccine reagent -- antigen capture ELISA was used to compare the antigenicity of gp120 and o-gp140 using a panel of well characterized MAbs -- 2F5 recognized o-gp140.
Srivastava2002
(vaccine antigen design)
-
2F5: Twenty HIV clade C isolates from five different countries were susceptible to neutralization by anti-clade B MAbs in a synergistic quadruple combination of mAbs IgG1b12, 2G12, 2F5, and 4E10.
Xu2001
(antibody interactions)
-
2F5: A combination of MAbs IgG1b12, 2F5, and 2G12 was given postnatally to four neonates macaques that were then challenged with highly pathogenic SHIV89.6P -- one of the four infants remained uninfected after oral challenge, two infants had no or a delayed CD4(+) T-cell decline.
HofmannLehmann2001
(immunoprophylaxis)
-
2F5: 4E10 binds proximal to 2F5 and neutralizes primary isolates of clades A, B, C, D, and E -- viruses that were resistant to 2F5 were neutralized by 4E10 and vice versa.
Stiegler2001
(variant cross-reactivity, subtype comparisons)
-
2F5: A panel of 12 MAbs was used to identify those that could neutralize the dual-tropic primary isolate HIV-1 89.6 -- six gave significant neutralization at 2 to 10 ug/ml: 2F5, 50-69, IgG1b12, 447-52D, 2G12, and 670-D six did not have neutralizing activity: 654-D, 4.8D, 450-D, 246-D, 98-6, and 1281 -- no synergy, only additive effects were seen for pairwise combinations of MAbs, and antagonism was noted between gp41 MAbs 50-69 and 98-6, as well as 98-6 and 2F5.
Verrier2001
(antibody interactions, variant cross-reactivity)
-
2F5: A luciferase-reporter gene-expressing T-cell line was developed to facilitate neutralization and drug-sensitivity assays -- luciferase and p24 antigen neutralization titer end points were found comparable using NAb from sera from HIV+ donors, and MAbs 2F5, 2G12 and IgG1b12.
Spenlehauer2001
(assay or method development)
-
2F5: Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) in combination with proteolytic protection was used to identify the functional epitope for MAb 2F5, NEQELLELDKWASLWN, in the disulfide bond associated gp120/gp41 protein SOS-gp140 (JRFL) -- this minimal epitope is much larger than the ELDKWA core epitope previously defined by peptide ELISA, and this could help explain why ELDKWA-peptides are poor immunogens in terms of eliciting a 2F5-like antibody response.
Parker2001
(antibody binding site)
-
2F5: Neutralizing synergy between MAbs 1b12, 2G12 and 2F5 was studied using surface plasmon resonance to determine the binding kinetics for these three mAbs with respect to monomeric and oligomeric env protein gp160 IIIB -- the 2G12 epitope is highly accessible on both monomeric and oligomeric Envs, 1b12 is highly accessible on monomers but not oligomers, and 2F5 on neither form -- binding of 2G12 exposes the 2F5 epitope on gp160 oligomers.
ZederLutz2001
(antibody interactions)
-
2F5: Moore and colleagues review the data concerning the lack of a clear relationship between genetic subtype and serotype -- 2F5 is considered in some detail, as it represents a rare vulnerability from the neutralizing antibody perspective, although while it is apparently linear, attempts to present the peptide to the immune system have failed to elicit neutralizing Abs.
Moore2001
(review, subtype comparisons)
-
2F5: Review of studies in macaques that have shown immune control of pathogenic SHIV viremia, improved clinical outcome, and protection, and the implications of the observations for HIV vaccines.
Mascola2001
(review)
-
2F5: Neutralization synergy between anti-HIV NAbs b12, 2G12, 2F5, and 4E10 was studied -- a classic fixed-ratio method was used, as well as a method where one Ab was fixed at a low neutralization titer and the other was varied -- using primary isolates, a two-four fold enhancement of neutralization was observed with MAb pairs, and a ten-fold enhancement with a quadruple Ab combination -- no synergy was observed with any MAb pair in the neutralization of TCLA strain HXB2.
Zwick2001c
(antibody interactions)
-
2F5: This paper primarily concerns 4E10 and Z13, MAbs that both bind proximally to the 2F5 binding site to a conserved epitope, and that neutralize some primary isolates from clades B, C, and E -- the minimal 2F5 epitope is determined to be EQELLELDKWASLW, based on screening a gp160 fragment expression library, longer than previous studies -- broadly neutralizing MAbs 2F5, IgG1b12, and 4E10 and Z13 fail to neutralize different subsets of viruses.
Zwick2001b
(antibody binding site, variant cross-reactivity, subtype comparisons)
-
2F5: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding.
York2001
(variant cross-reactivity)
-
2F5: A phage peptide library was screened with MAb 2F5, and from the peptides that bound the amino acids DKW were found to be most critical for binding -- the mimetic peptide RDWSFDRWSLSEFWL elicited a cross-reactive Ab response to gp41 when used to immunize rabbits.
Tumanova2001
-
2F5: A peptide called 5-Helix was designed that binds to the C-peptide region of gp41 -- 5-Helix is a potent inhibitor of HIV-1 entry that binds immediately COOH-terminal to the C-peptide region targeted by 5-Helix -- the conformation of the bound 2F5 epitope is a hairpin turn.
Root2001a
-
2F5: Mutations in two glycosylation sites in the V2 region of HIV-1 ADA at positions 190 and 197 (187 DNTSYRLINCNTS 199) cause the virus to become CD4-independent and able to enter cells through CCR5 alone -- these same mutations tended to increase the neutralization sensitivity of the virus, including to antibody 2F5.
Kolchinsky2001
(variant cross-reactivity)
-
2F5: ELNKWA is an escape variant not recognized by the broadly neutralizing MAb 2F5, which recognizes the core epitope ELDKWA -- Abs were raised against the peptide escape variant CGELNKWAGELNKWA linked to KLH carrier -- these polyclonal antibodies, like the monoclonal antibody TH-Ab1 also raised to ELNKWA, could recognize ELDKWA and escape mutant peptide epitopes ELEKWA and ELDEWA.
Dong2001
(variant cross-reactivity)
-
2F5: SHIV-HXBc2 is a neutralization sensitive non-pathogenic virus, and several in vivo passages through monkey's yielded highly pathogenic SHIV KU-1 -- HXBc2 and the KU-1 clone HXBc2P3.2 differ in 12 amino acids in gp160 -- substitutions in both gp120 and gp41 reduced the ability of sCD4, IgG1b12, F105 and AG1121 to Env achieve saturation and full occupancy, and neutralize KU-1 -- 17b and 2F5 also bound less efficiently to HXBc2P3.2, although 2G12 was able to bind both comparably.
Si2001
-
2F5: A combination of gp41 fusion with the GNC4 trimeric sequences and disruption of the YU2 gp120-gp41 cleavage site resulted in stable gp140 trimers (gp140-GNC4) -- gp41 MAbs T4, D12, T3, and D50 bound less efficiently to gp140-GNC4 than did pooled sera, but T4 and D12 recognized the gp140-GNC4 timer equivalently to gp140(-), and T3 and D50 recognized the trimer at greater levels than gp140(-) -- 2F5 did not bind efficiently to these constructs, presumably because of the YU2 strain has a substitution in the 2F5 epitope (ALDKWA instead of ELDKWA).
Yang2000
(vaccine antigen design, variant cross-reactivity)
-
2F5: 2F5 or sCD4-IgG chimeric immunoadhesin were transferred into 3T3 cells, incorporated into a collagen structure called the neo-organ, and transplanted into SCIDhu mice that were then challenged with MN or LAI -- the continuous production of the therapeutic molecules in this context resulted in dramatic reduction of viral load.
Sanhadji2000
(immunotherapy)
-
2F5: ELDKWAS co-crystallized bound to the Fab' 2F5 fragment showed the epitope peptide in a type I beta-turn conformation.
Pai2002
(structure)
-
2F5: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 6 cluster II anti-gp41 MAbs -- of these 2F5, 167-D, 126-6, and 1281 bound across clades, but usually weakly, while 98-6 and 1342 had poor cross reactivity -- Clade D isolates bound most consistently to cluster II MAbs.
Nyambi2000
(subtype comparisons)
-
2F5: ELDKWA peptide vaccine study.
Lu2000b
(vaccine antigen design)
-
2F5: ELDKWA peptide vaccine study.
Lu2000a
(vaccine antigen design)
-
2F5: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain.
Zhang2002
-
2F5: Low levels of anti-ELDKWA antibodies are observed in HIV-1+ individuals, so a C-domain P2 peptide linked to a carrier was used to immunize mice and rabbits, and stimulated a high-level anti-ELDKWA response.
Liao2000
(vaccine antigen design)
-
2F5: 2F5 is a candidate for immunotherapy, but generally IgG1 has a longer half-life in humans than IgG3, so the isotype was switched -- rec CHO-derived MAb 2F5 IgG1kappa and hybridoma-derived MAb 2F5 IgG3kappa displayed identical specificity, in vitro function, and epitope (ELDKWA) -- it remains to be determined if isotype switching will prolongs beta-clearance.
Kunert2000
(immunotherapy)
-
2F5: MAbs 98-6 and 2F5 both bind to a peptide N51-C43 complex trimer of heterodimers that approximates the core of the fusogenic form of gp41, and to C43 alone but not to N51 alone -- 98-6 and 2F5 have comparable affinities for C43, but 98-6 has a higher affinity for the complex and 2F5 may bind to an epitope of C43 that is directly involved with complex formation --and IgG1 rec form of the Ab was used in this study.
Gorny2000a
(antibody binding site)
-
2F5: A mini-review of observations of passive administration of IgG NAbs conferring protection against intervenous or vaginal SHIV challenge, that considers why IgG MAbs might protect against mucosal challenge. Database note: First author "RobertGuroff" is also found as "Robert-Guroff" on annotated papers in this database.
RobertGuroff2000
(review)
-
2F5: Paper uses IgG1 form of 2F5 -- a triple combination of 2F5, F105 and 2G12 effectively neutralized perinatal infection of macaque infants when challenged with SHIV-vpu+ -- the plasma half-life was 4.2 +/- 0.8 days.
Baba2000
(immunoprophylaxis)
-
2F5: Because HIV-1 is most often transmitted across mucosal surfaces, the ability of passive transfer of infused HIVIG/2F5/2G12 to protect against mucosal exposure of macaques to pathogenic SHIV 89.6PD was studied -- HIVIG/2F5/2G12 protected 4/5 animals against vaginal challenge, 2F5/2G12 combined protected 2/5 animals, and 2G12 alone protected 2/4 animals -- in contrast, Mascola and co-workers had previously shown single MAbs could not protect against intervenous challenge -- Ab treated animals that got infected through vaginal inoculation had low viral loads and only modest declines in CD4 counts -- the infused Abs were detected in the nasal, vaginal, and oral mucosa.
Mascola2000a
(genital and mucosal immunity, immunoprophylaxis)
-
2F5: Combinations of HIVIG, 2F5, 2G12 were administered in passive-transfer experiments 24 hours prior to challenge with pathogenic SHIV 89.6PD -- 3/6 animals given HIVIG/2F5/2G12 were completely protected, the others had reduced viremia and normal CD4 counts -- 1/3 monkeys given 2F5/2G12 showed transient infection, the other two had reduced viral load -- all monkeys that received HIVIG, 2F5, or 2G12 alone became infected and developed high-level plasma viremia, although animals that got HIVIG or 2G12 had a less profound CD4 T cell decline.
Mascola1999
(immunoprophylaxis)
-
2F5: Review of the neutralizing Ab response to HIV-1.
Parren1999
(review)
-
2F5: In a study of 116 HIV-1+ individuals, Ab reactivity to a peptide encompassing the ELDKWA peptide decreased in CDC stage C patients compared with stage A patients, and longitudinal studies showed a decline in 6/8 patients, while overall Ab reactivity to rec soluble gp160 stayed constant.
Muhlbacher1999
-
2F5: Hu-PBL-SCID mice were infected with HIV-1s JRCSF and SF162 to study the effect of NAbs on an established infection -- no significant differences in the initial rate of decrease in viral load or the plateau levels of viral RNA between the b12 treated and control mice were seen -- in most of the Ab treated mice b12 escape mutants were observed with varying patterns of mutations -- a combination of b12, 2G12 and 2F5 protected 1/3 mice, and an isolate from one of the other two was resistant to neutralization by all three MAbs.
Poignard1999
(immunotherapy)
-
2F5: A meeting summary presented results regarding neutralization --MAbs 2G12 and 2F5 tested for their ability to neutralize primary isolate infection of genetically engineered cell lines (cMAGI and others, presented by T. Matthews, A. Trkola, J. Bradac) -- an advantage of such cells lines over PBMCs is that markers (X-Gal) can be added for staining to simplify the assay -- the consensus of the meeting was that these engineered cell lines did not improve the sensitivity of detection of primary isolate neutralization -- D. Burton and J. Mascola presented results concerning passive immunization and protection of hu-PBL-SCID mice and macaques, respectively, and both found combinations of MAbs that were able to achieve 99% neutralization in vitro corresponded to efficacy in vivo.
Montefiori1999
(review)
-
2F5: rgp120 derived from a R5X4 subtype B virus was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs.
Beddows1999
-
2F5: Infection of dendritic cells cultured from CD14+ blood cells or from cadaveric human skin was blocked by neutralizing MAbs IgG1b12, or 2F5 and 2G12 delivered together, but not by control non-neutralizing anti-gp120 MAb 4.8D, indicating that NAbs could interrupt early mucosal transmission events.
Frankel1998
(genital and mucosal immunity)
-
2F5: The complete V, J and D(H) domain was sequenced -- unlike non-neutralizing anti-gp41 MAb 3D6, five neutralizing MAbs (2F5, 2G12, 1B1, 1F7, and 3D5) showed extensive somatic mutations giving evidence of persistent antigenic pressure over long periods -- in contrast to Geffin98, where multiple pediatric sera were found to compete with 2F5, cross-competition was noted to be very rare in sera from HIV+ adults -- Kunert et al. propose that because there is a binding site of human complement factor H which overlaps the 2F5 binding site, it may generally be masked from the immune system -- 2F5 also has a remarkably long CDR3 loop of 22 amino acids, and this region could not be readily assigned to any described D(H) fragment, leading to the suggestion of recombination of two fragments from novel regions.
Kunert1998
(antibody sequence)
-
2F5: The natural immune response to the epitope of 2F5, ELDKWA, was studied in perinatally infected children and levels of reactivity to this epitope were correlated with absolute CD4 numbers over time and health status -- 3/10 children who had no antibody reactivity to ELDKWA had substitutions in the epitope (ALDKWA, ELDQWA, and KLDKWA) -- 2F5 competed with the ELDKWA-reactive sera depending on the serum titer.
Geffin1998
-
2F5: MAbs 2G12, 2F5 and b12 are broadly neutralizing, as are some human polyconal sera, but this paper describes a set of primary isolates that are resistant to all three MAbs and 2 broadly neutralizing sera -- results indicate that resistance levels of pediatric isolates might be higher than adult isolates -- resistance in general did not seem to be conferred by a loss of binding affinity for gp120 or gp41, rather by a more global perturbation of oligomeric Envelope.
Parren1998a
(variant cross-reactivity)
-
2F5: Used as a control in the study of anti-gp41 MAb NC-1 -- 2F5 does not react with HIV-2 gp41 or gp160.
Jiang1998
(variant cross-reactivity)
-
2F5: Neutralization synergy was observed when the MAbs 694/98-D (V3), 2F5 (gp41), and 2G12 (gp120 discontinuous) were used in combination, and even greater neutralizing potential was seen with the addition of a fourth MAb, F105 (CD4 BS).
Li1998
(antibody interactions)
-
2F5: Induces complement-mediated lysis in MN but not primary isolates -- primary isolates are refractive to CML.
Takefman1998
(complement)
-
2F5: The ELDKWA epitope was inserted into the antigenic site B of influenza hemagglutinin and expressed on baculovirus infected insect cells, flanked by 3 additional random amino acids, xELDKWAxx -- FACS was used to isolate the clone that displayed the epitope with the most markedly increased binding capacity for 2F5, to identify particularly specific immunogenic constructs -- PELDKWAPP was a high affinity form selected by FACS.
Ernst1998
(vaccine antigen design)
-
2F5: Points out that 2G12 and 2F5, potent neutralizing antibodies, were identified by screening for cell surface (oligomeric Envelope) reactivity.
Fouts1998
-
2F5: A wide range of neutralizing titers was observed that was independent of co-receptor usage -- 2F5 was the most potent of the MAbs tested.
Trkola1998
(variant cross-reactivity)
-
2F5: A neutralization assay was developed based on hemi-nested PCR amplification of the LTR (HNPCR) -- LTR-HNPCR consistently revealed HIV DNA and was shown to be a rapid, specific and reliable neutralization assay based on tests with 6 MAbs and 5 isolates.
Yang1998
(assay or method development)
-
2F5: Ab from gp120 vaccinated individuals prior to infection, who subsequently became HIV infected, could not achieve 90% neutralization of the primary virus by which the individuals were ultimately infected -- these viruses were not particularly refractive to neutralization, as determined by their susceptibility to neutralization by MAbs 2G12, IgG1b12, 2F5 and 447-52D.
Connor1998
(variant cross-reactivity)
-
2F5: This MAb and the results of Ugolini1997 are discussed -- the authors propose that an Ab bound to gp41 would typically project less from the surface of the virion and so be unable to interfere with attachment Parren1998.
Ugolini1997,Parren1998
(review)
-
2F5: Post-exposure prophylaxis was effective when MAb 694/98-D was delivered 15 min post-exposure to HIV-1 LAI in hu-PBL-SCID mice, but declined to 50% if delivered 60 min post-exposure, and similar time constraints have been observed for HIVIG, 2F5 and 2G12, in contrast to MAb BAT123 that could protect delivered 4 hours post infection.
Andrus1998
(immunoprophylaxis)
-
2F5: This review summarizes results about 2F5: it binds extracellularly, near the transmembrane domain, it is the only gp41 MAb that is neutralizing, it reacts with many non-B clade viruses and has a paradoxically weak binding to virus, given the neutralizing titers.
Burton1997
(review)
-
2F5: The only MAb out of a large panel to show no correlation between viral binding inhibition and neutralization.
Ugolini1997
-
2F5: Used to standardize polyclonal response to CD4 BS.
Turbica1997
-
2F5: Using concentrations of Abs achievable in vivo, the triple combination of 2F5, 2G12 and HIVIG was found to be synergistic to have the greatest breadth and magnitude of response against 15 clade B primary isolates.
Mascola1997
(antibody interactions, variant cross-reactivity)
-
2F5: Binding of anti-gp120 MAbs IgG1b12 or 654-30D does not mediate significant exposure of the gp41 epitopes for MAbs 2F5 and 50-69.
Stamatatos1997
(antibody interactions)
-
2F5: Review: MAbs 2F5, 2G12 and IgG1b12 have potential for use in combination with CD4-IgG2 as an immunotherapeutic or immunoprophylactic -- homologous MAbs to these are rare in humans and vaccine strategies should consider including constructs that may enhance exposure of these MAbs' epitopes.
Moore1997
(review)
-
2F5: IgG1b12 was more potent with greater breadth than MAb 2F5 in an infection reduction assay including 35 primary isolates.
Kessler1997
(variant cross-reactivity)
-
2F5: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB Env -- strong neutralizer of SHIV-vpu+ -- all Ab combinations tested showed synergistic neutralization -- 2F5 has synergistic response with MAbs 694/98-D (anti-V3), 2G12, b12, and F105.
Li1997
(antibody interactions)
-
2F5: A JRCSF variant that was selected for IgG1b12 resistance remained sensitive to MAbs 2G12 and 2F5, for combination therapy.
Mo1997
(antibody interactions)
-
2F5: In a multilab evaluation of monoclonal antibodies, only IgG1b12, 2G12, and 2F5 could neutralize at least half of the 9 primary test isolates at a concentration of < 25 mug per ml for 90% viral inhibition -- the isolates with no 2F5 neutralizing susceptibility had the sequences ALGQWA or ELDTWA instead of EDLKWA -- 7/9 primary isolates were neutralized, and ALDKWQ and ALDKWA were susceptible to neutralization.
DSouza1997
(variant cross-reactivity)
-
2F5: Of three neutralizing MAbs (257-D, IgG1b12, and 2F5), 2F5 was the only one to inhibit the entry of all viruses studied, both SI and NSI, with a potency proportional to its affinity for monomeric gp126.
Schutten1997
(variant cross-reactivity)
-
2F5: Called IAM 2F5 -- antibody mediated enhancement or inhibition seemed to be determined by isolate rather than antibody specificity -- in this study, only 2F5 inhibited the entry of all the viruses studied, irrespective of their phenotype, and directly proportional to its affinity to monomeric HIV-1 gp160.
Schutten1997
(variant cross-reactivity)
-
2F5: A panel of immunotoxins were generated by linking Env MAbs to ricin A -- immunotoxins mediated cell killing, but killing was not directly proportional to binding.
Pincus1996
(immunotoxin)
-
2F5: 2F5 was infused into two chimpanzees which were then given an intravenous challenge with a primary HIV-1 isolate -- both became infected, but with delayed detection and prolonged decrease in viral load relative to controls, indicating that preexisting, neutralizing antibodies (passively administered or actively elicited) affect the course of acute-phase virus replication and can be influential after the Ab can no longer be detected in the peripheral circulation.
Conley1996
(immunoprophylaxis)
-
2F5: Review: only four epitopes have been described which can stimulate a useful neutralizing response to a broad spectrum of primary isolates, represented by the binding sites of MAbs: 447-52-D, 2G12, Fab b12, and 2F5.
Sattentau1996
(review)
-
2F5: Review: one of three MAbs (IgG1b12, 2G12, and 2F5) generally accepted as having significant potency against primary isolates.
Poignard1996
(review)
-
2F5: Neutralizes HXB2, primary isolates, and chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
(variant cross-reactivity)
-
2F5: Primary isolates from clade A, B, and E are neutralized by 2F5 -- neutralization requires the LDKW motif -- neutralization resistant isolates or 2F5 selected variants all had substitutions in the D or K.
Purtscher1996
(subtype comparisons)
-
2F5: ELDKWAS is in a gp41 binding region for the negative regulator of complement factor H (CFH) -- Abs to HIV generally do not cause efficient complement-mediated lysis, but binding of 2F5 can interfere with CHF binding, facilitating HIV destruction by complement.
Stoiber1996
(complement)
-
2F5: Only 4/20 Argentinian and 3/43 Swedish HIV+ sera reacted with LLELDKWASL -- sera reacting with peptides that contained ELDKWA tended to have high neutralization titers -- the region carboxyl terminal to EDLKWA was found to be more important for polyclonal sera AB binding, 670-675 WNWFDI -- 2F5 bound most strongly to the peptide QELLELDKWA.
Calarota1996
(antibody binding site, variant cross-reactivity)
-
2F5: Broad cross-clade neutralization of primary isolates -- additive neutralization in combination with anti-CD4BS MAb IgG1b12 (Called BM12).
Kessler1995
(subtype comparisons)
-
2F5: MAb binding decreases the accessibility or alters the conformation of the gp41 fusion domain and of gp120 domains, including the binding site for the CD4 cell receptor.
Neurath1995
(antibody binding site)
-
2F5: Review: binds to the only generally accepted strong neutralizing epitope outside of gp120, one of only 3 MAbs with strong broad activity against primary viruses, the others are 2G12 and IgG1b12 -- unique member of epitope cluster Moore1995c and John Moore, per comm 1996.
Moore1995c
(review)
-
2F5: Called IAM 41-2F5 -- exposed in the presence of gp120 on the cell surface, while most of gp41 is masked -- binds proximal to transmembrane region.
Sattentau1995
(antibody binding site)
-
2F5: Cross-clade primary virus neutralizing activity -- LDKW defined as the core epitope.
Trkola1995a
(variant cross-reactivity, subtype comparisons)
-
2F5: Found to neutralize MN, JRCSF, and two B subtype primary isolates, but not a D subtype primary isolate, by most labs in a multi-laboratory study involving 11 labs.
DSouza1995
(variant cross-reactivity, subtype comparisons)
-
2F5: 2F5 epitope ELDKWA inserted into an immunogenic loop in influenza virus hemagglutinin can elicit IIIB, MN and RF neutralizing sera in immunized mice.
Muster1994
(vaccine antigen design)
-
2F5: gp41 mutation (582 A/T) that reduces neutralization of anti-CD4 binding site MAbs does not alter 2F5's ability to neutralize.
Thali1994
-
2F5: Called IAM-41-2F5 -- neutralized lab and primary isolates -- t 1/2 dissociation 122 min for the peptide, and 156 min for gp41 -- core D(K/R)W -- Ab resistant isolate had the sequence KLDNWA.
Conley1994a
(antibody binding site, variant cross-reactivity)
-
2F5: Included in a multi-lab study for antibody characterization binding and neutralization assay comparison.
DSouza1994
(assay or method development)
-
2F5: MAb generated by electrofusion of PBL from HIV-1 positive volunteers with CB-F7 cells.
Buchacher1994
(antibody generation)
-
2F5: Failed to show synergy with anti-CD4 binding site IIIB neutralizing antibodies.
Laal1994
(antibody interactions)
-
2F5: Broadly reactive neutralizing activity, ELDKWA is relatively conserved -- neutralized 2 primary isolates.
Purtscher1994
(neutralization)
-
2F5: Called IAM-41-2F5 -- reports MAb to be IgG1 -- the gp41 mutation 582(Ala to Thr) results in conformational changes in gp120 that confer neutralization resistance to conformationally sensitive neutralizing MAbs -- neutralization efficiency of 2F5 is not affected.
Klasse1993b
(variant cross-reactivity)
-
2F5: Synergy with combinations of CD4-based molecules in inhibition of HIV-1 Env mediated cell fusion.
Allaway1993
(antibody interactions)
-
2F5: DKWA defined as the core sequence -- highly conserved epitope neutralizing MAb.
Buchacher1992,Muster1993
(antibody binding site)
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Binley2010
James M Binley, Yih-En Andrew Ban, Emma T. Crooks, Dirk Eggink, Keiko Osawa, William R. Schief, and Rogier W. Sanders. Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization. J. Virol., 84(11):5637-5655, Jun 2010. PubMed ID: 20335257.
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Biron2005
Zohar Biron, Sanjay Khare, Sabine R. Quadt, Yehezkiel Hayek, Fred Naider, and Jacob Anglister. The 2F5 Epitope is Helical in the HIV-1 Entry Inhibitor T-20. Biochemistry, 44(41):13602-13611, 18 Oct 2005. PubMed ID: 16216084.
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Blay2007
Wendy M. Blay, Theresa Kasprzyk, Lynda Misher, Barbra A. Richardson, and Nancy L. Haigwood. Mutations in Envelope gp120 Can Impact Proteolytic Processing of the gp160 Precursor and Thereby Affect Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Pseudoviruses. J. Virol., 81(23):13037-13049, Dec 2007. PubMed ID: 17855534.
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Blish2007
Catherine A. Blish, Wendy M. Blay, Nancy L. Haigwood, and Julie Overbaugh. Transmission of HIV-1 in the Face of Neutralizing Antibodies. Curr. HIV Res., 5(6):578-587, Nov 2007. PubMed ID: 18045114.
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Blish2008
Catherine A Blish, Minh-An Nguyen, and Julie Overbaugh. Enhancing Exposure of HIV-1 Neutralization Epitopes through Mutations in gp41. PLoS Med., 5(1):e9, 3 Jan 2008. PubMed ID: 18177204.
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Blish2009
Catherine A. Blish, Zahra Jalalian-Lechak, Stephanie Rainwater, Minh-An Nguyen, Ozge C. Dogan, and Julie Overbaugh. Cross-Subtype Neutralization Sensitivity Despite Monoclonal Antibody Resistance among Early Subtype A, C, and D Envelope Variants of Human Immunodeficiency Virus Type 1. J. Virol., 83(15):7783-7788, Aug 2009. PubMed ID: 19474105.
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Bontjer2010
Ilja Bontjer, Mark Melchers, Dirk Eggink, Kathryn David, John P. Moore, Ben Berkhout, and Rogier W. Sanders. Stabilized HIV-1 Envelope Glycoprotein Trimers Lacking the V1V2 Domain, Obtained by Virus Evolution. J. Biol. Chem, 285(47):36456-36470, 19 Nov 2010. PubMed ID: 20826824.
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Borggren2011
Marie Borggren, Johanna Repits, Jasminka Sterjovski, Hannes Uchtenhagen, Melissa J. Churchill, Anders Karlsson, Jan Albert, Adnane Achour, Paul R. Gorry, Eva Maria Fenyö, and Marianne Jansson. Increased Sensitivity to Broadly Neutralizing Antibodies of End-Stage Disease R5 HIV-1 Correlates with Evolution in Env Glycosylation and Charge. PLoS One, 6(6):e20135, 2011. PubMed ID: 21698221.
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Bouvin-Pley2014
M. Bouvin-Pley, M. Morgand, L. Meyer, C. Goujard, A. Moreau, H. Mouquet, M. Nussenzweig, C. Pace, D. Ho, P. J. Bjorkman, D. Baty, P. Chames, M. Pancera, P. D. Kwong, P. Poignard, F. Barin, and M. Braibant. Drift of the HIV-1 Envelope Glycoprotein gp120 Toward Increased Neutralization Resistance over the Course of the Epidemic: A Comprehensive Study Using the Most Potent and Broadly Neutralizing Monoclonal Antibodies. J. Virol., 88(23):13910-13917, Dec 2014. PubMed ID: 25231299.
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Bradley2016a
Todd Bradley, Ashley Trama, Nancy Tumba, Elin Gray, Xiaozhi Lu, Navid Madani, Fatemeh Jahanbakhsh, Amanda Eaton, Shi-Mao Xia, Robert Parks, Krissey E. Lloyd, Laura L. Sutherland, Richard M. Scearce, Cindy M. Bowman, Susan Barnett, Salim S. Abdool-Karim, Scott D. Boyd, Bruno Melillo, Amos B. Smith, 3rd., Joseph Sodroski, Thomas B. Kepler, S. Munir Alam, Feng Gao, Mattia Bonsignori, Hua-Xin Liao, M Anthony Moody, David Montefiori, Sampa Santra, Lynn Morris, and Barton F. Haynes. Amino Acid Changes in the HIV-1 gp41 Membrane Proximal Region Control Virus Neutralization Sensitivity. EBioMedicine, 12:196-207, Oct 2016. PubMed ID: 27612593.
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Braibant2006
Martine Braibant, Sylvie Brunet, Dominique Costagliola, Christine Rouzioux, Henri Agut, Hermann Katinger, Brigitte Autran, and Francis Barin. Antibodies to Conserved Epitopes of the HIV-1 Envelope in Sera from Long-Term Non-Progressors: Prevalence and Association with Neutralizing Activity. AIDS, 20(15):1923-30, 3 Oct 2006. PubMed ID: 16988513.
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Braibant2013
Martine Braibant, Eun-Yeung Gong, Jean-Christophe Plantier, Thierry Moreau, Elodie Alessandri, François Simon, and Francis Barin. Cross-Group Neutralization of HIV-1 and Evidence for Conservation of the PG9/PG16 Epitopes within Divergent Groups. AIDS, 27(8):1239-1244, 15 May 2013. PubMed ID: 23343910.
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Bricault2019
Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920.
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Brown2005a
Bruce K. Brown, Janice M. Darden, Sodsai Tovanabutra, Tamara Oblander, Julie Frost, Eric Sanders-Buell, Mark S. de Souza, Deborah L. Birx, Francine E. McCutchan, and Victoria R. Polonis. Biologic and Genetic Characterization of a Panel of 60 Human Immunodeficiency Virus Type 1 Isolates, Representing Clades A, B, C, D, CRF01\_AE, and CRF02\_AG, for the Development and Assessment of Candidate Vaccines. J. Virol., 79(10):6089-6101, May 2005. PubMed ID: 15857994.
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Bryson2008
Steve Bryson, Jean-Philippe Julien, David E. Isenman, Renate Kunert, Hermann Katinger, and Emil F. Pai. Crystal Structure of the Complex Between the Fab' Fragment of the Cross-Neutralizing Anti-HIV-1 Antibody 2F5 and the Fab Fragment of Its Anti-Idiotypic Antibody 3H6. J. Mol. Biol., 382(4):910-919, 17 Oct 2008. PubMed ID: 18692506.
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Bryson2009
Steve Bryson, Jean-Philippe Julien, Rosemary C. Hynes, and Emil F. Pai. Crystallographic Definition of the Epitope Promiscuity of the Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5: Vaccine Design Implications. J. Virol., 83(22):11862-11875, Nov 2009. PubMed ID: 19740978.
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Buchacher1992
Andrea Buchacher, Renate Predl, Christa Tauer, Martin Purtscher, Gerhard Gruber, Renate Heider, Fraz Steindl, Alexandra Trkola, Alois Jungbauer, and Herman Katinger. Human Monoclonal Antibodies against gp41 and gp120 as Potential Agent for Passive Immunization. Vaccines, 92:191-195, 1992.
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Bunnik2007
Evelien M Bunnik, Esther D Quakkelaar, Ad C. van Nuenen, Brigitte Boeser-Nunnink, and Hanneke Schuitemaker. Increased Neutralization Sensitivity of Recently Emerged CXCR4-Using Human Immunodeficiency Virus Type 1 Strains Compared to Coexisting CCR5-Using Variants from the Same Patient. J. Virol., 81(2):525-531, Jan 2007. PubMed ID: 17079299.
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Bunnik2009
Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Ad C. van Nuenen, and Hanneke Schuitemaker. Changing Sensitivity to Broadly Neutralizing Antibodies b12, 2G12, 2F5, and 4E10 of Primary Subtype B Human Immunodeficiency Virus Type 1 Variants in the Natural Course of Infection. Virology, 390(2):348-355, 1 Aug 2009. PubMed ID: 19539340.
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Bunnik2010
Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Nening M. Nanlohy, Debbie van Baarle, Ad C. van Nuenen, Ann J. Hessell, and Hanneke Schuitemaker. Emergence of Monoclonal Antibody b12-Resistant Human Immunodeficiency Virus Type 1 Variants during Natural Infection in the Absence of Humoral Or Cellular Immune Pressure. J. Gen. Virol., 91(5):1354-1364, May 2010. PubMed ID: 20053822.
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Bunnik2010a
Evelien M. Bunnik, Zelda Euler, Matthijs R. A. Welkers, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Adaptation of HIV-1 Envelope gp120 to Humoral Immunity at a Population Level. Nat. Med., 16(9):995-997, Sep 2010. PubMed ID: 20802498.
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Bures2002
Renata Bures, Lynn Morris, Carolyn Williamson, Gita Ramjee, Mark Deers, Susan A Fiscus, Salim Abdool-Karim, and David C. Montefiori. Regional Clustering of Shared Neutralization Determinants on Primary Isolates of Clade C Human Immunodeficiency Virus Type 1 from South Africa. J. Virol., 76(5):2233-2244, Mar 2002. PubMed ID: 11836401.
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Burrer2005
Renaud Burrer, Sandrine Haessig-Einius, Anne-Marie Aubertin, and Christiane Moog. Neutralizing as Well as Non-Neutralizing Polyclonal Immunoglobulin (Ig)G from Infected Patients Capture HIV-1 via Antibodies Directed against the Principal Immunodominant Domain of gp41. Virology, 333(1):102-113, 1 Mar 2005. PubMed ID: 15708596.
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Burton1997
D. R. Burton and D. C. Montefiori. The antibody response in HIV-1 infection. AIDS, 11 Suppl A:S87-S98, 1997. An excellent review of Ab epitopes and the implications for Envelope structure, neutralization of HIV, the distinction between primary and TCLA strains, ADCC and its role in clearance, and the Ab response during the course of infection. PubMed ID: 9451972.
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Burton2005
Dennis R. Burton, Robyn L. Stanfield, and Ian A. Wilson. Antibody vs. HIV in a Clash of Evolutionary Titans. Proc. Natl. Acad. Sci. U.S.A., 102(42):14943-14948, 18 Oct 2005. PubMed ID: 16219699.
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Burton2012
Dennis R. Burton, Pascal Poignard, Robyn L. Stanfield, and Ian A. Wilson. Broadly Neutralizing Antibodies Present New Prospects to Counter Highly Antigenically Diverse Viruses. Science, 337(6091):183-186, 13 Jul 2012. PubMed ID: 22798606.
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Burton2016
Dennis R. Burton and Lars Hangartner. Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. Annu. Rev. Immunol., 34:635-659, 20 May 2016. PubMed ID: 27168247.
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Buzon2010
Victor Buzon, Ganesh Natrajan, David Schibli, Felix Campelo, Michael M. Kozlov, and Winfried Weissenhorn. Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions. PLoS Pathog, 6(5):e1000880, May 2010. PubMed ID: 20463810.
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Calarota1996
S. Calarota, M. Jansson, M. Levi, K. Broliden, O. Libonatti, H. Wigzell, and B. Wahren. Immunodominant Glycoprotein 41 Epitope Identified by Seroreactivity in HIV Type 1-Infected Individuals. AIDS Res. Hum. Retroviruses, 12:705-713, 1996. PubMed ID: 8744581.
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Cavacini2002
Lisa A. Cavacini, Mark Duval, James Robinson, and Marshall R. Posner. Interactions of Human Antibodies, Epitope Exposure, Antibody Binding and Neutralization of Primary Isolate HIV-1 Virions. AIDS, 16(18):2409-2417, 6 Dec 2002. Erratum in AIDS. 2003 Aug 15;17(12):1863. PubMed ID: 12461414.
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Chakrabarti2002
Bimal K. Chakrabarti, Wing-pui Kong, Bei-yue Wu, Zhi-Yong Yang, Jacques Friborg, Xu Ling, Steven R. King, David C. Montefiori, and Gary J. Nabel. Modifications of the Human Immunodeficiency Virus Envelope Glycoprotein Enhance Immunogenicity for Genetic Immunization. J. Virol., 76(11):5357-5368, Jun 2002. PubMed ID: 11991964.
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Chakrabarti2005
Bimal K. Chakrabarti, Xu Ling, Zhi-Yong Yang, David C. Montefiori, Amos Panet, Wing-Pui Kong, Brent Welcher, Mark K. Louder, John R. Mascola, and Gary J. Nabel. Expanded Breadth of Virus Neutralization after Immunization with a Multiclade Envelope HIV Vaccine Candidate. Vaccine, 23(26):3434-3445, 16 May 2005. PubMed ID: 15837367.
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Chakrabarti2011
B. K. Chakrabarti, L. M. Walker, J. F. Guenaga, A. Ghobbeh, P. Poignard, D. R. Burton, and R. T. Wyatt. Direct Antibody Access to the HIV-1 Membrane-Proximal External Region Positively Correlates with Neutralization Sensitivity. J. Virol., 85(16):8217-8226, Aug 2011. PubMed ID: 21653673.
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Cham2006
Fatim Cham, Peng Fei Zhang, Leo Heyndrickx, Peter Bouma, Ping Zhong, Herman Katinger, James Robinson, Guido van der Groen, and Gerald V. Quinnan, Jr. Neutralization and Infectivity Characteristics of Envelope Glycoproteins from Human Immunodeficiency Virus Type 1 Infected Donors Whose Sera Exhibit Broadly Cross-Reactive Neutralizing Activity. Virology, 347(1):36-51, 30 Mar 2006. PubMed ID: 16378633.
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Cheeseman2017
Hannah M. Cheeseman, Natalia J. Olejniczak, Paul M. Rogers, Abbey B. Evans, Deborah F. L. King, Paul Ziprin, Hua-Xin Liao, Barton F. Haynes, and Robin J. Shattock. Broadly Neutralizing Antibodies Display Potential for Prevention of HIV-1 Infection of Mucosal Tissue Superior to That of Nonneutralizing Antibodies. J. Virol., 91(1), 1 Jan 2017. PubMed ID: 27795431.
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Chen1994
Y.-H. Chen, A. Susanna, G. Bock, F. Steindl, H. Katinger, and M. P. Dierich. HIV-1 gp41 Shares a Common Immunologic Determinant with Human T, B and Monocyte Cell Lines. Immunol. Lett., 39:219-222, 1994. The MAb 3D6 binds to HIV gp41, and to a 43 kd protein found in human T, B and monocyte cell lines. The authors suggest the possibility of molecular mimicry. PubMed ID: 7518416.
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Chen2007
Ping Chen, Wolfgang Hübner, Matthew A. Spinelli, and Benjamin K. Chen. Predominant Mode of Human Immunodeficiency Virus Transfer between T Cells Is Mediated by Sustained Env-Dependent Neutralization-Resistant Virological Synapses. J. Virol., 81(22):12582-12595, Nov 2007. PubMed ID: 17728240.
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Chen2008a
Hongying Chen, Xiaodong Xu, Hsin-Hui Lin, Ssu-Hsien Chen, Anna Forsman, Marlen Aasa-Chapman, and Ian M. Jones. Mapping the Immune Response to the Outer Domain of a Human Immunodeficiency Virus-1 Clade C gp120. J. Gen. Virol., 89(10):2597-2604, Oct 2008. PubMed ID: 18796729.
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Chen2009b
Weizao Chen and Dimiter S. Dimitrov. Human Monoclonal Antibodies and Engineered Antibody Domains as HIV-1 Entry Inhibitors. Curr. Opin. HIV AIDS, 4(2):112-117, Mar 2009. PubMed ID: 19339949.
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Chen2013
Yao Chen, Jinsong Zhang, Kwan-Ki Hwang, Hilary Bouton-Verville, Shi-Mao Xia, Amanda Newman, Ying-Bin Ouyang, Barton F. Haynes, and Laurent Verkoczy. Common Tolerance Mechanisms, but Distinct Cross-Reactivities Associated with gp41 and Lipids, Limit Production of HIV-1 Broad Neutralizing Antibodies 2F5 and 4E10. J. Immunol., 191(3):1260-1275, Aug 1 2013. PubMed ID: 23825311.
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Chen2015
Jia Chen, James M. Kovacs, Hanqin Peng, Sophia Rits-Volloch, Jianming Lu, Donghyun Park, Elise Zablowsky, Michael S. Seaman, and Bing Chen. Effect of the Cytoplasmic Domain on Antigenic Characteristics of HIV-1 Envelope Glycoprotein. Science, 349(6244):191-195, 10 Jul 2015. PubMed ID: 26113642.
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Chenine2013
Agnès-Laurence Chenine, Lindsay Wieczorek, Eric Sanders-Buell, Maggie Wesberry, Teresa Towle, Devin M. Pillis, Sebastian Molnar, Robert McLinden, Tara Edmonds, Ivan Hirsch, Robert O'Connell, Francine E. McCutchan, David C. Montefiori, Christina Ochsenbauer, John C. Kappes, Jerome H. Kim, Victoria R. Polonis, and Sodsai Tovanabutra. Impact of HIV-1 Backbone on Neutralization Sensitivity: Neutralization Profiles of Heterologous Envelope Glycoproteins Expressed in Native Subtype C and CRF01\_AE Backbone. PLoS One, 8(11):e76104, 2013. PubMed ID: 24312165.
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Chenine2018
Agnes-Laurence Chenine, Melanie Merbah, Lindsay Wieczorek, Sebastian Molnar, Brendan Mann, Jenica Lee, Anne-Marie O'Sullivan, Meera Bose, Eric Sanders-Buell, Gustavo H. Kijak, Carolina Herrera, Robert McLinden, Robert J. O'Connell, Nelson L. Michael, Merlin L. Robb, Jerome H. Kim, Victoria R. Polonis, and Sodsai Tovanabutra. Neutralization Sensitivity of a Novel HIV-1 CRF01\_AE Panel of Infectious Molecular Clones. J. Acquir. Immune Defic. Syndr., 78(3):348-355, 1 Jul 2018. PubMed ID: 29528942.
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Ching2010
Lance Ching and Leonidas Stamatatos. Alterations in the Immunogenic Properties of Soluble Trimeric Human Immunodeficiency Virus Type 1 Envelope Proteins Induced by Deletion or Heterologous Substitutions of the V1 Loop. J. Virol., 84(19):9932-9946, Oct 2010. PubMed ID: 20660181.
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Chomont2008
Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650.
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Chong2008
Huihui Chong, Kunxue Hong, Chuntao Zhang, Jianhui Nie, Aijing Song, Wei Kong, and Youchun Wang. Genetic and Neutralization Properties of HIV-1 env Clones from Subtype B/BC/AE Infections in China. J. Acquir. Immune Defic. Syndr., 47(5):535-543, 15 Apr 2008. PubMed ID: 18209676.
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Choudhry2006
Vidita Choudhry, Mei-Yun Zhang, Ilia Harris, Igor A. Sidorov, Bang Vu, Antony S. Dimitrov, Timothy Fouts, and Dimiter S. Dimitrov. Increased Efficacy of HIV-1 Neutralization by Antibodies at Low CCR5 Surface Concentration. Biochem. Biophys. Res. Commun., 348(3):1107-1115, 29 Sep 2006. PubMed ID: 16904645.
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Choudhry2007
Vidita Choudhry, Mei-Yun Zhang, Igor A. Sidorov, John M. Louis, Ilia Harris, Antony S. Dimitrov, Peter Bouma, Fatim Cham, Anil Choudhary, Susanna M. Rybak, Timothy Fouts, David C. Montefiori, Christopher C. Broder, Gerald V. Quinnan, Jr., and Dimiter S. Dimitrov. Cross-Reactive HIV-1 Neutralizing Monoclonal Antibodies Selected by Screening of an Immune Human Phage Library Against an Envelope Glycoprotein (gp140) Isolated from a Patient (R2) with Broadly HIV-1 Neutralizing Antibodies. Virology, 363(1):79-90, 20 Jun 2007. PubMed ID: 17306322.
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Chuang2013
Gwo-Yu Chuang, Priyamvada Acharya, Stephen D. Schmidt, Yongping Yang, Mark K. Louder, Tongqing Zhou, Young Do Kwon, Marie Pancera, Robert T. Bailer, Nicole A. Doria-Rose, Michel C. Nussenzweig, John R. Mascola, Peter D. Kwong, and Ivelin S. Georgiev. Residue-Level Prediction of HIV-1 Antibody Epitopes Based on Neutralization of Diverse Viral Strains. J. Virol., 87(18):10047-10058, Sep 2013. PubMed ID: 23843642.
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Chun2014
Tae-Wook Chun, Danielle Murray, Jesse S. Justement, Jana Blazkova, Claire W. Hallahan, Olivia Fankuchen, Kathleen Gittens, Erika Benko, Colin Kovacs, Susan Moir, and Anthony S. Fauci. Broadly Neutralizing Antibodies Suppress HIV in the Persistent Viral Reservoir. Proc. Natl. Acad. Sci. U.S.A., 111(36):13151-13156, 9 Sep 2014. PubMed ID: 25157148.
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Clerici2002
Mario Clerici, Claudia Barassi, Claudia Devito, Claudia Pastori, Stefania Piconi, Daria Trabattoni, Renato Longhi, Jorma Hinkula, Kristina Broliden, and Lucia Lopalco. Serum IgA of HIV-Exposed Uninfected Individuals Inhibit HIV Through Recognition of a Region within the Alpha-Helix of gp41. AIDS, 16(13):1731-1741, 6 Sep 2002. PubMed ID: 12218383.
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Coeffier2000
E. Coeffier, J. M. Clement, V. Cussac, N. Khodaei-Boorane, M. Jehanno, M. Rojas, A. Dridi, M. Latour, R. El Habib, F. Barre-Sinoussi, M. Hofnung, and C. Leclerc. Antigenicity and Immunogenicity of the HIV-1 gp41 Epitope ELDKWA Inserted into Permissive Sites of the MalE Protein. Vaccine, 19(7-8):684-693, 22 Nov 2000. PubMed ID: 11115689.
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Cognasse2009
Fabrice Cognasse, Hind Hamzeh-Cognasse, Julien Berthet, Pauline Damien, Frédéric Lucht, Bruno Pozzetto, and Olivier Garraud. Altered Release of Regulated upon Activation, Normal T-Cell Expressed and Secreted Protein from Human, Normal Platelets: Contribution of Distinct HIV-1MN gp41 Peptides. AIDS, 23(15):2057-2059, 24 Sep 2009. PubMed ID: 19654498.
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Conley1994a
A. J. Conley, J. A. Kessler, II, L. J. Boots, J.-S. Tung, B. A. Arnold, P. M. Keller, A. R. Shaw, and E. A. Emini. Neutralization of Divergent Human Immunodeficiency Virus Type 1 Variants and Primary Isolates by IAM-41-2F5, an Anti-gp41 Human Monoclonal Antibody. Proc. Natl. Acad. Sci. U.S.A., 91:3348-3352, 1994. 2F5 is capable of neutralizing a broad range of primary isolates and lab strains. Susceptibility to neutralization was dependent on presence of a conserved antibody binding site. Kinetic studies were done, and 2F5 has a very long t$_1/2$ of dissociation, 156 minutes for gp41. The authors point out that LDKW core is present in highly diverged international isolates. PubMed ID: 7512731.
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Conley1996
A. J. Conley, J. A. Kessler, II, L. J. Boots, P. M. McKenna, W. A. Schleif, E. A. Emini, G. E. Mark, III, H. Katinger, E. K. Cobb, S. M. Lunceford, S. R. Rouse, and K. K. Murthy. The Consequence of Passive Administration of an Anti-Human Immunodeficiency Virus Type 1 Neutralizing Monoclonal Antibody before Challenge of Chimpanzees with a Primary Virus Isolate. J. Virol., 70:6751-6758, 1996. The MAb 2F5 was infused into two chimpanzees which were then given an intravenous challenge with a primary HIV-1 isolate -- both became infected, but with delayed detection and prolonged decrease in viral load relative to controls, indicating that preexisting, neutralizing antibodies (passively administered or actively elicited) affect the course of acute-phase virus replication and can be influential after the Ab can no longer be detected in the peripheral circulation. PubMed ID: 8794312.
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Connor1998
R. I. Connor, B. T. Korber, B. S. Graham, B. H. Hahn, D. D. Ho, B. D. Walker, A. U. Neumann, S. H. Vermund, J. Mestecky, S. Jackson, E. Fenamore, Y. Cao, F. Gao, S. Kalams, K. J. Kunstman, D. McDonald, N. McWilliams, A. Trkola, J. P. Moore, and S. M. Wolinsky. Immunological and virological analyses of persons infected by human immunodeficiency virus type 1 while participating in trials of recombinant gp120 subunit vaccines. J. Virol., 72:1552-76, 1998. No gp120-vaccine induced antibodies in a human trial of gp120 MN and SF2 could neutralize the primary viruses that infected the vaccinees. The primary isolates from the infected vaccinees were shown not to be particularly refractive to neutralization by their susceptibility to a panel of neutralizing MAbs. PubMed ID: 9445059.
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Corti2010
Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712.
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Coutant2008
Jérôme Coutant, Huifeng Yu, Marie-Jeanne Clément, Annette Alfsen, Flavio Toma, Patrick A. Curmi, and Morgane Bomsel. Both Lipid Environment and pH Are Critical for Determining Physiological Solution Structure of 3-D-Conserved Epitopes of the HIV-1 gp41-MPER Peptide P1. FASEB J., 22(12):4338-4351, Dec 2008. PubMed ID: 18776068.
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Crooks2005
Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980.
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Crooks2008
Emma T. Crooks, Pengfei Jiang, Michael Franti, Sharon Wong, Michael B. Zwick, James A. Hoxie, James E. Robinson, Penny L. Moore, and James M. Binley. Relationship of HIV-1 and SIV Envelope Glycoprotein Trimer Occupation and Neutralization. Virology, 377(2):364-378, 1 Aug 2008. PubMed ID: 18539308.
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Crooks2011
Ema T. Crooks, Tommy Tong, Keiko Osawa, and James M. Binley. Enzyme Digests Eliminate Nonfunctional Env from HIV-1 Particle Surfaces, Leaving Native Env Trimers Intact and Viral Infectivity Unaffected. J. Virol., 85(12):5825-5839, Jun 2011. PubMed ID: 21471242.
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Crooks2015
Ema T. Crooks, Tommy Tong, Bimal Chakrabarti, Kristin Narayan, Ivelin S. Georgiev, Sergey Menis, Xiaoxing Huang, Daniel Kulp, Keiko Osawa, Janelle Muranaka, Guillaume Stewart-Jones, Joanne Destefano, Sijy O'Dell, Celia LaBranche, James E. Robinson, David C. Montefiori, Krisha McKee, Sean X. Du, Nicole Doria-Rose, Peter D. Kwong, John R. Mascola, Ping Zhu, William R. Schief, Richard T. Wyatt, Robert G. Whalen, and James M. Binley. Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site. PLoS Pathog, 11(5):e1004932, May 2015. PubMed ID: 26023780.
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Dacheux2004
Laurent Dacheux, Alain Moreau, Yasemin Ataman-Önal, François Biron, Bernard Verrier, and Francis Barin. Evolutionary Dynamics of the Glycan Shield of the Human Immunodeficiency Virus Envelope during Natural Infection and Implications for Exposure of the 2G12 Epitope. J. Virol., 78(22):12625-12637, Nov 2004. PubMed ID: 15507649.
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Danesh2020
Ali Danesh, Yanqin Ren, and R. Brad Jones. Roles of Fragment Crystallizable-Mediated Effector Functions in Broadly Neutralizing Antibody Activity against HIV. Curr. Opin. HIV AIDS, 15(5):316-323, Sep 2020. PubMed ID: 32732552.
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Davis2006
David Davis, Helen Donners, Betty Willems, Michel Ntemgwa, Tine Vermoesen, Guido van der Groen, and Wouter Janssens. Neutralization Kinetics of Sensitive and Resistant Subtype B Primary Human Immunodeficiency Virus Type 1 Isolates. J. Med. Virol., 78(7):864-786, Jul 2006. PubMed ID: 16721864.
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Davis2009
Katie L. Davis, Frederic Bibollet-Ruche, Hui Li, Julie M. Decker, Olaf Kutsch, Lynn Morris, Aidy Salomon, Abraham Pinter, James A. Hoxie, Beatrice H. Hahn, Peter D. Kwong, and George M. Shaw. Human Immunodeficiency Virus Type 2 (HIV-2)/HIV-1 Envelope Chimeras Detect High Titers of Broadly Reactive HIV-1 V3-Specific Antibodies in Human Plasma. J. Virol., 83(3):1240-1259, Feb 2009. PubMed ID: 19019969.
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Decamp2014
Allan deCamp, Peter Hraber, Robert T. Bailer, Michael S. Seaman, Christina Ochsenbauer, John Kappes, Raphael Gottardo, Paul Edlefsen, Steve Self, Haili Tang, Kelli Greene, Hongmei Gao, Xiaoju Daniell, Marcella Sarzotti-Kelsoe, Miroslaw K. Gorny, Susan Zolla-Pazner, Celia C. LaBranche, John R. Mascola, Bette T. Korber, and David C. Montefiori. Global Panel of HIV-1 Env Reference Strains for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 88(5):2489-2507, Mar 2014. PubMed ID: 24352443.
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delaArada2009
Igor de la Arada, Jean-Philippe Julien, Beatriz G. de la Torre, Nerea Huarte, David Andreu, Emil F. Pai, José L. R. Arrondo, and José L. Nieva. Structural Constraints Imposed by the Conserved Fusion Peptide on the HIV-1 gp41 Epitope Recognized by the Broadly Neutralizing Antibody 2F5. J. Phys. Chem. B, 113(41):13626-13637, 15 Oct 2009. PubMed ID: 19754136.
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Dennison2009
S. Moses Dennison, Shelley M. Stewart, Kathryn C. Stempel, Hua-Xin Liao, Barton F. Haynes, and S. Munir Alam. Stable Docking of Neutralizing Human Immunodeficiency Virus Type 1 gp41 Membrane-Proximal External Region Monoclonal Antibodies 2F5 and 4E10 Is Dependent on the Membrane Immersion Depth of Their Epitope Regions. J. Virol., 83(19):10211-10223, Oct 2009. PubMed ID: 19640992.
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Dennison2011
S. Moses Dennison, Laura L. Sutherland, Frederick H. Jaeger, Kara M. Anasti, Robert Parks, Shelley Stewart, Cindy Bowman, Shi-Mao Xia, Ruijun Zhang, Xiaoying Shen, Richard M. Scearce, Gilad Ofek, Yongping Yang, Peter D. Kwong, Sampa Santra, Hua-Xin Liao, Georgia Tomaras, Norman L. Letvin, Bing Chen, S. Munir Alam, and Barton F. Haynes. Induction of Antibodies in Rhesus Macaques That Recognize a Fusion-Intermediate Conformation of HIV-1 gp41. PLoS One, 6(11):e27824, 2011. PubMed ID: 22140469.
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Dennison2011a
S. Moses Dennison, Kara Anasti, Richard M. Scearce, Laura Sutherland, Robert Parks, Shi-Mao Xia, Hua-Xin Liao, Miroslaw K. Gorny, Susan Zolla-Pazner, Barton F. Haynes, and S. Munir Alam. Nonneutralizing HIV-1 gp41 Envelope Cluster II Human Monoclonal Antibodies Show Polyreactivity for Binding to Phospholipids and Protein Autoantigens. J. Virol., 85(3):1340-1347, Feb 2011. PubMed ID: 21106741.
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Dennison2014
S. Moses Dennison, Kara M. Anasti, Frederick H. Jaeger, Shelley M. Stewart, Justin Pollara, Pinghuang Liu, Erika L. Kunz, Ruijun Zhang, Nathan Vandergrift, Sallie Permar, Guido Ferrari, Georgia D. Tomaras, Mattia Bonsignori, Nelson L. Michael, Jerome H Kim, Jaranit Kaewkungwal, Sorachai Nitayaphan, Punnee Pitisuttithum, Supachai Rerks-Ngarm, Hua-Xin Liao, Barton F. Haynes, and S. Munir Alam. Vaccine-Induced HIV-1 Envelope gp120 Constant Region 1-Specific Antibodies Expose a CD4-Inducible Epitope and Block the Interaction of HIV-1 gp140 with Galactosylceramide. J. Virol., 88(16):9406-9417, Aug 2014. PubMed ID: 24920809.
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Depetris2012
Rafael S Depetris, Jean-Philippe Julien, Reza Khayat, Jeong Hyun Lee, Robert Pejchal, Umesh Katpally, Nicolette Cocco, Milind Kachare, Evan Massi, Kathryn B. David, Albert Cupo, Andre J. Marozsan, William C. Olson, Andrew B. Ward, Ian A. Wilson, Rogier W. Sanders, and John P Moore. Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers. J. Biol. Chem., 287(29):24239-24254, 13 Jul 2012. PubMed ID: 22645128.
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Derby2006
Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322.
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Derby2007
Nina R. Derby, Sean Gray, Elizabeth Wayner, Dwayne Campogan, Giorgos Vlahogiannis, Zane Kraft, Susan W. Barnett, Indresh K. Srivastava, and Leonidas Stamatatos. Isolation and Characterization of Monoclonal Antibodies Elicited by Trimeric HIV-1 Env gp140 Protein Immunogens. Virology, 366(2):433-445, 30 Sep 2007. PubMed ID: 17560621.
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deRosny2004
Eve de Rosny, Russell Vassell, Shibo Jiang, Renate Kunert, and Carol D. Weiss. Binding of the 2F5 Monoclonal Antibody to Native and Fusion-Intermediate Forms of Human Immunodeficiency Virus Type 1 gp41: Implications for Fusion-Inducing Conformational Changes. J. Virol., 78(5):2627-2631, Mar 2004. PubMed ID: 14963170.
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Dervillez2010
Xavier Dervillez, Volker Klaukien, Ralf Dürr, Joachim Koch, Alexandra Kreutz, Thomas Haarmann, Michaela Stoll, Donghan Lee, Teresa Carlomagno, Barbara Schnierle, Kalle Möbius, Christoph Königs, Christian Griesinger, and Ursula Dietrich. Peptide Ligands Selected with CD4-Induced Epitopes on Native Dualtropic HIV-1 Envelope Proteins Mimic Extracellular Coreceptor Domains and Bind to HIV-1 gp120 Independently of Coreceptor Usage. J. Virol., 84(19):10131-10138, Oct 2010. PubMed ID: 20660187.
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Dey2003
Barna Dey, Christie S. Del Castillo, and Edward A. Berger. Neutralization of Human Immunodeficiency Virus Type 1 by sCD4-17b, a Single-Chain Chimeric Protein, Based on Sequential Interaction of gp120 with CD4 and Coreceptor. J. Virol., 77(5):2859-2865, Mar 2003. PubMed ID: 12584309.
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Dey2007
Antu K. Dey, Kathryn B. David, Per J. Klasse, and John P. Moore. Specific Amino Acids in the N-Terminus of the gp41 Ectodomain Contribute to the Stabilization of a Soluble, Cleaved gp140 Envelope Glycoprotein from Human Immunodeficiency Virus Type 1. Virology, 360(1):199-208, 30 Mar 2007. PubMed ID: 17092531.
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Dey2008
Antu K. Dey, Kathryn B. David, Neelanjana Ray, Thomas J. Ketas, Per J. Klasse, Robert W. Doms, and John P. Moore. N-Terminal Substitutions in HIV-1 gp41 Reduce the Expression of Non-Trimeric Envelope Glycoproteins on the Virus. Virology, 372(1):187-200, 1 Mar 2008. PubMed ID: 18031785.
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Dhillon2007
Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160.
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Dieltjens2009
Tessa Dieltjens, Leo Heyndrickx, Betty Willems, Elin Gray, Lies Van Nieuwenhove, Katrijn Grupping, Guido Vanham, and Wouter Janssens. Evolution of Antibody Landscape and Viral Envelope Escape in an HIV-1 CRF02\_AG Infected Patient with 4E10-Like Antibodies. Retrovirology, 6:113, 2009. PubMed ID: 20003438.
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Dimitrov2007
Antony S. Dimitrov, Amy Jacobs, Catherine M. Finnegan, Gabriela Stiegler, Hermann Katinger, and Robert Blumenthal. Exposure of the Membrane-Proximal External Region of HIV-1 gp41 in the Course of HIV-1 Envelope Glycoprotein-Mediated Fusion. Biochemistry, 46(5):1398-1401, 6 Feb 2007. PubMed ID: 17260969.
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Diomede2012
L. Diomede, S. Nyoka, C. Pastori, L. Scotti, A. Zambon, G. Sherman, C. M. Gray, M. Sarzotti-Kelsoe, and L. Lopalco. Passively Transmitted gp41 Antibodies in Babies Born from HIV-1 Subtype C-Seropositive Women: Correlation between Fine Specificity and Protection. J. Virol., 86(8):4129-4138, Apr 2012. PubMed ID: 22301151.
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Dong2001
X. N. Dong, Y. Xiao, and Y. H. Chen. ELNKWA-epitope specific antibodies induced by epitope-vaccine recognize ELDKWA- and other two neutralizing-resistant mutated epitopes on HIV-1 gp41. Immunol. Lett., 75(2):149--52, 1 Jan 2001. PubMed ID: 11137140.
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Dong2005
Xiao-Nan Dong, Yi Wu, and Ying-Hua Chen. The Neutralizing Epitope ELDKWA on HIV-1 gp41: Genetic Variability and Antigenicity. Immunol. Lett., 101(1):81-86, 15 Oct 2005. PubMed ID: 15951025.
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Dong2006
Xiao-Nan Dong and Ying-Hua Chen. Neutralizing Epitopes in the Membrane-Proximal Region of HIV-1 gp41: Genetic Variability and Co-Variation. Immunol. Lett., 106(2):180-186, 15 Aug 2006. PubMed ID: 16859756.
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Doria-Rose2010
Nicole A. Doria-Rose, Rachel M. Klein, Marcus G. Daniels, Sijy O'Dell, Martha Nason, Alan Lapedes, Tanmoy Bhattacharya, Stephen A. Migueles, Richard T. Wyatt, Bette T. Korber, John R. Mascola, and Mark Connors. Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables. J. Virol., 84(3):1631-1636, Feb 2010. PubMed ID: 19923174.
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Doria-Rose2017
Nicole A. Doria-Rose, Han R. Altae-Tran, Ryan S. Roark, Stephen D. Schmidt, Matthew S. Sutton, Mark K. Louder, Gwo-Yu Chuang, Robert T. Bailer, Valerie Cortez, Rui Kong, Krisha McKee, Sijy O'Dell, Felicia Wang, Salim S. Abdool Karim, James M. Binley, Mark Connors, Barton F. Haynes, Malcolm A. Martin, David C. Montefiori, Lynn Morris, Julie Overbaugh, Peter D. Kwong, John R. Mascola, and Ivelin S. Georgiev. Mapping Polyclonal HIV-1 Antibody Responses via Next-Generation Neutralization Fingerprinting. PLoS Pathog., 13(1):e1006148, Jan 2017. PubMed ID: 28052137.
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Dorosko2008
Stephanie M. Dorosko, Sandra L. Ayres, and Ruth I. Connor. Induction of HIV-1 MPR(649-684)-Specific IgA and IgG Antibodies in Caprine Colostrum Using a Peptide-Based Vaccine. Vaccine, 26(42):5416-5422, 3 Oct 2008. PubMed ID: 18708113.
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Drummer2013
Heidi E. Drummer, Melissa K. Hill, Anne L. Maerz, Stephanie Wood, Paul A. Ramsland, Johnson Mak, and Pantelis Poumbourios. Allosteric Modulation of the HIV-1 gp120-gp41 Association Site by Adjacent gp120 Variable Region 1 (V1) N-Glycans Linked to Neutralization Sensitivity. PLoS Pathog., 9(4):e1003218, 2013. PubMed ID: 23592978.
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DSouza1994
M. P. D'Souza, S. J. Geyer, C. V. Hanson, R. M. Hendry, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 Envelope by Neutralization and Binding Assays: An International Collaboration. AIDS, 8:169-181, 1994. PubMed ID: 7519019.
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DSouza1995
M. P. D'Souza, G. Milman, J. A. Bradac, D. McPhee, C. V. Hanson, and R. M. Hendry. Neutralization of Primary HIV-1 Isolates by Anti-Envelope Monoclonal Antibodies. AIDS, 9:867-874, 1995. Eleven labs tested the 6 human MAbs 1125H, TH9, 4.8D, 257-D-IV, TH1, 2F5, and also HIVIG for neutralization of MN, JRCSF, the two B clade primary isolates 301657 and THA/92/026, and the D clade isolate UG/92/21. 2F5 was the most broadly neutralizing, better than HIVIG. The other MAbs showed limited neutralization of only MN (anti-CD4BS MAbs 1125H, TH9, and 4.8D), or MN and JRCSF (anti-V3 MAbs 257-D-IV and TH1). PubMed ID: 7576320.
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DSouza1997
M. P. D'Souza, D. Livnat, J. A. Bradac, S. H. Bridges, the AIDS Clinical Trials Group Antibody Selection Working Group, and Collaborating Investigators. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. J. Infect. Dis., 175:1056-1062, 1997. Five laboratories evaluated neutralization of nine primary B clade isolates by a coded panel of seven human MAbs to HIV-1 subtype B envelope. IgG1b12, 2G12, 2F5 showed potent and broadly cross-reactive neutralizing ability; F105, 447/52-D, 729-D, 19b did not neutralize the primary isolates. PubMed ID: 9129066.
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Du2009
Sean X. Du, Rebecca J. Idiart, Ellaine B. Mariano, Helen Chen, Peifeng Jiang, Li Xu, Kristin M. Ostrow, Terri Wrin, Pham Phung, James M. Binley, Christos J. Petropoulos, John A. Ballantyne, and Robert G. Whalen. Effect of Trimerization Motifs on Quaternary Structure, Antigenicity, and Immunogenicity of a Noncleavable HIV-1 gp140 Envelope Glycoprotein. Virology, 395(1):33-44, 5 Dec 2009. PubMed ID: 19815247.
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Dunfee2007
Rebecca L. Dunfee, Elaine R. Thomas, Jianbin Wang, Kevin Kunstman, Steven M. Wolinsky, and Dana Gabuzda. Loss of the N-Linked Glycosylation Site at Position 386 in the HIV Envelope V4 Region Enhances Macrophage Tropism and Is Associated with Dementia. Virology, 367(1):222-234, 10 Oct 2007. PubMed ID: 17599380.
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Earl1997
P. L. Earl, C. C. Broder, R. W. Doms, and B. Moss. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol., 71:2674-84, 1997. PubMed ID: 9060620.
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Edmonds2010
Tara G. Edmonds, Haitao Ding, Xing Yuan, Qing Wei, Kendra S. Smith, Joan A. Conway, Lindsay Wieczorek, Bruce Brown, Victoria Polonis, John T. West, David C. Montefiori, John C. Kappes, and Christina Ochsenbauer. Replication Competent Molecular Clones of HIV-1 Expressing Renilla Luciferase Facilitate the Analysis of Antibody Inhibition in PBMC. Virology, 408(1):1-13, 5 Dec 2010. PubMed ID: 20863545.
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Ernst1998
W. Ernst, R. Grabherr, D. Wegner, N. Borth, A. Grassauer, and H. Katinger. Baculovirus surface display: construction and screening of a eukaryotic epitope library. Nucl. Acids Res., 26:1718-23, 1998. PubMed ID: 9512544.
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Euler2011
Zelda Euler, Evelien M. Bunnik, Judith A. Burger, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Activity of Broadly Neutralizing Antibodies, Including PG9, PG16, and VRC01, against Recently Transmitted Subtype B HIV-1 Variants from Early and Late in the Epidemic. J. Virol., 85(14):7236-7245, Jul 2011. PubMed ID: 21561918.
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Falkowska2012
Emilia Falkowska, Alejandra Ramos, Yu Feng, Tongqing Zhou, Stephanie Moquin, Laura M. Walker, Xueling Wu, Michael S. Seaman, Terri Wrin, Peter D. Kwong, Richard T. Wyatt, John R. Mascola, Pascal Poignard, and Dennis R. Burton. PGV04, an HIV-1 gp120 CD4 Binding Site Antibody, Is Broad and Potent in Neutralization but Does Not Induce Conformational Changes Characteristic of CD4. J. Virol., 86(8):4394-4403, Apr 2012. PubMed ID: 22345481.
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Fenyo2009
Eva Maria Fenyö, Alan Heath, Stefania Dispinseri, Harvey Holmes, Paolo Lusso, Susan Zolla-Pazner, Helen Donners, Leo Heyndrickx, Jose Alcami, Vera Bongertz, Christian Jassoy, Mauro Malnati, David Montefiori, Christiane Moog, Lynn Morris, Saladin Osmanov, Victoria Polonis, Quentin Sattentau, Hanneke Schuitemaker, Ruengpung Sutthent, Terri Wrin, and Gabriella Scarlatti. International Network for Comparison of HIV Neutralization Assays: The NeutNet Report. PLoS One, 4(2):e4505, 2009. PubMed ID: 19229336.
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Ferrantelli2002
Flavia Ferrantelli and Ruth M. Ruprecht. Neutralizing Antibodies Against HIV --- Back in the Major Leagues? Curr. Opin. Immunol., 14(4):495-502, Aug 2002. PubMed ID: 12088685.
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Ferrantelli2003
Flavia Ferrantelli, Regina Hofmann-Lehmann, Robert A. Rasmussen, Tao Wang, Weidong Xu, Pei-Lin Li, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Post-Exposure Prophylaxis with Human Monoclonal Antibodies Prevented SHIV89.6P Infection or Disease in Neonatal Macaques. AIDS, 17(3):301-309, 14 Feb 2003. PubMed ID: 12556683.
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Ferrantelli2004
Flavia Ferrantelli, Robert A. Rasmussen, Kathleen A. Buckley, Pei-Lin Li, Tao Wang, David C. Montefiori, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Complete Protection of Neonatal Rhesus Macaques against Oral Exposure to Pathogenic Simian-Human Immunodeficiency Virus by Human Anti-HIV Monoclonal Antibodies. J. Infect. Dis., 189(12):2167-2173, 15 Jun 2004. PubMed ID: 15181562.
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Ferrantelli2004a
Flavia Ferrantelli, Moiz Kitabwalla, Robert A. Rasmussen, Chuanhai Cao, Ting-Chao Chou, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Yun Bai, Joseph Cotropia, Kenneth E. Ugen, and Ruth M. Ruprecht. Potent Cross-Group Neutralization of Primary Human Immunodeficiency Virus Isolates with Monoclonal Antibodies--Implications for Acquired Immunodeficiency Syndrome Vaccine. J. Infect. Dis., 189(1):71-74, 1 Jan 2004. PubMed ID: 14702155.
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Ferrantelli2007
Flavia Ferrantelli, Kathleen A. Buckley, Robert A. Rasmussen, Alistair Chalmers, Tao Wang, Pei-Lin Li, Alison L. Williams, Regina Hofmann-Lehmann, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Time Dependence of Protective Post-Exposure Prophylaxis with Human Monoclonal Antibodies Against Pathogenic SHIV Challenge in Newborn Macaques. Virology, 358(1):69-78, 5 Feb 2007. PubMed ID: 16996554.
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Fiebig2009
Uwe Fiebig, Mirco Schmolke, Magdalena Eschricht, Reinhard Kurth, and Joachim Denner. Mode of Interaction between the HIV-1-Neutralizing Monoclonal Antibody 2F5 and Its Epitope. AIDS, 23(8):887-895, 15 May 2009. PubMed ID: 19414989.
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Finnegan2002
Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Transmembrane Glycoprotein during Cell-Cell Fusion. J. Virol., 76(23):12123-12134, Dec 2002. PubMed ID: 12414953.
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Finton2013
Kathryn A. K. Finton, Kevin Larimore, H. Benjamin Larman, Della Friend, Colin Correnti, Peter B. Rupert, Stephen J. Elledge, Philip D. Greenberg, and Roland K. Strong. Autoreactivity and Exceptional CDR Plasticity (but Not Unusual Polyspecificity) Hinder Elicitation of the Anti-HIV Antibody 4E10. PLoS Pathog., 9(9):e1003639, 2013. PubMed ID: 24086134.
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Floss2008
Doreen M. Floss, Markus Sack, Johannes Stadlmann, Thomas Rademacher, Jürgen Scheller, Eva Stöger, Rainer Fischer, and Udo Conrad. Biochemical and Functional Characterization of Anti-HIV Antibody-ELP Fusion Proteins from Transgenic Plants. Plant Biotechnol. J., 6(4):379-391, May 2008. PubMed ID: 18312505.
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Follis2002
Kathryn E. Follis, Scott J. Larson, Min Lu, and Jack H. Nunberg. Genetic Evidence that Interhelical Packing Interactions in the gp41 Core Are Critical for Transition of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein to the Fusion-Active State. J. Virol., 76(14):7356-7362, Jul 2002. PubMed ID: 12072535.
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Forthal2009
Donald N. Forthal and Christiane Moog. Fc Receptor-Mediated Antiviral Antibodies. Curr. Opin. HIV AIDS, 4(5):388-393, Sep 2009. PubMed ID: 20048702.
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Fouts1998
T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713.
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Frankel1998
S. S. Frankel, R. M. Steinman, N. L. Michael, S. R. Kim, N. Bhardwaj, M. Pope, M. K. Louder, P. K. Ehrenberg, P. W. Parren, D. R. Burton, H. Katinger, T. C. VanCott, M. L. Robb, D. L. Birx, and J. R. Mascola. Neutralizing Monoclonal Antibodies Block Human Immunodeficiency Virus Type 1 Infection of Dendritic Cells and Transmission to T Cells. J. Virol., 72:9788-9794, 1998. Investigation of three human MAbs to elicit a neutralizing effect and block HIV-1 infection in human dendritic cells. Preincubation with NAbs IgG1b12 or a combination of 2F5/2G12 prevented infection of purified DC and transmission in DC/T-cell cultures. PubMed ID: 9811714.
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Franquelim2011
Henri G. Franquelim, Salvatore Chiantia, Ana Salomé Veiga, Nuno C. Santos, Petra Schwille, and Miguel A. R. B. Castanho. Anti-HIV-1 Antibodies 2F5 and 4E10 Interact Differently with Lipids to Bind Their Epitopes. AIDS, 25(4):419-428, 20 Feb 2011. PubMed ID: 21245727.
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Frey2008
Gary Frey, Hanqin Peng, Sophia Rits-Volloch, Marco Morelli, Yifan Cheng, and Bing Chen. A Fusion-Intermediate State of HIV-1 gp41 Targeted by Broadly Neutralizing Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(10):3739-3744, 11 Mar 2008. PubMed ID: 18322015.
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Frey2010
Gary Frey, Jia Chen, Sophia Rits-Volloch, Michael M. Freeman, Susan Zolla-Pazner, and Bing Chen. Distinct Conformational States of HIV-1 gp41 Are Recognized by Neutralizing and Non-Neutralizing Antibodies. Nat. Struct. Mol. Biol., 17(12):1486-1491, Dec 2010. PubMed ID: 21076402.
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Fu2018
Qingshan Fu, Md Munan Shaik, Yongfei Cai, Fadi Ghantous, Alessandro Piai, Hanqin Peng, Sophia Rits-Volloch, Zhijun Liu, Stephen C. Harrison, Michael S. Seaman, Bing Chen, and James J. Chou. Structure of the Membrane Proximal External Region of HIV-1 Envelope Glycoprotein. Proc. Natl. Acad. Sci. U.S.A., 115(38):E8892-E8899, 18 Sep 2018. PubMed ID: 30185554.
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Gach2007a
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Gach2008
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Gach2013
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Gach2014
Johannes S. Gach, Chad J. Achenbach, Veronika Chromikova, Baiba Berzins, Nina Lambert, Gary Landucci, Donald N. Forthal, Christine Katlama, Barbara H. Jung, and Robert L. Murphy. HIV-1 Specific Antibody Titers and Neutralization among Chronically Infected Patients on Long-Term Suppressive Antiretroviral Therapy (ART): A Cross-Sectional Study. PLoS One, 9(1):e85371, 2014. PubMed ID: 24454852.
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Gao2005a
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Feng Gao, Hua-Xin Liao, Beatrice H. Hahn, Norman L. Letvin, Bette T. Korber, and Barton F. Haynes. Centralized HIV-1 Envelope Immunogens and Neutralizing Antibodies. Curr. HIV Res., 5(6):572-577, Nov 2007. PubMed ID: 18045113.
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Geonnotti2010
Anthony R. Geonnotti, Miroslawa Bilska, Xing Yuan, Christina Ochsenbauer, Tara G. Edmonds, John C. Kappes, Hua-Xin Liao, Barton F. Haynes, and David C. Montefiori. Differential Inhibition of Human Immunodeficiency Virus Type 1 in Peripheral Blood Mononuclear Cells and TZM-bl Cells by Endotoxin-Mediated Chemokine and Gamma Interferon Production. AIDS Res. Hum. Retroviruses, 26(3):279-291, Mar 2010. PubMed ID: 20218881.
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Georgiev2013
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Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295.
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Elin Solomonovna Gray, Tammy Meyers, Glenda Gray, David Charles Montefiori, and Lynn Morris. Insensitivity of Paediatric HIV-1 Subtype C Viruses to Broadly Neutralising Monoclonal Antibodies Raised against Subtype B. PLoS Med., 3(7):e255, Jul 2006. PubMed ID: 16834457.
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Javier Guenaga and Richard T Wyatt. Structure-Guided Alterations of the gp41-Directed HIV-1 Broadly Neutralizing Antibody 2F5 Reveal New Properties Regarding Its Neutralizing Function. PLoS Pathog, 8(7):e1002806, 2012. PubMed ID: 22829767.
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Gupta2013
Sandeep Gupta, Johannes S. Gach, Juan C. Becerra, Tran B. Phan, Jeffrey Pudney, Zina Moldoveanu, Sarah B. Joseph, Gary Landucci, Medalyn Jude Supnet, Li-Hua Ping, Davide Corti, Brian Moldt, Zdenek Hel, Antonio Lanzavecchia, Ruth M. Ruprecht, Dennis R. Burton, Jiri Mestecky, Deborah J. Anderson, and Donald N. Forthal. The Neonatal Fc Receptor (FcRn) Enhances Human Immunodeficiency Virus Type 1 (HIV-1) Transcytosis across Epithelial Cells. PLoS Pathog., 9(11):e1003776, Nov 2013. PubMed ID: 24278022.
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Elena Gustchina, John M. Louis, Son N. Lam, Carole A. Bewley, and G. Marius Clore. A Monoclonal Fab Derived from a Human Nonimmune Phage Library Reveals a New Epitope on gp41 and Neutralizes Diverse Human Immunodeficiency Virus Type 1 Strains. J. Virol., 81(23):12946-12953, Dec 2007. PubMed ID: 17898046.
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Habte2015
Habtom H. Habte, Saikat Banerjee, Heliang Shi, Yali Qin, and Michael W. Cho. Immunogenic Properties of a Trimeric gp41-Based Immunogen Containing an Exposed Membrane-Proximal External Region. Virology, 486:187-197, Dec 2015. PubMed ID: 26454663.
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Haim2011
Hillel Haim, Bettina Strack, Aemro Kassa, Navid Madani, Liping Wang, Joel R. Courter, Amy Princiotto, Kathleen McGee, Beatriz Pacheco, Michael S. Seaman, Amos B. Smith, 3rd., and Joseph Sodroski. Contribution of Intrinsic Reactivity of the HIV-1 Envelope Glycoproteins to CD4-Independent Infection and Global Inhibitor Sensitivity. PLoS Pathog., 7(6):e1002101, Jun 2011. PubMed ID: 21731494.
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Gregory J. Hardy, Yee Lam, Shelley M. Stewart, Kara Anasti, S. Munir Alam, and Stefan Zauscher. Screening the Interactions between HIV-1 Neutralizing Antibodies and Model Lipid Surfaces. J. Immunol. Methods, 376(1-2):13-19, 28 Feb 2012. PubMed ID: 22033342.
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Haynes2005
Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590.
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Haynes2005a
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Barton F. Haynes, Nathan I. Nicely, and S. Munir Alam. HIV-1 Autoreactive Antibodies: Are They Good or Bad for HIV-1 Prevention? Nat. Struct. Mol. Biol., 17(5):543-545, May 2010. PubMed ID: 20442740.
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Haynes2012
Barton F. Haynes, Garnett Kelsoe, Stephen C. Harrison, and Thomas B. Kepler. B-Cell-Lineage Immunogen Design in Vaccine Development with HIV-1 as a Case Study. Nat. Biotechnol., 30(5):423-433, May 2012. PubMed ID: 22565972.
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Haynes2012a
Barton F. Haynes, Peter B. Gilbert, M. Juliana McElrath, Susan Zolla-Pazner, Georgia D. Tomaras, S. Munir Alam, David T. Evans, David C. Montefiori, Chitraporn Karnasuta, Ruengpueng Sutthent, Hua-Xin Liao, Anthony L. DeVico, George K. Lewis, Constance Williams, Abraham Pinter, Youyi Fong, Holly Janes, Allan DeCamp, Yunda Huang, Mangala Rao, Erik Billings, Nicos Karasavvas, Merlin L. Robb, Viseth Ngauy, Mark S. de Souza, Robert Paris, Guido Ferrari, Robert T. Bailer, Kelly A. Soderberg, Charla Andrews, Phillip W. Berman, Nicole Frahm, Stephen C. De Rosa, Michael D. Alpert, Nicole L. Yates, Xiaoying Shen, Richard A. Koup, Punnee Pitisuttithum, Jaranit Kaewkungwal, Sorachai Nitayaphan, Supachai Rerks-Ngarm, Nelson L. Michael, and Jerome H. Kim. Immune-Correlates Analysis of an HIV-1 Vaccine Efficacy Trial. N. Engl. J. Med., 366(14):1275-1286, 5 Apr 2012. PubMed ID: 22475592.
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Haynes2013
Barton F. Haynes and M. Juliana McElrath. Progress in HIV-1 Vaccine Development. Curr. Opin. HIV AIDS, 8(4):326-332, Jul 2013. PubMed ID: 23743722.
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Haynes2016
Barton F. Haynes, George M. Shaw, Bette Korber, Garnett Kelsoe, Joseph Sodroski, Beatrice H. Hahn, Persephone Borrow, and Andrew J. McMichael. HIV-Host Interactions: Implications for Vaccine Design. Cell Host Microbe, 19(3):292-303, 9 Mar 2016. PubMed ID: 26922989.
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Henderson2019
Rory Henderson, Brian E. Watts, Hieu N. Ergin, Kara Anasti, Robert Parks, Shi-Mao Xia, Ashley Trama, Hua-Xin Liao, Kevin O. Saunders, Mattia Bonsignori, Kevin Wiehe, Barton F. Haynes, and S. Munir Alam. Selection of Immunoglobulin Elbow Region Mutations Impacts Interdomain Conformational Flexibility in HIV-1 Broadly Neutralizing Antibodies. Nat. Commun., 10(1):654, 8 Feb 2019. PubMed ID: 30737386.
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Herrera2005
Carolina Herrera, Per Johan Klasse, Elizabeth Michael, Shivani Kake, Kelly Barnes, Christopher W. Kibler, Lila. Campbell-Gardener, Zhihai Si, Joseph Sodroski, John P. Moore, and Simon Beddows. The Impact of Envelope Glycoprotein Cleavage on the Antigenicity, Infectivity, and Neutralization Sensitivity of Env-Pseudotyped Human Immunodeficiency Virus Type 1 Particles. Virology, 338(1):154-172, 20 Jul 2005. PubMed ID: 15932765.
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Herrera2006
Carolina Herrera, Per Johan Klasse, Christopher W. Kibler, Elizabeth Michael, John P. Moore, and Simon Beddows. Dominant-Negative Effect of Hetero-Oligomerization on the Function of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex. Virology, 351(1):121-132, 20 Jul 2006. PubMed ID: 16616288.
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Hessell2010
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Hicar2010
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Hoffenberg2013
Simon Hoffenberg, Rebecca Powell, Alexei Carpov, Denise Wagner, Aaron Wilson, Sergei Kosakovsky Pond, Ross Lindsay, Heather Arendt, Joanne DeStefano, Sanjay Phogat, Pascal Poignard, Steven P. Fling, Melissa Simek, Celia LaBranche, David Montefiori, Terri Wrin, Pham Phung, Dennis Burton, Wayne Koff, C. Richter King, Christopher L. Parks, and Michael J. Caulfield. Identification of an HIV-1 Clade A Envelope That Exhibits Broad Antigenicity and Neutralization Sensitivity and Elicits Antibodies Targeting Three Distinct Epitopes. J. Virol., 87(10):5372-5383, May 2013. PubMed ID: 23468492.
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R. Hofmann-Lehmann, J. Vlasak, R. A. Rasmussen, B. A. Smith, T. W. Baba, V. Liska, F. Ferrantelli, D. C. Montefiori, H. M. McClure, D. C. Anderson, B. J. Bernacky, T. A. Rizvi, R. Schmidt, L. R. Hill, M. E. Keeling, H. Katinger, G. Stiegler, L. A. Cavacini, M. R. Posner, T. C. Chou, J. Andersen, and R. M. Ruprecht. Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge. J. Virol., 75(16):7470--80, Aug 2001. URL: http://jvi.asm.org/cgi/content/full/75/16/7470. PubMed ID: 11462019.
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Holl2006
Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957.
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Vincent Holl, Maryse Peressin, Sylvie Schmidt, Thomas Decoville, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Efficient Inhibition of HIV-1 Replication in Human Immature Monocyte-Derived Dendritic Cells by Purified Anti-HIV-1 IgG without Induction of Maturation. Blood, 107(11):4466-4474, 1 Jun 2006. PubMed ID: 16469871.
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Qinxue Hu, Naheed Mahmood, and Robin J. Shattock. High-Mannose-Specific Deglycosylation of HIV-1 gp120 Induced by Resistance to Cyanovirin-N and the Impact on Antibody Neutralization. Virology, 368(1):145-154, 10 Nov 2007. PubMed ID: 17658575.
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Bin Hu, Hua-Xin Liao, S. Munir Alam, and Byron Goldstein. Estimating the Probability of Polyreactive Antibodies 4E10 and 2F5 Disabling a gp41 Trimer after T Cell-HIV Adhesion. PLoS Comput. Biol., 10(1):e1003431, Jan 2014. PubMed ID: 24499928.
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Li Huang, Weihong Lai, Phong Ho, and Chin Ho Chen. Induction of a Nonproductive Conformational Change in gp120 by a Small Molecule HIV Type 1 Entry Inhibitor. AIDS Res. Hum. Retroviruses, 23(1):28-32, Jan 2007. PubMed ID: 17263629.
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Jinghe Huang, Gilad Ofek, Leo Laub, Mark K. Louder, Nicole A. Doria-Rose, Nancy S. Longo, Hiromi Imamichi, Robert T. Bailer, Bimal Chakrabarti, Shailendra K. Sharma, S. Munir Alam, Tao Wang, Yongping Yang, Baoshan Zhang, Stephen A. Migueles, Richard Wyatt, Barton F. Haynes, Peter D. Kwong, John R. Mascola, and Mark Connors. Broad and Potent Neutralization of HIV-1 by a gp41-Specific Human Antibody. Nature, 491(7424):406-412, 15 Nov 2012. PubMed ID: 23151583.
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Nerea Huarte, Maier Lorizate, Renate Kunert, and José L. Nieva. Lipid Modulation of Membrane-Bound Epitope Recognition and Blocking by HIV-1 Neutralizing Antibodies. FEBS Lett, 582(27):3798-3804, 12 Nov 2008. PubMed ID: 18930052.
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Nerea Huarte, Maier Lorizate, Rubén Maeso, Renate Kunert, Rocio Arranz, José M. Valpuesta, and José L. Nieva. The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 4E10 Monoclonal Antibody Is Better Adapted to Membrane-Bound Epitope Recognition and Blocking than 2F5. J. Virol., 82(18):8986-8996, Sep 2008. PubMed ID: 18596094.
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Huarte2012
Nerea Huarte, Aitziber Araujo, Rocio Arranz, Maier Lorizate, Heribert Quendler, Renate Kunert, José M. Valpuesta, and José L. Nieva. Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity. PLoS One, 7(12):e52740, 2012. PubMed ID: 23285173.
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M. Huber and A. Trkola. Humoral Immunity to HIV-1: Neutralization and Beyond. J. Intern. Med., 262(1):5-25, Jul 2007. PubMed ID: 17598812.
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Janda2016
Alena Janda, Anthony Bowen, Neil S. Greenspan, and Arturo Casadevall. Ig Constant Region Effects on Variable Region Structure and Function. Front. Microbiol., 7:22, 4 Feb 2016. PubMed ID: 26870003.
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S. A. Jeffs, S. Goriup, B. Kebble, D. Crane, B. Bolgiano, Q. Sattentau, S. Jones, and H. Holmes. Expression and Characterisation of Recombinant Oligomeric Envelope Glycoproteins Derived from Primary Isolates of HIV-1. Vaccine, 22(8):1032-1046, 25 Feb 2004. PubMed ID: 15161081.
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Jenabian2010
Mohammad-Ali Jenabian, Héla Saïdi, Charlotte Charpentier, Hicham Bouhlal, Dominique Schols, Jan Balzarini, Thomas W. Bell, Guido Vanham, and Laurent Bélec. Differential Activity of Candidate Microbicides against Early Steps of HIV-1 Infection upon Complement Virus Opsonization. AIDS Res. Ther., 7:16, 2010. PubMed ID: 20546571.
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S. Jiang, K. Lin, and M. Lu. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 72:10213-7, 1998. MAb NC-1 specifically recognizes the fusogenic core of gp41, which allows for analysis of CD4-induced conformational changes in gp120 and gp41 as well as identification of mediators for HIV-1 fusion. PubMed ID: 9811763.
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Jiang2006
Pengfei Jiang, Yanxia Liu, Xiaolei Yin, Fei Yuan, YuChun Nie, Min Luo, Zheng Aihua, Du Liyin, Mingxiao Ding, and Hongkui Deng. Elicitation of Neutralizing Antibodies by Intranasal Administration of Recombinant Vesicular Stomatitis Virus Expressing Human Immunodeficiency Virus Type 1 gp120. Biochem. Biophys. Res. Commun., 339(2):526-352, 13 Jan 2006. PubMed ID: 16313884.
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Joos2006
Beda Joos, Alexandra Trkola, Herbert Kuster, Leonardo Aceto, Marek Fischer, Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Hermann Katinger, and Huldrych F. Günthard. Long-Term Multiple-Dose Pharmacokinetics of Human Monoclonal Antibodies (MAbs) against Human Immunodeficiency Virus Type 1 Envelope gp120 (MAb 2G12) and gp41 (MAbs 4E10 and 2F5). Antimicrob. Agents Chemother., 50(5):1773-1779, May 2006. PubMed ID: 16641449.
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Joshi2020
Vinita R. Joshi, Ruchi M. Newman, Melissa L. Pack, Karen A. Power, James B. Munro, Ken Okawa, Navid Madani, Joseph G. Sodroski, Aaron G. Schmidt, and Todd M. Allen. Gp41-Targeted Antibodies Restore Infectivity of a Fusion-Deficient HIV-1 Envelope Glycoprotein. PLoS Pathog, 16(5):e1008577, May 2020. PubMed ID: 32392227.
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Joyce2002
Joseph G. Joyce, William M. Hurni, Michael J. Bogusky, Victor M. Garsky, Xiaoping. Liang, Michael P. Citron, Renee C. Danzeisen, Michael D. Miller, John W. Shiver, and Paul M. Keller. Enhancement of Alpha -Helicity in the HIV-1 Inhibitory Peptide DP178 Leads to an Increased Affinity for Human Monoclonal Antibody 2F5 but Does Not Elicit Neutralizing Responses in Vitro: Implications for Vaccine Design. J. Biol. Chem., 277(48):45811-45820, 29 Nov 2002. PubMed ID: 12237296.
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Joyner2011
Amanda S. Joyner, Jordan R. Willis, James E.. Crowe, Jr., and Christopher Aiken. Maturation-Induced Cloaking of Neutralization Epitopes on HIV-1 Particles. PLoS Pathog., 7(9):e1002234, Sep 2011. PubMed ID: 21931551.
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B. Jülg and F. D. Goebel. What's New in HIV/AIDS? Neutralizing HIV Antibodies: Do They Really Protect? Infection, 33(5-6):405-407, Oct 2005. PubMed ID: 16258878.
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Julien2008
Jean-Philippe Julien, Steve Bryson, Jose L. Nieva, and Emil F. Pai. Structural Details of HIV-1 Recognition by the Broadly Neutralizing Monoclonal Antibody 2F5: Epitope Conformation, Antigen-Recognition Loop Mobility, and Anion-Binding Site. J. Mol. Biol., 384(2):377-392, 12 Dec 2008. PubMed ID: 18824005.
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Julien2010
Jean-Philippe Julien, Nerea Huarte, Rubén Maeso, Stefka G. Taneva, Annie Cunningham, José L. Nieva, and Emil F. Pai. Ablation of the Complementarity-Determining Region H3 Apex of the Anti-HIV-1 Broadly Neutralizing Antibody 2F5 Abrogates Neutralizing Capacity without Affecting Core Epitope Binding. J. Virol., 84(9):4136-4147, May 2010. PubMed ID: 20147404.
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Kalia2005
Vandana Kalia, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41. J. Virol., 79(4):2097-2107, Feb 2005. PubMed ID: 15681412.
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Kanduc2008
Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732.
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Kang2005
Sang-Moo Kang, Fu Shi Quan, Chunzi Huang, Lizheng Guo, Ling Ye, Chinglai Yang, and Richard W. Compans. Modified HIV Envelope Proteins with Enhanced Binding to Neutralizing Monoclonal Antibodies. Virology, 331(1):20-32, 5 Jan 2005. PubMed ID: 15582650.
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Kang2009
Yun Kenneth Kang, Sofija Andjelic, James M. Binley, Emma T. Crooks, Michael Franti, Sai Prasad N. Iyer, Gerald P. Donovan, Antu K. Dey, Ping Zhu, Kenneth H. Roux, Robert J. Durso, Thomas F. Parsons, Paul J. Maddon, John P. Moore, and William C. Olson. Structural and Immunogenicity Studies of a Cleaved, Stabilized Envelope Trimer Derived from Subtype A HIV-1. Vaccine, 27(37):5120-5132, 13 Aug 2009. PubMed ID: 19567243.
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Keele2008
Brandon F. Keele, Elena E. Giorgi, Jesus F. Salazar-Gonzalez, Julie M. Decker, Kimmy T. Pham, Maria G. Salazar, Chuanxi Sun, Truman Grayson, Shuyi Wang, Hui Li, Xiping Wei, Chunlai Jiang, Jennifer L. Kirchherr, Feng Gao, Jeffery A. Anderson, Li-Hua Ping, Ronald Swanstrom, Georgia D. Tomaras, William A. Blattner, Paul A. Goepfert, J. Michael Kilby, Michael S. Saag, Eric L. Delwart, Michael P. Busch, Myron S. Cohen, David C. Montefiori, Barton F. Haynes, Brian Gaschen, Gayathri S. Athreya, Ha Y. Lee, Natasha Wood, Cathal Seoighe, Alan S. Perelson, Tanmoy Bhattacharya, Bette T. Korber, Beatrice H. Hahn, and George M. Shaw. Identification and Characterization of Transmitted and Early Founder Virus Envelopes in Primary HIV-1 Infection. Proc. Natl. Acad. Sci. U.S.A., 105(21):7552-7557, 27 May 2008. PubMed ID: 18490657.
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Kelsoe2017
Garnett Kelsoe and Barton F. Haynes. Host Controls of HIV Broadly Neutralizing Antibody Development. Immunol. Rev., 275(1):79-88, Jan 2017. PubMed ID: 28133807.
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J. A. Kessler, II, P. M. McKenna, E. A. Emini, and A. J. Conley. In vitro assessment of the therapeutic potential of anti-HIV-1 monoclonal neutralizing antibodies. Gen. Meet. Am. Soc. Microbiol., 95:586, T-25, 1995. Aidsline: 96050622 Abstract.
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J. A. Kessler II, P. M. McKenna, E. A. Emini, C. P. Chan, M. D. Patel, S. K. Gupta, G. E. Mark III, C. F. Barbas III, D. R. Burton, and A. J. Conley. Recombinant human monoclonal antibody IgG1b12 neutralizes diverse human immunodeficiency virus type 1 primary isolates. AIDS Res. Hum. Retroviruses, 13:575-82, 1997. Anti-CD4 binding domain antibodies generally do not neutralize primary HIV-1 isolates, with the exception of IgG1b12. Many primary isolates were shown to be neutralized by IgG1b12, including several non-B clade international isolates. Neutralization of a primary isolate with MAb IgG1b12 did not require continuous exposure to the antibody. A complete IgG1 molecule of a selected b12 FAb mutant with a > 400-fold increase in affinity was assembled and evaluated in the infectivity reduction assay in comparative studies with the parent IgG1b12 antibody. The mutant did not retain the level of primary isolate neutralization potency of IgG1b12, despite the increase in affinity for gp120. PubMed ID: 9135875.
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Kim2005
Mikyung Kim, Zhi-Song Qiao, David C. Montefiori, Barton F. Haynes, Ellis L. Reinherz, and Hua-Xin Liao. Comparison of HIV Type 1 ADA gp120 Monomers Versus gp140 Trimers as Immunogens for the Induction of Neutralizing Antibodies. AIDS Res. Hum. Retroviruses, 21(1):58-67, Jan 2005. PubMed ID: 15665645.
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Kim2007
Mikyung Kim, Zhisong Qiao, Jessica Yu, David Montefiori, and Ellis L. Reinherz. Immunogenicity of Recombinant Human Immunodeficiency Virus Type 1-Like Particles Expressing gp41 Derivatives in a Pre-Fusion State. Vaccine, 25(27):5102-5114, 28 Jun 2007. PubMed ID: 17055621.
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Kirchherr2007
Jennifer L. Kirchherr, Xiaozhi Lu, Webster Kasongo, Victor Chalwe, Lawrence Mwananyanda, Rosemary M. Musonda, Shi-Mao Xia, Richard M. Scearce, Hua-Xin Liao, David C. Montefiori, Barton F. Haynes, and Feng Gao. High Throughput Functional Analysis of HIV-1 env Genes Without Cloning. J. Virol. Methods, 143(1):104-111, Jul 2007. PubMed ID: 17416428.
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Kishko2011
Michael Kishko, Mohan Somasundaran, Frank Brewster, John L. Sullivan, Paul R. Clapham, and Katherine Luzuriaga. Genotypic and Functional Properties of Early Infant HIV-1 Envelopes. Retrovirology, 8:67, 2011. PubMed ID: 21843318.
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Moiz Kitabwalla, Flavia Ferrantelli, Tao Wang, Alistair Chalmers, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Ting-Chao Chou, and Ruth M. Ruprecht. Primary African HIV Clade A and D Isolates: Effective Cross-Clade Neutralization with a Quadruple Combination of Human Monoclonal Antibodies Raised against Clade B. AIDS Res. Hum. Retroviruses, 19(2):125-131, Feb 2003. PubMed ID: 12639248.
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P. Klasse, J. A. McKeating, M. Schutten, M. S. Reitz, Jr., and M. Robert-Guroff. An Immune-Selected Point Mutation in the Transmembrane Protein of Human Immunodeficiency Virus Type 1 (HXB2-Env:Ala 582(--> Thr)) Decreases Viral Neutralization by Monoclonal Antibodies to the CD4-Binding Site. Virology, 196:332-337, 1993. PubMed ID: 8356803.
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Klein2010
Joshua S. Klein and Pamela J. Bjorkman. Few and Far Between: How HIV May Be Evading Antibody Avidity. PLoS Pathog., 6(5):e1000908, May 2010. PubMed ID: 20523901.
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Klein2013
Florian Klein, Ron Diskin, Johannes F. Scheid, Christian Gaebler, Hugo Mouquet, Ivelin S. Georgiev, Marie Pancera, Tongqing Zhou, Reha-Baris Incesu, Brooks Zhongzheng Fu, Priyanthi N. P. Gnanapragasam, Thiago Y. Oliveira, Michael S. Seaman, Peter D. Kwong, Pamela J. Bjorkman, and Michel C. Nussenzweig. Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization. Cell, 153(1):126-138, 28 Mar 2013. PubMed ID: 23540694.
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Willie W. L. Koh, Anna Forsman, Stéphane Hué, Gisela J. van der Velden, David L. Yirrell, Áine McKnight, Robin A. Weiss, and Marlén M. I. Aasa-Chapman. Novel Subtype C Human Immunodeficiency Virus Type 1 Envelopes Cloned Directly from Plasma: Coreceptor Usage and Neutralization Phenotypes. J. Gen. Virol., 91(9):2374-2380, Sep 2010. PubMed ID: 20484560.
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P. Kolchinsky, E. Kiprilov, P. Bartley, R. Rubinstein, and J. Sodroski. Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops. J. Virol., 75(7):3435--43, Apr 2001. URL: http://jvi.asm.org/cgi/content/full/75/7/3435. PubMed ID: 11238869.
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Bette Korber and S. Gnanakaran. The Implications of Patterns in HIV Diversity for Neutralizing Antibody Induction and Susceptibility. Curr. Opin. HIV AIDS, 4(5):408-417, Sep 2009. PubMed ID: 20048705.
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Kothe2007
Denise L. Kothe, Julie M Decker, Yingying Li, Zhiping Weng, Frederic Bibollet-Ruche, Kenneth P. Zammit, Maria G. Salazar, Yalu Chen, Jesus F. Salazar-Gonzalez, Zina Moldoveanu, Jiri Mestecky, Feng Gao, Barton F. Haynes, George M. Shaw, Mark Muldoon, Bette T. M. Korber, and Beatrice H. Hahn. Antigenicity and Immunogenicity of HIV-1 Consensus Subtype B Envelope Glycoproteins. Virology, 360(1):218-234, 30 Mar 2007. PubMed ID: 17097711.
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Kovacs2012
James M. Kovacs, Joseph P. Nkolola, Hanqin Peng, Ann Cheung, James Perry, Caroline A. Miller, Michael S. Seaman, Dan H. Barouch, and Bing Chen. HIV-1 Envelope Trimer Elicits More Potent Neutralizing Antibody Responses than Monomeric gp120. Proc. Natl. Acad. Sci. U.S.A., 109(30):12111-12116, 24 Jul 2012. PubMed ID: 22773820.
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Krachmarov2005
Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306.
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Kraft2007
Zane Kraft, Nina R. Derby, Ruth A. McCaffrey, Rachel Niec, Wendy M. Blay, Nancy L. Haigwood, Eirini Moysi, Cheryl J. Saunders, Terri Wrin, Christos J. Petropoulos, M. Juliana McElrath, and Leonidas Stamatatos. Macaques Infected with a CCR5-Tropic Simian/Human Immunodeficiency Virus (SHIV) Develop Broadly Reactive Anti-HIV Neutralizing Antibodies. J. Virol., 81(12):6402-6411, Jun 2007. PubMed ID: 17392364.
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Kramer2007
Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119.
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Krebs2019
Shelly J. Krebs, Young D. Kwon, Chaim A. Schramm, William H. Law, Gina Donofrio, Kenneth H. Zhou, Syna Gift, Vincent Dussupt, Ivelin S. Georgiev, Sebastian Schätzle, Jonathan R. McDaniel, Yen-Ting Lai, Mallika Sastry, Baoshan Zhang, Marissa C. Jarosinski, Amy Ransier, Agnes L. Chenine, Mangaiarkarasi Asokan, Robert T. Bailer, Meera Bose, Alberto Cagigi, Evan M. Cale, Gwo-Yu Chuang, Samuel Darko, Jefferson I. Driscoll, Aliaksandr Druz, Jason Gorman, Farida Laboune, Mark K. Louder, Krisha McKee, Letzibeth Mendez, M. Anthony Moody, Anne Marie O'Sullivan, Christopher Owen, Dongjun Peng, Reda Rawi, Eric Sanders-Buell, Chen-Hsiang Shen, Andrea R. Shiakolas, Tyler Stephens, Yaroslav Tsybovsky, Courtney Tucker, Raffaello Verardi, Keyun Wang, Jing Zhou, Tongqing Zhou, George Georgiou, S Munir Alam, Barton F. Haynes, Morgane Rolland, Gary R. Matyas, Victoria R. Polonis, Adrian B. McDermott, Daniel C. Douek, Lawrence Shapiro, Sodsai Tovanabutra, Nelson L. Michael, John R. Mascola, Merlin L. Robb, Peter D. Kwong, and Nicole A. Doria-Rose. Longitudinal Analysis Reveals Early Development of Three MPER-Directed Neutralizing Antibody Lineages from an HIV-1-Infected Individual. Immunity, 50(3):677-691.e13, 19 Mar 2019. PubMed ID: 30876875.
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Kulkarni2009
Smita S. Kulkarni, Alan Lapedes, Haili Tang, S. Gnanakaran, Marcus G. Daniels, Ming Zhang, Tanmoy Bhattacharya, Ming Li, Victoria R. Polonis, Francine E. McCutchan, Lynn Morris, Dennis Ellenberger, Salvatore T. Butera, Robert C. Bollinger, Bette T. Korber, Ramesh S. Paranjape, and David C. Montefiori. Highly Complex Neutralization Determinants on a Monophyletic Lineage of Newly Transmitted Subtype C HIV-1 Env Clones from India. Virology, 385(2):505-520, 15 Mar 2009. PubMed ID: 19167740.
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Kumar2018
Amit Kumar, Claire E. P. Smith, Elena E. Giorgi, Joshua Eudailey, David R. Martinez, Karina Yusim, Ayooluwa O. Douglas, Lisa Stamper, Erin McGuire, Celia C. LaBranche, David C. Montefiori, Genevieve G. Fouda, Feng Gao, and Sallie R. Permar. Infant Transmitted/Founder HIV-1 Viruses from Peripartum Transmission Are Neutralization Resistant to Paired Maternal Plasma. PLoS Pathog., 14(4):e1006944, Apr 2018. PubMed ID: 29672607.
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Kunert1998
R. Kunert, F. Ruker, and H. Katinger. Molecular Characterization of Five Neutralizing Anti-HIV Type 1 Antibodies: Identification of Nonconventional D Segments in the Human Monoclonal Antibodies 2G12 and 2F5. AIDS Res. Hum. Retroviruses, 14:1115-1128, 1998. Study identifies five human MAbs which were able to neutralize primary isolates of different clades in vitro and reports the nucleotide and amino acid sequences of the heavy and light chain V segments of the antibodies. PubMed ID: 9737583.
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Kunert2000
R. Kunert, W. Steinfellner, M. Purtscher, A. Assadian, and H. Katinger. Stable recombinant expression of the anti HIV-1 monoclonal antibody 2F5 after IgG3/IgG1 subclass switch in CHO cells. Biotechnol. Bioeng., 67:97-103, 2000. PubMed ID: 10581440.
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Kunert2002
Renate E. Kunert, Robert Weik, Boris Ferko, Gabriela Stiegler, and Hermann Katinger. Anti-Idiotypic Antibody Ab2/3H6 Mimics the Epitope of the Neutralizing Anti-HIV-1 Monoclonal Antibody 2F5. AIDS, 16(4):667-668, 8 Mar 2002. PubMed ID: 11873012.
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Kunert2011
Renate Kunert and Alexander Mader. Anti-Idiotypic Antibody Ab2/3H6 Mimicking gp41: A Potential HIV-1 vaccine? BMC Proc, 5(Suppl 8):P64, 22 Nov 2011. PubMed ID: 22373352.
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Kwong2009a
Peter D. Kwong and Ian A. Wilson. HIV-1 and Influenza Antibodies: Seeing Antigens in New Ways. Nat. Immunol., 10(6):573-578, Jun 2009. PubMed ID: 19448659.
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Kwong2011
Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Rational Design of Vaccines to Elicit Broadly Neutralizing Antibodies to HIV-1. Cold Spring Harb. Perspect. Med., 1(1):a007278, Sep 2011. PubMed ID: 22229123.
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Kwong2012
Peter D. Kwong and John R. Mascola. Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies. Immunity, 37(3):412-425, 21 Sep 2012. PubMed ID: 22999947.
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Kwong2013
Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Broadly Neutralizing Antibodies and the Search for an HIV-1 Vaccine: The End of the Beginning. Nat. Rev. Immunol., 13(9):693-701, Sep 2013. PubMed ID: 23969737.
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Laal1994
Suman Laal, Sherri Burda, Miroslav K. Gorny, Sylwia Karwowska, Aby Buchbinder, and Susan Zolla-Pazner. Synergistic Neutralization of Human Immunodeficiency Virus Type 1 by Combinations of Human Monoclonal Antibodies. J. Virol., 68(6):4001-4008, Jun 1994. PubMed ID: 7514683.
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Laurel A. Lagenaur, Vadim A. Villarroel, Virgilio Bundoc, Barna Dey, and Edward A. Berger. sCD4-17b Bifunctional Protein: Extremely Broad and Potent Neutralization of HIV-1 Env Pseudotyped Viruses from Genetically Diverse Primary Isolates. Retrovirology, 7:11, 2010. PubMed ID: 20158904.
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Lai2011
Rachel P. J. Lai, Jin Yan, Jonathan Heeney, Myra O. McClure, Heinrich Göttlinger, Jeremy Luban, and Massimo Pizzato. Nef Decreases HIV-1 Sensitivity to Neutralizing Antibodies that Target the Membrane-Proximal External Region of TMgp41. PLoS Pathog, 7(12):e1002442, Dec 2011. PubMed ID: 22194689.
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Lai2012
Rachel P. J. Lai, Michael S. Seaman, Paul Tonks, Frank Wegmann, David J. Seilly, Simon D. W. Frost, Celia C. LaBranche, David C. Montefiori, Antu K. Dey, Indresh K. Srivastava, Quentin Sattentau, Susan W. Barnett, and Jonathan L. Heeney. Mixed Adjuvant Formulations Reveal a New Combination That Elicit Antibody Response Comparable to Freund's Adjuvants. PLoS One, 7(4):e35083, 2012. PubMed ID: 22509385.
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Lambotte2009
Olivier Lambotte, Guido Ferrari, Christiane Moog, Nicole L. Yates, Hua-Xin Liao, Robert J. Parks, Charles B. Hicks, Kouros Owzar, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, and Jean-François Delfraissy. Heterogeneous Neutralizing Antibody and Antibody-Dependent Cell Cytotoxicity Responses in HIV-1 Elite Controllers. AIDS, 23(8):897-906, 15 May 2009. PubMed ID: 19414990.
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Lapelosa2009
Mauro Lapelosa, Emilio Gallicchio, Gail Ferstandig Arnold, Eddy Arnold, and Ronald M. Levy. In Silico Vaccine Design Based on Molecular Simulations of Rhinovirus Chimeras Presenting HIV-1 gp41 Epitopes. J. Mol. Biol., 385(2):675-691, 16 Jan 2009. PubMed ID: 19026659.
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Lapelosa2010
Mauro Lapelosa, Gail Ferstandig Arnold, Emilio Gallicchio, Eddy Arnold, and Ronald M. Levy. Antigenic Characteristics of Rhinovirus Chimeras Designed In Silico for Enhanced Presentation of HIV-1 gp41 Epitopes. J. Mol. Biol., 397(3):752-766, 2 Apr 2010. PubMed ID: 20138057.
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Lavine2012
Christy L. Lavine, Socheata Lao, David C. Montefiori, Barton F. Haynes, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI). High-Mannose Glycan-Dependent Epitopes Are Frequently Targeted in Broad Neutralizing Antibody Responses during Human Immunodeficiency Virus Type 1 Infection. J. Virol., 86(4):2153-2164, Feb 2012. PubMed ID: 22156525.
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Mansun Law, Rosa M. F. Cardoso, Ian A. Wilson, and Dennis R. Burton. Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy. J. Virol., 81(8):4272-4285, Apr 2007. PubMed ID: 17267498.
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Leaman2010
Daniel P. Leaman, Heather Kinkead, and Michael B. Zwick. In-Solution Virus Capture Assay Helps Deconstruct Heterogeneous Antibody Recognition of Human Immunodeficiency Virus Type 1. J. Virol., 84(7):3382-3395, Apr 2010. PubMed ID: 20089658.
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Leaman2013
Daniel P. Leaman and Michael B. Zwick. Increased Functional Stability and Homogeneity of Viral Envelope Spikes through Directed Evolution. PLoS Pathog., 9(2):e1003184, Feb 2013. PubMed ID: 23468626.
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Oliver Lenz, Matthias T Dittmar, Andreas Wagner, Boris Ferko, Karola Vorauer-Uhl, Gabriela Stiegler, and Winfried Weissenhorn. Trimeric Membrane-Anchored gp41 Inhibits HIV Membrane Fusion. J. Biol. Chem., 280(6):4095-4101, 11 Feb 2005. PubMed ID: 15574416.
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A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic Neutralization of a Chimeric SIV/HIV Type 1 Virus with Combinations of Human Anti-HIV Type 1 Envelope Monoclonal Antibodies or Hyperimmune Globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233.
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Li1998
A. Li, H. Katinger, M. R. Posner, L. Cavacini, S. Zolla-Pazner, M. K. Gorny, J. Sodroski, T. C. Chou, T. W. Baba, and R. M. Ruprecht. Synergistic Neutralization of Simian-Human Immunodeficiency Virus SHIV-vpu+ by Triple and Quadruple Combinations of Human Monoclonal Antibodies and High-Titer Anti-Human Immunodeficiency Virus Type 1 Immunoglobulins. J. Virol., 72:3235-3240, 1998. PubMed ID: 9525650.
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Li2002
Hua Li, Zu-Qiang Liu, Jian Ding, and Ying-Hua Chen. Recombinant Multi-Epitope Vaccine Induce Predefined Epitope-Specific Antibodies against HIV-1. Immunol. Lett., 84(2):153-157, 1 Nov 2002. PubMed ID: 12270553.
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Li2005a
Ming Li, Feng Gao, John R. Mascola, Leonidas Stamatatos, Victoria R. Polonis, Marguerite Koutsoukos, Gerald Voss, Paul Goepfert, Peter Gilbert, Kelli M. Greene, Miroslawa Bilska, Denise L Kothe, Jesus F. Salazar-Gonzalez, Xiping Wei, Julie M. Decker, Beatrice H. Hahn, and David C. Montefiori. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 79(16):10108-10125, Aug 2005. PubMed ID: 16051804.
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Li2006a
Ming Li, Jesus F. Salazar-Gonzalez, Cynthia A. Derdeyn, Lynn Morris, Carolyn Williamson, James E. Robinson, Julie M. Decker, Yingying Li, Maria G. Salazar, Victoria R. Polonis, Koleka Mlisana, Salim Abdool Karim, Kunxue Hong, Kelli M. Greene, Miroslawa Bilska, Jintao Zhou, Susan Allen, Elwyn Chomba, Joseph Mulenga, Cheswa Vwalika, Feng Gao, Ming Zhang, Bette T. M. Korber, Eric Hunter, Beatrice H. Hahn, and David C. Montefiori. Genetic and Neutralization Properties of Subtype C Human Immunodeficiency Virus Type 1 Molecular env Clones from Acute and Early Heterosexually Acquired Infections in Southern Africa. J. Virol., 80(23):11776-11790, Dec 2006. PubMed ID: 16971434.
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Li2009c
Yuxing Li, Krisha Svehla, Mark K. Louder, Diane Wycuff, Sanjay Phogat, Min Tang, Stephen A. Migueles, Xueling Wu, Adhuna Phogat, George M. Shaw, Mark Connors, James Hoxie, John R. Mascola, and Richard Wyatt. Analysis of Neutralization Specificities in Polyclonal Sera Derived from Human Immunodeficiency Virus Type 1-Infected Individuals. J Virol, 83(2):1045-1059, Jan 2009. PubMed ID: 19004942.
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Li2017
Hongru Li, Chati Zony, Ping Chen, and Benjamin K. Chen. Reduced Potency and Incomplete Neutralization of Broadly Neutralizing Antibodies against Cell-to-Cell Transmission of HIV-1 with Transmitted Founder Envs. J. Virol., 91(9), 1 May 2017. PubMed ID: 28148796.
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Liao2000
M. Liao, Y. Lu, Y. Xiao, M. P. Dierich, and Y. Chen. Induction of High Level of Specific Antibody Response to the Neutralizing Epitope ELDKWA on HIV-1 gp41 by Peptide-Vaccine. Peptides, 21:463-468, 2000. PubMed ID: 10822100.
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Liao2004
Hua-Xin Liao, S Munir Alam, John R. Mascola, James Robinson, Benjiang Ma, David C. Montefiori, Maria Rhein, Laura L. Sutherland, Richard Scearce, and Barton F. Haynes. Immunogenicity of Constrained Monoclonal Antibody A32-Human Immunodeficiency Virus (HIV) Env gp120 Complexes Compared to That of Recombinant HIV Type 1 gp120 Envelope Glycoproteins. J. Virol., 78(10):5270-5278, May 2004. PubMed ID: 15113908.
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Liao2006
Hua-Xin Liao, Laura L. Sutherland, Shi-Mao Xia, Mary E. Brock, Richard M. Scearce, Stacie Vanleeuwen, S. Munir Alam, Mildred McAdams, Eric A. Weaver, Zenaido Camacho, Ben-Jiang Ma, Yingying Li, Julie M. Decker, Gary J. Nabel, David C. Montefiori, Beatrice H. Hahn, Bette T. Korber, Feng Gao, and Barton F. Haynes. A Group M Consensus Envelope Glycoprotein Induces Antibodies That Neutralize Subsets of Subtype B and C HIV-1 Primary Viruses. Virology, 353(2):268-282, 30 Sep 2006. PubMed ID: 17039602.
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Liao2009
Hua-Xin Liao, Marc C. Levesque, Ashleigh Nagel, Ashlyn Dixon, Ruijun Zhang, Emmanuel Walter, Robert Parks, John Whitesides, Dawn J. Marshall, Kwan-Ki Hwang, Yi Yang, Xi Chen, Feng Gao, Supriya Munshaw, Thomas B. Kepler, Thomas Denny, M. Anthony Moody, and Barton F. Haynes. High-Throughput Isolation of Immunoglobulin Genes from Single Human B Cells and Expression as Monoclonal Antibodies. J. Virol. Methods, 158(1-2):171-179, Jun 2009. PubMed ID: 19428587.
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Liao2013c
Hua-Xin Liao, Chun-Yen Tsao, S. Munir Alam, Mark Muldoon, Nathan Vandergrift, Ben-Jiang Ma, Xiaozhi Lu, Laura L. Sutherland, Richard M. Scearce, Cindy Bowman, Robert Parks, Haiyan Chen, Julie H. Blinn, Alan Lapedes, Sydeaka Watson, Shi-Mao Xia, Andrew Foulger, Beatrice H. Hahn, George M. Shaw, Ron Swanstrom, David C. Montefiori, Feng Gao, Barton F. Haynes, and Bette Korber. Antigenicity and Immunogenicity of Transmitted/Founder, Consensus, and Chronic Envelope Glycoproteins of Human Immunodeficiency Virus Type 1. J. Virol., 87(8):4185-4201, Apr 2013. PubMed ID: 23365441.
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Lin2007
George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109.
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Ling2004
Hong Ling, Peng Xiao, Osamu Usami, and Toshio Hattori. Thrombin Activates Envelope Glycoproteins of HIV Type 1 and Enhances Fusion. Microbes Infect., 6(5):414-420, Apr 2004. PubMed ID: 15109955.
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Liu2002
Xiao Song Liu, Wen Jun Liu, Kong Nan Zhao, Yue Hua Liu, Graham Leggatt, and Ian H. Frazer. Route of Administration of Chimeric BPV1 VLP Determines the Character of the Induced Immune Responses. Immunol. Cell Biol., 80(1):21-9, Feb 2002. PubMed ID: 11869359.
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Liu2005a
Zuqiang Liu, Zuguang Wang, and Ying-Hua Chen. Predefined Spacers between Epitopes on a Recombinant Epitope-Peptide Impacted Epitope-Specific Antibody Response. Immunol. Lett., 97(1):41-45, 15 Feb 2005. PubMed ID: 15626474.
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Liu2009
Jie Liu, Yiqun Deng, Antu K. Dey, John P. Moore, and Min Lu. Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation. Biochemistry, 48(13):2915-2923, 7 Apr 2009. PubMed ID: 19226163.
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Liu2010
Jie Liu, Yiqun Deng, Qunnu Li, Antu K. Dey, John P. Moore, and Min Lu. Role of a Putative gp41 Dimerization Domain in Human Immunodeficiency Virus Type 1 Membrane Fusion. J. Virol., 84(1):201-209, Jan 2010. PubMed ID: 19846514.
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Liu2015a
Mengfei Liu, Guang Yang, Kevin Wiehe, Nathan I. Nicely, Nathan A. Vandergrift, Wes Rountree, Mattia Bonsignori, S. Munir Alam, Jingyun Gao, Barton F. Haynes, and Garnett Kelsoe. Polyreactivity and Autoreactivity among HIV-1 Antibodies. J. Virol., 89(1):784-798, Jan 2015. PubMed ID: 25355869.
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Lorin2004
Clarisse Lorin, Lucile Mollet, Frédéric Delebecque, Chantal Combredet, Bruno Hurtrel, Pierre Charneau, Michel Brahic, and Frédéric Tangy. A Single Injection of Recombinant Measles Virus Vaccines Expressing Human Immunodeficiency Virus (HIV) Type 1 Clade B Envelope Glycoproteins Induces Neutralizing Antibodies and Cellular Immune Responses to HIV. J. Virol., 78(1):146-157, Jan 2004. PubMed ID: 14671096.
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Lorizate2006
Maier Lorizate, Antonio Cruz, Nerea Huarte, Renate Kunert, Jesús Pérez-Gil, and José L. Nieva. Recognition and Blocking of HIV-1 gp41 Pre-Transmembrane Sequence by Monoclonal 4E10 Antibody in a Raft-Like Membrane Environment. J. Biol. Chem., 281(51):39598-39606, 22 Dec 2006. PubMed ID: 17050535.
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Lorizate2006a
Maier Lorizate, Igor de la Arada, Nerea Huarte, Silvia Sánchez-Martínez, Beatriz G. de la Torre, David Andreu, José L. R. Arrondo, and José L. Nieva. Structural Analysis and Assembly of the HIV-1 Gp41 Amino-Terminal Fusion Peptide and the Pretransmembrane Amphipathic-At-Interface Sequence. Biochemistry, 45(48):14337-14346, 5 Dec 2006. PubMed ID: 17128972.
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Louder2005
Mark K. Louder, Anna Sambor, Elena Chertova, Tai Hunte, Sarah Barrett, Fallon Ojong, Eric Sanders-Buell, Susan Zolla-Pazner, Francine E. McCutchan, James D. Roser, Dana Gabuzda, Jeffrey D. Lifson, and John R. Mascola. HIV-1 Envelope Pseudotyped Viral Vectors and Infectious Molecular Clones Expressing the Same Envelope Glycoprotein Have a Similar Neutralization Phenotype, but Culture in Peripheral Blood Mononuclear Cells Is Associated with Decreased Neutralization Sensitivity. Virology, 339(2):226-238, 1 Sep 2005. PubMed ID: 16005039.
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Louis2005
John M. Louis, Carole A. Bewley, Elena Gustchina, Annie Aniana, and G. Marius Clore. Characterization and HIV-1 Fusion Inhibitory Properties of Monoclonal Fabs Obtained from a Human Non-Immune Phage Library Selected against Diverse Epitopes of the Ectodomain of HIV-1 gp41. J. Mol. Biol., 353(5):945-951, 11 Nov 2005. PubMed ID: 16216270.
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Lovelace2011
Erica Lovelace, Hengyu Xu, Catherine A. Blish, Roland Strong, and Julie Overbaugh. The Role of Amino Acid Changes in the Human Immunodeficiency Virus Type 1 Transmembrane Domain in Antibody Binding and Neutralization. Virology, 421(2):235-244, 20 Dec 2011. PubMed ID: 22029936.
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Lu2000a
Y. Lu, Y. Xiao, J. Ding, M. P. Dierich, and Y. H. Chen. Multiepitope vaccines intensively increased levels of antibodies recognizing three neutralizing epitopes on human immunodeficiency virus-1 envelope protein. Scand. J. Immunol., 51:497-501, 2000. PubMed ID: 10792842.
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Lu2000b
Y. Lu, Y. Xiao, J. Ding, M. Dierich, and Y. H. Chen. Immunogenicity of neutralizing epitopes on multiple-epitope vaccines against HIV-1. Int. Arch. Allergy Immunol., 121:80-84, 2000. PubMed ID: 10686512.
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Luallen2009
Robert J. Luallen, Hu Fu, Caroline Agrawal-Gamse, Innocent Mboudjeka, Wei Huang, Fang-Hua Lee, Lai-Xi Wang, Robert W. Doms, and Yu Geng. A Yeast Glycoprotein Shows High-Affinity Binding to the Broadly Neutralizing Human Immunodeficiency Virus Antibody 2G12 and Inhibits gp120 Interactions with 2G12 and DC-SIGN. J. Virol., 83(10):4861-4870, May 2009. PubMed ID: 19264785.
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Luo2006
Min Luo, Fei Yuan, Yanxia Liu, Siming Jiang, Xijun Song, Pengfei Jiang, Xiaolei Yin, Mingxiao Ding, and Hongkui Deng. Induction of Neutralizing Antibody against Human Immunodeficiency Virus Type 1 (HIV-1) by Immunization with gp41 Membrane-Proximal External Region (MPER) Fused with Porcine Endogenous Retrovirus (PERV) p15E Fragment. Vaccine, 24(4):4354-4342, 23 Jan 2006. PubMed ID: 16143433.
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Lusso2005
Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935.
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Lynch2011
John B. Lynch, Ruth Nduati, Catherine A. Blish, Barbra A. Richardson, Jennifer M. Mabuka, Zahra Jalalian-Lechak, Grace John-Stewart, and Julie Overbaugh. The Breadth and Potency of Passively Acquired Human Immunodeficiency Virus Type 1-Specific Neutralizing Antibodies Do Not Correlate with the Risk of Infant Infection. J. Virol., 85(11):5252-5261, Jun 2011. PubMed ID: 21411521.
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Ma2011
Ben-Jiang Ma, S. Munir Alam, Eden P. Go, Xiaozhi Lu, Heather Desaire, Georgia D. Tomaras, Cindy Bowman, Laura L. Sutherland, Richard M. Scearce, Sampa Santra, Norman L. Letvin, Thomas B. Kepler, Hua-Xin Liao, and Barton F. Haynes. Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog., 7(9):e1002200, Sep 2011. PubMed ID: 21909262.
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Mader2010
A. Mader and R. Kunert. Humanization Strategies for an Anti-Idiotypic Antibody Mimicking HIV-1 gp41. Protein Eng. Des. Sel., 23(12):947-954, Dec 2010. PubMed ID: 21037278.
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Magnus2010
Carsten Magnus and Roland R. Regoes. Estimating the Stoichiometry of HIV Neutralization. PLoS Comput. Biol., 6(3):e1000713, Mar 2010. PubMed ID: 20333245.
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Magnus2016
Carsten Magnus, Lucia Reh, and Alexandra Trkola. HIV-1 Resistance to Neutralizing Antibodies: Determination of Antibody Concentrations Leading to Escape Mutant Evolution. Virus Res., 218:57-70, 15 Jun 2016. PubMed ID: 26494166.
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Malherbe2014
Delphine C. Malherbe, Franco Pissani, D. Noah Sather, Biwei Guo, Shilpi Pandey, William F. Sutton, Andrew B. Stuart, Harlan Robins, Byung Park, Shelly J. Krebs, Jason T. Schuman, Spyros Kalams, Ann J. Hessell, and Nancy L. Haigwood. Envelope variants circulating as initial neutralization breadth developed in two HIV-infected subjects stimulate multiclade neutralizing antibodies in rabbits. J Virol, 88(22):12949-67 doi, Nov 2014. PubMed ID: 25210191
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Mann2009
Axel M. Mann, Peter Rusert, Livia Berlinger, Herbert Kuster, Huldrych F. Günthard, and Alexandra Trkola. HIV Sensitivity to Neutralization Is Determined by Target and Virus Producer Cell Properties. AIDS, 23(13):1659-1667, 24 Aug 2009. PubMed ID: 19581791.
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Martin2011
Grégoire Martin, Brian Burke, Robert Thaï, Antu K. Dey, Olivier Combes, Bernadette Heyd, Anthony R. Geonnotti, David C. Montefiori, Elaine Kan, Ying Lian, Yide Sun, Toufik Abache, Jeffrey B. Ulmer, Hocine Madaoui, Raphaël Guérois, Susan W. Barnett, Indresh K. Srivastava, Pascal Kessler, and Loïc Martin. Stabilization of HIV-1 Envelope in the CD4-Bound Conformation through Specific Cross-Linking of a CD4 Mimetic. J. Biol. Chem., 286(24):21706-21716, 17 Jun 2011. PubMed ID: 21487012.
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Martinez2009
Valérie Martinez, Marie-Claude Diemert, Martine Braibant, Valérie Potard, Jean-Luc Charuel, Francis Barin, Dominique Costagliola, Eric Caumes, Jean-Pierre Clauvel, Brigitte Autran, Lucile Musset, and ALT ANRS CO15 Study Group. Anticardiolipin Antibodies in HIV Infection Are Independently Associated with Antibodies to the Membrane Proximal External Region of gp41 and with Cell-Associated HIV DNA and Immune Activation. Clin. Infect. Dis., 48(1):123-32, 1 Jan 2009. PubMed ID: 19035778.
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Marusic2009
Carla Marusic, Alessandro Vitale, Emanuela Pedrazzini, Marcello Donini, Lorenzo Frigerio, Ralph Bock, Philip J. Dix, Matthew S. McCabe, Michele Bellucci, and Eugenio Benvenuto. Plant-Based Strategies Aimed at Expressing HIV Antigens and Neutralizing Antibodies at High Levels. Nef as a Case Study. Transgenic Res., 18(4):499-512, Aug 2009. PubMed ID: 19169897.
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Mascola1997
J. R. Mascola, M. K. Louder, T. C. VanCott, C. V. Sapan, J. S. Lambert, L. R. Muenz, B. Bunow, D. L. Birx, and M. L. Robb. Potent and Synergistic Neutralization of Human Immunodeficiency Virus (HIV) Type 1 Primary Isolates by Hyperimmune Anti-HIV Immunoglobulin Combined with Monoclonal Antibodies 2F5 and 2G12. J. Virol., 71:7198-7206, 1997. HIVIG derived from the plasma of HIV-1-infected donors, and MAbs 2F5 and 2G12 were tested against a panel of 15 clade B HIV-1 isolates, using a single concentration that is achievable in vivo (HIVIG, 2,500 microg/ml; MAbs, 25 microg/ml). While the three antibody reagents neutralized many of the viruses tested, potency varied. The virus neutralization achieved by double or triple combinations was generally equal to or greater than that predicted by the effect of individual antibodies, and the triple combination was shown to be synergistic and to have the greatest breadth and potency. Passive immunotherapy for treatment or prophylaxis of HIV-1 should consider mixtures of these potent neutralizing antibody reagents. PubMed ID: 9311792.
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Mascola1999
J. R. Mascola, M. G. Lewis, G. Stiegler, D. Harris, T. C. VanCott, D. Hayes, M. K. Louder, C. R. Brown, C. V. Sapan, S. S. Frankel, Y. Lu, M. L. Robb, H. Katinger, and D. L. Birx. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol., 73(5):4009--18, May 1999. URL: http://jvi.asm.org/cgi/content/full/73/5/4009. PubMed ID: 10196297.
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Mascola2000a
John R. Mascola, Gabriela Stiegler, Thomas C. VanCott, Hermann Katinger, Calvin B. Carpenter, Chris E. Hanson, Holly Beary, Deborah Hayes, Sarah S. Frankel, Deborah L. Birx, and Mark G. Lewis. Protection of Macaques against Vaginal Transmission of a Pathogenic HIV-1/SIV Chimeric Virus by Passive Infusion of Neutralizing Antibodies. Nat. Med., 6(2):207-210, Feb 2000. PubMed ID: 10655111.
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Mascola2001
J. R. Mascola and G. J. Nabel. Vaccines for the prevention of HIV-1 disease. Curr. Opin. Immunol., 13(4):489--95, Aug 2001. PubMed ID: 11498307.
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Mascola2002
John R. Mascola. Passive Transfer Studies to Elucidate the Role of Antibody-Mediated Protection against HIV-1. Vaccine, 20(15):1922-1925, 6 May 2002. PubMed ID: 11983246.
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Mascola2003
John R. Mascola, Mark G. Lewis, Thomas C. VanCott, Gabriela Stiegler, Hermann Katinger, Michael Seaman, Kristin Beaudry, Dan H. Barouch, Birgit Korioth-Schmitz, Georgia Krivulka, Anna Sambor, Brent Welcher, Daniel C. Douek, David C. Montefiori, John W. Shiver, Pascal Poignard, Dennis R. Burton, and Norman L. Letvin. Cellular Immunity Elicited by Human Immunodeficiency Virus Type 1/Simian Immunodeficiency Virus DNA Vaccination Does Not Augment the Sterile Protection Afforded by Passive Infusion of Neutralizing Antibodies. J. Virol., 77(19):10348-10356, Oct 2003. PubMed ID: 12970419.
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Mascola2003a
John R. Mascola. Defining the Protective Antibody Response for HIV-1. Curr. Mol. Med., 3(3):209-216, May 2003. PubMed ID: 12699358.
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Mascola2010
John R. Mascola and David C. Montefiori. The Role of Antibodies in HIV Vaccines. Annu. Rev. Immunol., 28:413-444, Mar 2010. PubMed ID: 20192810.
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Massanella2009
Marta Massanella, Isabel Puigdomènech, Cecilia Cabrera, Maria Teresa Fernandez-Figueras, Anne Aucher, Gerald Gaibelet, Denis Hudrisier, Elisabet García, Margarita Bofill, Bonaventura Clotet, and Julià Blanco. Antigp41 Antibodies Fail to Block Early Events of Virological Synapses but Inhibit HIV Spread between T Cells. AIDS, 23(2):183-188, 14 Jan 2009. PubMed ID: 19098487.
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Matoba2008
Nobuyuki Matoba, Tagan A. Griffin, Michele Mittman, Jeffrey D. Doran, Annette Alfsen, David C. Montefiori, Carl V. Hanson, Morgane Bomsel, and Tsafrir S. Mor. Transcytosis-Blocking Abs Elicited by an Oligomeric Immunogen Based on the Membrane Proximal Region of HIV-1 gp41 Target Non-Neutralizing Epitopes. Curr. HIV Res., 6(3):218-229, May 2008. PubMed ID: 18473785.
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Matyas2009
Gary R. Matyas, Zoltan Beck, Nicos Karasavvas, and Carl R. Alving. Lipid Binding Properties of 4E10, 2F5, and WR304 Monoclonal Antibodies that Neutralize HIV-1. Biochim. Biophys. Acta, 1788(3):660-665, Mar 2009. PubMed ID: 19100711.
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Matyas2009a
Gary R. Matyas, Lindsay Wieczorek, Zoltan Beck, Christina Ochsenbauer-Jambor, John C. Kappes, Nelson L. Michael, Victoria R. Polonis, and Carl R. Alving. Neutralizing Antibodies Induced by Liposomal HIV-1 Glycoprotein 41 Peptide Simultaneously Bind to Both the 2F5 or 4E10 Epitope and Lipid Epitopes. AIDS, 23(16):2069-2077, 23 Oct 2009. PubMed ID: 19710597.
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McCaffrey2004
Ruth A McCaffrey, Cheryl Saunders, Mike Hensel, and Leonidas Stamatatos. N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies. J. Virol., 78(7):3279-3295, Apr 2004. PubMed ID: 15016849.
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McCann2005
C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016.
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McCoy2015
Laura E. McCoy, Emilia Falkowska, Katie J. Doores, Khoa Le, Devin Sok, Marit J. van Gils, Zelda Euler, Judith A. Burger, Michael S. Seaman, Rogier W. Sanders, Hanneke Schuitemaker, Pascal Poignard, Terri Wrin, and Dennis R. Burton. Incomplete Neutralization and Deviation from Sigmoidal Neutralization Curves for HIV Broadly Neutralizing Monoclonal Antibodies. PLoS Pathog., 11(8):e1005110, Aug 2015. PubMed ID: 26267277.
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McGaughey2003
G. B. McGaughey, M. Citron, R. C. Danzeisen, R. M. Freidinger, V. M. Garsky, W. M. Hurni, J. G. Joyce, X. Liang, M. Miller, J. Shiver, and M. J. Bogusky. HIV-1 Vaccine Development: Constrained Peptide Immunogens Show Improved Binding to the Anti-HIV-1 gp41 MAb. Biochemistry, 42(11):3214-3223, 25 Mar 2003. PubMed ID: 12641452.
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McGaughey2004
Georgia B. McGaughey, Gaetano Barbato, Elisabetta Bianchi, Roger M. Freidinger, Victor M. Garsky, William M. Hurni, Joseph G. Joyce, Xiaoping Liang, Michael D. Miller, Antonello Pessi, John W. Shiver, and Michael J. Bogusky. Progress Towards the Development of a HIV-1 gp41-Directed Vaccine. Curr. HIV Res., 2(2):193-204, Apr 2004. PubMed ID: 15078183.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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McKeating1996c
J. A. McKeating. Biological Consequences of Human Immunodeficiency Virus Type 1 Envelope Polymorphism: Does Variation Matter? 1995 Fleming Lecture. J. Gen. Virol., 77:2905-2919, 1996. PubMed ID: 9000081.
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McKnight2007
Aine McKnight and Marlen M. I. Aasa-Chapman. Clade Specific Neutralising Vaccines for HIV: An Appropriate Target? Curr. HIV Res., 5(6):554-560, Nov 2007. PubMed ID: 18045111.
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McLinden2013
Robert J. McLinden, Celia C. LaBranche, Agnès-Laurence Chenine, Victoria R. Polonis, Michael A. Eller, Lindsay Wieczorek, Christina Ochsenbauer, John C. Kappes, Stephen Perfetto, David C. Montefiori, Nelson L. Michael, and Jerome H. Kim. Detection of HIV-1 Neutralizing Antibodies in a Human CD4+/CXCR4+/CCR5+ T-Lymphoblastoid Cell Assay System. PLoS One, 8(11):e77756, 2013. PubMed ID: 24312168.
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Mehandru2007
Saurabh Mehandru, Brigitta Vcelar, Terri Wrin, Gabriela Stiegler, Beda Joos, Hiroshi Mohri, Daniel Boden, Justin Galovich, Klara Tenner-Racz, Paul Racz, Mary Carrington, Christos Petropoulos, Hermann Katinger, and Martin Markowitz. Adjunctive Passive Immunotherapy in Human Immunodeficiency Virus Type 1-Infected Individuals Treated with Antiviral Therapy during Acute and Early Infection. J. Virol., 81(20):11016-11031, Oct 2007. PubMed ID: 17686878.
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Melchers2012
Mark Melchers, Ilja Bontjer, Tommy Tong, Nancy P. Y. Chung, Per Johan Klasse, Dirk Eggink, David C. Montefiori, Maurizio Gentile, Andrea Cerutti, William C. Olson, Ben Berkhout, James M. Binley, John P. Moore, and Rogier W. Sanders. Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses. J. Virol., 86(5):2488-2500, Mar 2012. PubMed ID: 22205734.
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Menendez2004
Alfredo Menendez, Keith C. Chow, Oscar C. C. Pan, and Jamie K. Scott. Human Immunodeficiency Virus Type 1-Neutralizing Monoclonal Antibody 2F5 is Multispecific for Sequences Flanking the DKW Core Epitope. J. Mol. Biol., 338(2):311-327, 23 Apr 2004. PubMed ID: 15066434.
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Miglietta2014
Riccardo Miglietta, Claudia Pastori, Assunta Venuti, Christina Ochsenbauer, and Lucia Lopalco. Synergy in Monoclonal Antibody Neutralization of HIV-1 Pseudoviruses and Infectious Molecular Clones. J. Transl. Med., 12:346, 2014. PubMed ID: 25496375.
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Miller2005
Michael D. Miller, Romas Geleziunas, Elisabetta Bianchi, Simon Lennard, Renee Hrin, Hangchun Zhang, Meiqing Lu, Zhiqiang An, Paolo Ingallinella, Marco Finotto, Marco Mattu, Adam C. Finnefrock, David Bramhill, James Cook, Debra M. Eckert, Richard Hampton, Mayuri Patel, Stephen Jarantow, Joseph Joyce, Gennaro Ciliberto, Riccardo Cortese, Ping Lu, William Strohl, William Schleif, Michael McElhaugh, Steven Lane, Christopher Lloyd, David Lowe, Jane Osbourn, Tristan Vaughan, Emilio Emini, Gaetano Barbato, Peter S. Kim, Daria J. Hazuda, John W. Shiver, and Antonello Pessi. A Human Monoclonal Antibody Neutralizes Diverse HIV-1 Isolates By Binding a Critical gp41 Epitope. Proc. Natl. Acad. Sci. U.S.A., 102(41):14759-14764, 11 Oct 2005. PubMed ID: 16203977.
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Mishra2020
Nitesh Mishra, Shaifali Sharma, Ayushman Dobhal, Sanjeev Kumar, Himanshi Chawla, Ravinder Singh, Bimal Kumar Das, Sushil Kumar Kabra, Rakesh Lodha, and Kalpana Luthra. A Rare Mutation in an Infant-Derived HIV-1 Envelope Glycoprotein Alters Interprotomer Stability and Susceptibility to Broadly Neutralizing Antibodies Targeting the Trimer Apex. J. Virol., 94(19), 15 Sep 2020. PubMed ID: 32669335.
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Mishra2021
Nitesh Mishra, Sanjeev Kumar, Swarandeep Singh, Tanu Bansal, Nishkarsh Jain, Sumedha Saluja, Rajesh Kumar, Sankar Bhattacharyya, Jayanth Kumar Palanichamy, Riyaz Ahmad Mir, Subrata Sinha, and Kalpana Luthra. Cross-Neutralization of SARS-CoV-2 by HIV-1 Specific Broadly Neutralizing Antibodies and Polyclonal Plasma. PLoS Pathog., 17(9):e1009958, Sep 2021. PubMed ID: 34559854.
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Mo1997
H. Mo, L. Stamatatos, J. E. Ip, C. F. Barbas, P. W. H. I. Parren, D. R. Burton, J. P. Moore, and D. D. Ho. Human Immunodeficiency Virus Type 1 Mutants That Escape Neutralization by Human Monoclonal Antibody IgG1b12. J. Virol., 71:6869-6874, 1997. A JRCSF resistant variant was selected by culturing in the presence of IgG1b12. The resistant virus remained sensitive to 2G12 and 2F5 and to CD4-IgG, encouraging for the possibility of combination therapy. PubMed ID: 9261412.
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Mohr2010
Emma L. Mohr, Jinhua Xiang, James H. McLinden, Thomas M. Kaufman, Qing Chang, David C. Montefiori, Donna Klinzman, and Jack T. Stapleton. GB Virus Type C Envelope Protein E2 Elicits Antibodies That React with a Cellular Antigen on HIV-1 Particles and Neutralize Diverse HIV-1 Isolates. J. Immunol., 185(7):4496-4505, 1 Oct 2010. PubMed ID: 20826757.
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Molinos-Albert2023
Luis M. Molinos-Albert, Eduard Baquero, Melanie Bouvin-Pley, Valerie Lorin, Caroline Charre, Cyril Planchais, Jordan D. Dimitrov, Valerie Monceaux, Matthijn Vos, Laurent Hocqueloux, Jean-Luc Berger, Michael S. Seaman, Martine Braibant, Veronique Avettand-Fenoel, Asier Saez-Cirion, and Hugo Mouquet. Anti-V1/V3-glycan broadly HIV-1 neutralizing antibodies in a post-treatment controller. Cell Host Microbe, 31(8):1275-1287e8 doi, Aug 2023. PubMed ID: 37433296
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Mondor1998
I. Mondor, S. Ugolini, and Q. J. Sattentau. Human Immunodeficiency Virus Type 1 Attachment to HeLa CD4 Cells Is CD4 Independent and Gp120 Dependent and Requires Cell Surface Heparans. J. Virol., 72:3623-3634, 1998. PubMed ID: 9557643.
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Montefiori1999
D. Montefiori and T. Evans. Toward an HIV Type 1 Vaccine That Generates Potent Broadly Cross-Reactive Neutralizing Antibodies. AIDS Res. Hum. Retroviruses, 15:689-698, 1999. PubMed ID: 10357464.
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Montefiori2003
David C. Montefiori, Marcus Altfeld, Paul K. Lee, Miroslawa Bilska, Jintao Zhou, Mary N. Johnston, Feng Gao, Bruce D. Walker, and Eric S. Rosenberg. Viremia Control Despite Escape from a Rapid and Potent Autologous Neutralizing Antibody Response after Therapy Cessation in an HIV-1-Infected Individual. J. Immunol., 170(7):3906-3914, Apr 2003. PubMed ID: 12646660.
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Montefiori2005
David C. Montefiori. Neutralizing Antibodies Take a Swipe at HIV In Vivo. Nat. Med., 11(6):593-594, Jun 2005. PubMed ID: 15937465.
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Montefiori2009
David C. Montefiori and John R. Mascola. Neutralizing Antibodies against HIV-1: Can We Elicit Them with Vaccines and How Much Do We Need? Curr. Opin. HIV AIDS, 4(5):347-351, Sep 2009. PubMed ID: 20048696.
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Montero2012
Marinieve Montero, Naveed Gulzar, Kristina-Ana Klaric, Jason E. Donald, Christa Lepik, Sampson Wu, Sue Tsai, Jean-Philippe Julien, Ann J. Hessell, Shixia Wang, Shan Lu, Dennis R. Burton, Emil F. Pai, William F. DeGrado, and Jamie K. Scott. Neutralizing Epitopes in the Membrane-Proximal External Region of HIV-1 gp41 Are Influenced by the Transmembrane Domain and the Plasma Membrane. J. Virol., 86(6):2930-2941, Mar 2012. PubMed ID: 22238313.
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Moody2010
M. Anthony Moody, Hua-Xin Liao, S. Munir Alam, Richard M. Scearce, M. Kelly Plonk, Daniel M. Kozink, Mark S. Drinker, Ruijun Zhang, Shi-Mao Xia, Laura L. Sutherland, Georgia D. Tomaras, Ian P. Giles, John C. Kappes, Christina Ochsenbauer-Jambor, Tara G. Edmonds, Melina Soares, Gustavo Barbero, Donald N. Forthal, Gary Landucci, Connie Chang, Steven W. King, Anita Kavlie, Thomas N. Denny, Kwan-Ki Hwang, Pojen P. Chen, Philip E. Thorpe, David C. Montefiori, and Barton F. Haynes. Anti-Phospholipid Human Monoclonal Antibodies Inhibit CCR5-Tropic HIV-1 and Induce beta-Chemokines. J. Exp. Med., 207(4):763-776, 12 Apr 2010. PubMed ID: 20368576.
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Moog2014
C. Moog, N. Dereuddre-Bosquet, J.-L. Teillaud, M. E. Biedma, V. Holl, G. Van Ham, L. Heyndrickx, A. Van Dorsselaer, D. Katinger, B. Vcelar, S. Zolla-Pazner, I. Mangeot, C. Kelly, R. J. Shattock, and R. Le Grand. Protective Effect of Vaginal Application of Neutralizing and Nonneutralizing Inhibitory Antibodies Against Vaginal SHIV Challenge in Macaques. Mucosal Immunol., 7(1):46-56, Jan 2014. PubMed ID: 23591718.
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J. P. Moore and D. D. Ho. HIV-1 Neutralization: The Consequences of Adaptation to Growth on Transformed T-Cells. AIDS, 9(suppl A):S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579.
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Moore1997
J. Moore and A. Trkola. HIV Type 1 Coreceptors, Neutralization Serotypes and Vaccine Development. AIDS Res. Hum. Retroviruses, 13:733-736, 1997. PubMed ID: 9171216.
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Moore2001
J. P. Moore, P. W. Parren, and D. R. Burton. Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development. J. Virol., 75(13):5721--9, Jul 2001. URL: http://jvi.asm.org/cgi/content/full/75/13/5721. PubMed ID: 11390574.
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Moore2006
Penny L. Moore, Emma T. Crooks, Lauren Porter, Ping Zhu, Charmagne S. Cayanan, Henry Grise, Paul Corcoran, Michael B. Zwick, Michael Franti, Lynn Morris, Kenneth H. Roux, Dennis R. Burton, and James M. Binley. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1. J. Virol., 80(5):2515-2528, Mar 2006. PubMed ID: 16474158.
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Moore2009
Penny L. Moore, Elin S. Gray, and Lynn Morris. Specificity of the Autologous Neutralizing Antibody Response. Curr. Opin. HIV AIDS, 4(5):358-363, Sep 2009. PubMed ID: 20048698.
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Morgand2015
Marion Morgand, Mélanie Bouvin-Pley, Jean-Christophe Plantier, Alain Moreau, Elodie Alessandri, François Simon, Craig S. Pace, Marie Pancera, David D. Ho, Pascal Poignard, Pamela J. Bjorkman, Hugo Mouquet, Michel C. Nussenzweig, Peter D. Kwong, Daniel Baty, Patrick Chames, Martine Braibant, and Francis Barin. A V1V2 Neutralizing Epitope Is Conserved in Divergent Non-M Groups of HIV-1. J. Acquir. Immune Defic. Syndr., 21 Sep 2015. PubMed ID: 26413851.
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Morris2011
Lynn Morris, Xi Chen, Munir Alam, Georgia Tomaras, Ruijun Zhang, Dawn J. Marshall, Bing Chen, Robert Parks, Andrew Foulger, Frederick Jaeger, Michele Donathan, Mira Bilska, Elin S. Gray, Salim S. Abdool Karim, Thomas B. Kepler, John Whitesides, David Montefiori, M. Anthony Moody, Hua-Xin Liao, and Barton F. Haynes. Isolation of a Human Anti-HIV gp41 Membrane Proximal Region Neutralizing Antibody by Antigen-Specific Single B Cell Sorting. PLoS One, 6(9):e23532, 2011. PubMed ID: 21980336.
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Mouquet2012a
Hugo Mouquet, Louise Scharf, Zelda Euler, Yan Liu, Caroline Eden, Johannes F. Scheid, Ariel Halper-Stromberg, Priyanthi N. P. Gnanapragasam, Daniel I. R. Spencer, Michael S. Seaman, Hanneke Schuitemaker, Ten Feizi, Michel C. Nussenzweig, and Pamela J. Bjorkman. Complex-Type N-Glycan Recognition by Potent Broadly Neutralizing HIV Antibodies. Proc. Natl. Acad. Sci. U.S.A, 109(47):E3268-E3277, 20 Nov 2012. PubMed ID: 23115339.
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Moyo2018
Thandeka Moyo, June Ereño-Orbea, Rajesh Abraham Jacob, Clara E. Pavillet, Samuel Mundia Kariuki, Emily N. Tangie, Jean-Philippe Julien, and Jeffrey R. Dorfman. Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11. J. Virol., 92(14), 15 Jul 2018. PubMed ID: 29618644.
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M. Muhlbacher, M. Spruth, F. Siegel, R. Zangerle, and M. P. Dierich. Longitudinal Study of Antibody Reactivity against HIV-1 Envelope and a Peptide Representing a Conserved Site on Gp41 in HIV-1-Infected Patients. Immunobiology, 200:295-305, 1999. PubMed ID: 10416136.
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Muhle2013
Michael Mühle, Kerstin Hoffmann, Martin Löchelt, and Joachim Denner. Construction and Characterisation of Replicating Foamy Viral Vectors Expressing HIV-1 Epitopes Recognised by Broadly Neutralising Antibodies. Antiviral Res., 100(2):314-320, Nov 2013. PubMed ID: 24055836.
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T. Muster, F. Steindl, M. Purtscher, A. Trkola, A. Klima, G. Himmler, F. Ruker, and H. Katinger. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol., 67:6642-6647, 1993. Peptides containing the amino acid sequence LDKWAS or DKWASL showed reduced reactivity. The peptides LELDKW and KWASLW showed no significant reaction. These data suggest that the epitope of the MAb 2F5 comprises the amino acid sequence ELDKWA, with DKWA being the core sequence. PubMed ID: 7692082.
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Muster1994
T. Muster, R. Guinea, A. Trkola, M. Purtscher, A. Klima, F. Steindl, P. Palese, and H. Katinger. Cross-Neutralization Activity against Divergent Human Immunodeficiency Virus Type 1 Isolates Induced by the gp41 Sequence ELDKWAS. J. Virol., 68:4031-4034, 1994. PubMed ID: 7514684.
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Alexey A. Nabatov, Georgios Pollakis, Thomas Linnemann, Aletta Kliphius, Moustapha I. M. Chalaby, and William A. Paxton. Intrapatient Alterations in the Human Immunodeficiency Virus Type 1 gp120 V1V2 and V3 Regions Differentially Modulate Coreceptor Usage, Virus Inhibition by CC/CXC Chemokines, Soluble CD4, and the b12 and 2G12 Monoclonal Antibodies. J. Virol., 78(1):524-530, Jan 2004. PubMed ID: 14671134.
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Gary J. Nabel. Close to the Edge: Neutralizing the HIV-1 Envelope. Science, 308(5730):1878-1879, 24 Jun 2005. PubMed ID: 15976295.
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Nakowitsch2005
Sabine Nakowitsch, Heribert Quendler, Helga Fekete, Renate Kunert, Hermann Katinger, and Gabriela Stiegler. HIV-1 Mutants Escaping Neutralization by the Human Antibodies 2F5, 2G12, and 4E10: In Vitro Experiments Versus Clinical Studies. AIDS, 19(17):1957-1966, 18 Nov 2005. PubMed ID: 16260901.
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Nandi2010
Avishek Nandi, Christine L. Lavine, Pengcheng Wang, Inna Lipchina, Paul A. Goepfert, George M. Shaw, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, Philippa Easterbrook, James E. Robinson, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology. Epitopes for Broad and Potent Neutralizing Antibody Responses during Chronic Infection with Human Immunodeficiency Virus Type 1. Virology, 396(2):339-348, 20 Jan 2010. PubMed ID: 19922969.
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Narayan2013
Kristin M. Narayan, Nitish Agrawal, Sean X. Du, Janelle E. Muranaka, Katherine Bauer, Daniel P. Leaman, Pham Phung, Kay Limoli, Helen Chen, Rebecca I. Boenig, Terri Wrin, Michael B. Zwick, and Robert G. Whalen. Prime-Boost Immunization of Rabbits with HIV-1 gp120 Elicits Potent Neutralization Activity against a Primary Viral Isolate. PLoS One, 8(1):e52732, 9 Jan 2013. PubMed ID: 23326351.
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Nelson2007
Josh D. Nelson, Florence M. Brunel, Richard Jensen, Emma T. Crooks, Rosa M. F. Cardoso, Meng Wang, Ann Hessell, Ian A. Wilson, James M. Binley, Philip E. Dawson, Dennis R. Burton, and Michael B. Zwick. An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10. J. Virol., 81(8):4033-4043, Apr 2007. PubMed ID: 17287272.
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Nelson2008
Josh D. Nelson, Heather Kinkead, Florence M. Brunel, Dan Leaman, Richard Jensen, John M. Louis, Toshiaki Maruyama, Carole A. Bewley, Katherine Bowdish, G. Marius Clore, Philip E. Dawson, Shana Frederickson, Rose G. Mage, Douglas D. Richman, Dennis R. Burton, and Michael B. Zwick. Antibody Elicited against the gp41 N-Heptad Repeat (NHR) Coiled-Coil Can Neutralize HIV-1 with Modest Potency but Non-Neutralizing Antibodies Also Bind to NHR Mimetics. Virology, 377(1):170-183, 20 Jul 2008. PubMed ID: 18499210.
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A. R. Neurath, N. Strick, K. Lin, and S. Jiang. Multifaceted Consequences of Anti-gp41 Monoclonal Antibody 2F5 Binding to HIV Type 1 Virions. AIDS Res. Hum. Retroviruses, 11:687-696, 1995. PubMed ID: 7576928.
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Nathan I. Nicely, S. Moses Dennison, Leonard Spicer, Richard M. Scearce, Garnett Kelsoe, Yoshihiro Ueda, Haiyan Chen, Hua-Xin Liao, S. Munir Alam, and Barton F. Haynes. Crystal Structure of a Non-Neutralizing Antibody to the HIV-1 gp41 Membrane-Proximal External Region. Nat. Struct. Mol. Biol., 17(12):1492-1494, Dec 2010. PubMed ID: 21076400.
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Nie2010
Jianhui Nie, Chuntao Zhang, Wei Liu, Xueling Wu, Feng Li, Suting Wang, Fuxiong Liang, Aijing Song, and Youchun Wang. Genotypic and Phenotypic Characterization of HIV-1 CRF01\_AE env Molecular Clones from Infections in China. J. Acquir. Immune Defic. Syndr., 53(4):440-450, 1 Apr 2010. PubMed ID: 20090544.
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Nie2020
Jianhui Nie, Weijin Huang, Qiang Liu, and Youchun Wang. HIV-1 Pseudoviruses Constructed in China Regulatory Laboratory. Emerg. Microbes Infect., 9(1):32-41, 2020. PubMed ID: 31859609.
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Nora2008
Tamara Nora, Francine Bouchonnet, Béatrice Labrosse, Charlotte Charpentier, Fabrizio Mammano, François Clavel, and Allan J. Hance. Functional Diversity of HIV-1 Envelope Proteins Expressed by Contemporaneous Plasma Viruses. Retrovirology, 5:23, 2008. PubMed ID: 18312646.
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Nyambi2000
P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650.
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Ofek2004
Gilad Ofek, Min Tang, Anna Sambor, Hermann Katinger, John R. Mascola, Richard Wyatt, and Peter D. Kwong. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope. J. Virol., 78(19):10724-10737, Oct 2004. PubMed ID: 15367639.
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Ofek2010
Gilad Ofek, Krisha McKee, Yongping Yang, Zhi-Yong Yang, Jeff Skinner, F. Javier Guenaga, Richard Wyatt, Michael B. Zwick, Gary J. Nabel, John R. Mascola, and Peter D. Kwong. Relationship between Antibody 2F5 Neutralization of HIV-1 and Hydrophobicity of Its Heavy Chain Third Complementarity-Determining Region. J Virol, 84(6):2955-2962, Mar 2010. PubMed ID: 20042512.
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Ofek2010a
Gilad Ofek, F. Javier Guenaga, William R. Schief, Jeff Skinner, David Baker, Richard Wyatt, and Peter D. Kwong. Elicitation of Structure-Specific Antibodies by Epitope Scaffolds. Proc. Natl. Acad. Sci. U.S.A., 107(42):17880-17887, 19 Oct 2010. PubMed ID: 20876137.
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Ofek2014
Gilad Ofek, Brett Zirkle, Yongping Yang, Zhongyu Zhu, Krisha McKee, Baoshan Zhang, Gwo-Yu Chuang, Ivelin S. Georgiev, Sijy O'Dell, Nicole Doria-Rose, John R. Mascola, Dimiter S. Dimitrov, and Peter D. Kwong. Structural Basis for HIV-1 neutralization By 2F5-Like Antibodies m66 and m66.6. J. Virol., 88(5):2426-2441, Mar 2014. PubMed ID: 24335316.
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Ohagen2003
Asa Ohagen, Amy Devitt, Kevin J. Kunstman, Paul R. Gorry, Patrick P. Rose, Bette Korber, Joann Taylor, Robert Levy, Robert L. Murphy, Steven M. Wolinsky, and Dana Gabuzda. Genetic and Functional Analysis of Full-Length Human Immunodeficiency Virus Type 1 env Genes Derived from Brain and Blood of Patients with AIDS. J. Virol., 77(22):12336-12345, Nov 2003. PubMed ID: 14581570.
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Opalka2004
David Opalka, Antonello Pessi, Elisabetta Bianchi, Gennaro Ciliberto, William Schleif, Michael McElhaugh, Renee Danzeisen, Romas Geleziunas, Michael Miller, Debra M. Eckert, David Bramhill, Joseph Joyce, James Cook, William Magilton, John Shiver, Emilio Emini, and Mark T. Esser. Analysis of the HIV-1 gp41 Specific Immune Response Using a Multiplexed Antibody Detection Assay. J. Immunol. Methods, 287(1-2):49-65, Apr 2004. PubMed ID: 15099755.
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ORourke2009
Sara M. O'Rourke, Becky Schweighardt, William G. Scott, Terri Wrin, Dora P. A. J. Fonseca, Faruk Sinangil, and Phillip W. Berman. Novel Ring Structure in the gp41 Trimer of Human Immunodeficiency Virus Type 1 That Modulates Sensitivity and Resistance to Broadly Neutralizing Antibodies. J. Virol., 83(15):7728-7738, Aug 2009. PubMed ID: 19474108.
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ORourke2010
Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Dora P. A. J. Fonseca, Karianne Terry, Terri Wrin, Faruk Sinangil, and Phillip W. Berman. Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus. J. Virol., 84(21):11200-11209, Nov 2010. PubMed ID: 20702624.
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Wu Ou, Ning Lu, Sloane S. Yu, and Jonathan Silver. Effect of Epitope Position on Neutralization by Anti-Human Immunodeficiency Virus Monoclonal Antibody 2F5. J. Virol., 80(5):2539-2547, Mar 2006. PubMed ID: 16474160.
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Overbaugh2012
Julie Overbaugh and Lynn Morris. The Antibody Response against HIV-1. Cold Spring Harb. Perspect. Med., 2(1):a007039, Jan 2012. PubMed ID: 22315717.
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Pacheco2008
Beatriz Pacheco, Stephane Basmaciogullari, Jason A. Labonte, Shi-Hua Xiang, and Joseph Sodroski. Adaptation of the Human Immunodeficiency Virus Type 1 Envelope Glycoproteins to New World Monkey Receptors. J. Virol., 82(1):346-357, Jan 2008. PubMed ID: 17959679.
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Bapi Pahar, Mayra A. Cantu, Wei Zhao, Marcelo J. Kuroda, Ronald S. Veazey, David C. Montefiori, John D. Clements, Pyone P. Aye, Andrew A. Lackner, Karin Lovgren-Bengtsson, and Karol Sestak. Single Epitope Mucosal Vaccine Delivered via Immuno-Stimulating Complexes Induces Low Level of Immunity Against Simian-HIV. Vaccine, 24(47-48):6839-6849, 17 Nov 2006. PubMed ID: 17050045.
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Emil F. Pai, Michel H. Klein, Pele Chong, and Arthur Pedyczak. Fab'-Epitope Complex from the HIV-1 Cross-Neutralizing Monoclonal Antibody 2F5. U.S. Patent 6,482,928, WIPO Patent WO 00/61618, 19 Nov 2002. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=US39699302. Filed USPTO Apr. 13, 1999.
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Palacios-Rodriguez2011
Yadira Palacios-Rodríguez, Tatiana Gazarian, Leonor Huerta, and Karlen Gazarian. Constrained Peptide Models from Phage Display Libraries Highlighting the Cognate Epitope-Specific Potential of the Anti-HIV-1 mAb 2F5. Immunol. Lett., 136(1):80-89, 30 Apr 2011. PubMed ID: 21237206.
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Pancera2013
Marie Pancera, Syed Shahzad-ul-Hussan, Nicole A. Doria-Rose, Jason S. McLellan, Robert T. Bailer, Kaifan Dai, Sandra Loesgen, Mark K. Louder, Ryan P. Staupe, Yongping Yang, Baoshan Zhang, Robert Parks, Joshua Eudailey, Krissey E. Lloyd, Julie Blinn, S. Munir Alam, Barton F. Haynes, Mohammed N. Amin, Lai-Xi Wang, Dennis R. Burton, Wayne C. Koff, Gary J. Nabel, John R. Mascola, Carole A. Bewley, and Peter D. Kwong. Structural Basis for Diverse N-Glycan Recognition by HIV-1-Neutralizing V1-V2-Directed Antibody PG16. Nat. Struct. Mol. Biol., 20(7):804-813, Jul 2013. PubMed ID: 23708607.
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Ralph Pantophlet. Antibody Epitope Exposure and Neutralization of HIV-1. Curr. Pharm. Des., 16(33):3729-3743, 2010. PubMed ID: 21128886.
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E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031.
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C. E. Parker, L. J. Deterding, C. Hager-Braun, J. M. Binley, N. Schulke, H. Katinger, J. P. Moore, and K. B. Tomer. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol., 75(22):10906--11, Nov 2001. URL: http://jvi.asm.org/cgi/content/full/75/22/10906. PubMed ID: 11602730.
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Parren1998
P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629.
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Parren1998a
P. W. Parren, M. Wang, A. Trkola, J. M. Binley, M. Purtscher, H. Katinger, J. P. Moore, and D. R. Burton. Antibody neutralization-resistant primary isolates of human immunodeficiency virus type 1. J. Virol., 72:10270-4, 1998. PubMed ID: 9811774.
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P. W. Parren, J. P. Moore, D. R. Burton, and Q. J. Sattentau. The Neutralizing Antibody Response to HIV-1: Viral Evasion and Escape from Humoral Immunity. AIDS, 13(Suppl A):S137-162, 1999. PubMed ID: 10885772.
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Kristina K. Peachman, Lindsay Wieczorek, Victoria R. Polonis, Carl R. Alving, and Mangala Rao. The Effect of sCD4 on the Binding and Accessibility of HIV-1 gp41 MPER Epitopes to Human Monoclonal Antibodies. Virology, 408(2):213-223, 20 Dec 2010. PubMed ID: 20961591.
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Lautaro G. Perez, Susan Zolla-Pazner, and David C. Montefiori. Antibody-Dependent, Fc-gamma-RI-Mediated Neutralization of HIV-1 in TZM-bl Cells Occurs Independently of Phagocytosis. J. Virol., 87(9):5287-5290, May 2013. PubMed ID: 23408628.
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Paul J. Peters, Maria J. Duenas-Decamp, W. Matthew Sullivan, Richard Brown, Chiambah Ankghuambom, Katherine Luzuriaga, James Robinson, Dennis R. Burton, Jeanne Bell, Peter Simmonds, Jonathan Ball, and Paul R. Clapham. Variation in HIV-1 R5 Macrophage-Tropism Correlates with Sensitivity to Reagents that Block Envelope: CD4 Interactions But Not with Sensitivity to Other Entry Inhibitors. Retrovirology, 5:5, 2008. PubMed ID: 18205925.
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Yanqin Ren, Maria Korom, Ronald Truong, Dora Chan, Szu-Han Huang, Colin C. Kovacs, Erika Benko, Jeffrey T. Safrit, John Lee, Hermes Garbán, Richard Apps, Harris Goldstein, Rebecca M. Lynch, and R. Brad Jones. Susceptibility to Neutralization by Broadly Neutralizing Antibodies Generally Correlates with Infected Cell Binding for a Panel of Clade B HIV Reactivated from Latent Reservoirs. J. Virol., 92(23), 1 Dec 2018. PubMed ID: 30209173.
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Jeffrey T. Safrit, Ruth Ruprecht, Flavia Ferrantelli, Weidong Xu, Moiz Kitabwalla, Koen Van Rompay, Marta Marthas, Nancy Haigwood, John R. Mascola, Katherine Luzuriaga, Samuel Adeniyi Jones, Bonnie J. Mathieson, Marie-Louise Newell, and Ghent IAS Working Group on HIV in Women Children. Immunoprophylaxis to Prevent Mother-to-Child Transmission of HIV-1. J. Acquir. Immune Defic. Syndr., 35(2):169-177, 1 Feb 2004. PubMed ID: 14722451.
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Schorcht2020
Anna Schorcht, Tom L. G. M. van den Kerkhof, Christopher A. Cottrell, Joel D. Allen, Jonathan L. Torres, Anna-Janina Behrens, Edith E. Schermer, Judith A. Burger, Steven W. de Taeye, Alba Torrents de la Peña, Ilja Bontjer, Stephanie Gumbs, Gabriel Ozorowski, Celia C. LaBranche, Natalia de Val, Anila Yasmeen, Per Johan Klasse, David C. Montefiori, John P. Moore, Hanneke Schuitemaker, Max Crispin, Marit J. van Gils, Andrew B. Ward, and Rogier W. Sanders. Neutralizing Antibody Responses Induced by HIV-1 Envelope Glycoprotein SOSIP Trimers Derived from Elite Neutralizers. J. Virol., 94(24), 23 Nov 2020. PubMed ID: 32999024.
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Schulke2002
Norbert Schulke, Mika S. Vesanen, Rogier W. Sanders, Ping Zhu, Min Lu, Deborah J. Anselma, Anthony R. Villa, Paul W. H. I. Parren, James M. Binley, Kenneth H. Roux, Paul J. Maddon, John P. Moore, and William C. Olson. Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein. J. Virol., 76(15):7760-76, Aug 2002. PubMed ID: 12097589.
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Schultz2018
Anke Schultz, Anja Germann, Martina Fuss, Marcella Sarzotti-Kelsoe, Daniel A. Ozaki, David C. Montefiori, Heiko Zimmermann, and Hagen von Briesen. Validation of an Automated System for Aliquoting of HIV-1 Env-Pseudotyped Virus Stocks. PLoS One, 13(1):1-20, Jan 2018. PubMed ID: 29300769.
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Schutten1997
M. Schutten, A. C. Andeweg, G. F. Rimmelzwaan, and A. D. Osterhaus. Modulation of primary human immunodeficiency virus type 1 envelope glycoprotein-mediated entry by human antibodies. J. Gen. Virol., 78:999-1006, 1997. A series of HIV-1 envelope glycoproteins from related primary virus isolates of different SI phenotypes, together with chimeras of these proteins, were tested in an envelope trans-complementation assay for their sensitivity to either antibody mediated inhibition or enhancement of HIV-1 entry. In contrast to the inhibition of HIV-1 entry, antibody mediated enhancement was not temperature dependent and could not be mediated by F(ab) fragments, implicating cross-linking as an important step. Enhancement or inhibition seemed to be determined by virus isolate rather than by the specificity of the antiserum used. 2F5 was the only MAb that inhibited the entry of all viruses. PubMed ID: 9152416.
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Schweighardt2007
Becky Schweighardt, Yang Liu, Wei Huang, Colombe Chappey, Yolanda S. Lie, Christos J. Petropoulos, and Terri Wrin. Development of an HIV-1 Reference Panel of Subtype B Envelope Clones Isolated from the Plasma of Recently Infected Individuals. J. Acquir. Immune Defic. Syndr., 46(1):1-11, 1 Sep 2007. PubMed ID: 17514017.
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Sellhorn2012
George Sellhorn, Zane Kraft, Zachary Caldwell, Katharine Ellingson, Christine Mineart, Michael S. Seaman, David C. Montefiori, Eliza Lagerquist, and Leonidas Stamatatos. Engineering, Expression, Purification, and Characterization of Stable Clade A/B Recombinant Soluble Heterotrimeric gp140 Proteins. J. Virol., 86(1):128-142, Jan 2012. PubMed ID: 22031951.
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Serrano2014
Soraya Serrano, Aitziber Araujo, Beatriz Apellániz, Steve Bryson, Pablo Carravilla, Igor de la Arada, Nerea Huarte, Edurne Rujas, Emil F. Pai, José L. R. Arrondo, Carmen Domene, María Angeles Jiménez, and José L. Nieva. Structure and Immunogenicity of a Peptide Vaccine, Including the Complete HIV-1 gp41 2F5 Epitope: Implications for Antibody Recognition Mechanism and Immunogen Design. J. Biol. Chem., 289(10):6565-6580, 7 Mar 2014. PubMed ID: 24429284.
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Shang2011
Hong Shang, Xiaoxu Han, Xuanling Shi, Teng Zuo, Mark Goldin, Dan Chen, Bing Han, Wei Sun, Hao Wu, Xinquan Wang, and Linqi Zhang. Genetic and Neutralization Sensitivity of Diverse HIV-1 env Clones from Chronically Infected Patients in China. J. Biol. Chem., 286(16):14531-14541, 22 Apr 2011. PubMed ID: 21325278.
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Shen2009
Xiaoying Shen, Robert J. Parks, David C. Montefiori, Jennifer L. Kirchherr, Brandon F. Keele, Julie M. Decker, William A. Blattner, Feng Gao, Kent J. Weinhold, Charles B. Hicks, Michael L. Greenberg, Beatrice H. Hahn, George M. Shaw, Barton F. Haynes, and Georgia D. Tomaras. In Vivo gp41 Antibodies Targeting the 2F5 Monoclonal Antibody Epitope Mediate Human Immunodeficiency Virus Type 1 Neutralization Breadth. J. Virol., 83(8):3617-3625, Apr 2009. PubMed ID: 19193787.
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Shen2010
Xiaoying Shen, S. Moses Dennison, Pinghuang Liu, Feng Gao, Frederick Jaeger, David C. Montefiori, Laurent Verkoczy, Barton F. Haynes, S. Munir Alam, and Georgia D. Tomaras. Prolonged Exposure of the HIV-1 gp41 Membrane Proximal Region with L669S Substitution. Proc. Natl. Acad. Sci. U.S.A., 107(13):5972-5977, 30 Mar 2010. PubMed ID: 20231447.
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Shen2010a
Ruizhong Shen, Ernesto R. Drelichman, Diane Bimczok, Christina Ochsenbauer, John C. Kappes, Jamie A. Cannon, Daniela Tudor, Morgane Bomsel, Lesley E. Smythies, and Phillip D. Smith. GP41-Specific Antibody Blocks Cell-Free HIV Type 1 Transcytosis through Human Rectal Mucosa and Model Colonic Epithelium. J. Immunol., 184(7):3648-3655, 1 Apr 2010. PubMed ID: 20208001.
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Shi2010
Wuxian Shi, Jen Bohon, Dong P. Han, Habtom Habte, Yali Qin, Michael W. Cho, and Mark R. Chance. Structural Characterization of HIV gp41 with the Membrane-Proximal External Region. J. Biol. Chem., 285(31):24290-24298, 30 Jul 2010. PubMed ID: 20525690.
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Si2001
Zhihai Si, Mark Cayabyab, and Joseph Sodroski. Envelope Glycoprotein Determinants of nEutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys. J. Virol., 75(9):4208-4218, May 2001. PubMed ID: 11287570.
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Siddappa2010
Nagadenahalli B. Siddappa, Jennifer D. Watkins, Klemens J. Wassermann, Ruijiang Song, Wendy Wang, Victor G. Kramer, Samir Lakhashe, Michael Santosuosso, Mark C. Poznansky, Francis J. Novembre, François Villinger, James G. Else, David C. Montefiori, Robert A. Rasmussen, and Ruth M. Ruprecht. R5 Clade C SHIV Strains with Tier 1 or 2 Neutralization Sensitivity: Tools to Dissect Env Evolution and to Develop AIDS Vaccines in Primate Models. PLoS One, 5(7):e11689, 2010. PubMed ID: 20657739.
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Simek2009
Melissa D. Simek, Wasima Rida, Frances H. Priddy, Pham Pung, Emily Carrow, Dagna S. Laufer, Jennifer K. Lehrman, Mark Boaz, Tony Tarragona-Fiol, George Miiro, Josephine Birungi, Anton Pozniak, Dale A. McPhee, Olivier Manigart, Etienne Karita, André Inwoley, Walter Jaoko, Jack DeHovitz, Linda-Gail Bekker, Punnee Pitisuttithum, Robert Paris, Laura M. Walker, Pascal Poignard, Terri Wrin, Patricia E. Fast, Dennis R. Burton, and Wayne C. Koff. Human Immunodeficiency Virus Type 1 Elite Neutralizers: Individuals with Broad and Potent Neutralizing Activity Identified by Using a High-Throughput Neutralization Assay together with an Analytical Selection Algorithm. J. Virol., 83(14):7337-7348, Jul 2009. PubMed ID: 19439467.
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Simonich2016
Cassandra A. Simonich, Katherine L. Williams, Hans P. Verkerke, James A. Williams, Ruth Nduati, Kelly K. Lee, and Julie Overbaugh. HIV-1 Neutralizing Antibodies with Limited Hypermutation from an Infant. Cell, 166(1):77-87, 30 Jun 2016. PubMed ID: 27345369.
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Singh2011
Harvir Singh, Kevin A. Henry, Sampson S. T. Wu, Andrzej Chruscinski, Paul J. Utz, and Jamie K. Scott. Reactivity Profiles of Broadly Neutralizing Anti-HIV-1 Antibodies Are Distinct from Those of Pathogenic Autoantibodies. AIDS, 25(10):1247-1257, 19 Jun 2011. PubMed ID: 21508803.
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Smalls-Mantey2012
Adjoa Smalls-Mantey, Nicole Doria-Rose, Rachel Klein, Andy Patamawenu, Stephen A. Migueles, Sung-Youl Ko, Claire W. Hallahan, Hing Wong, Bai Liu, Lijing You, Johannes Scheid, John C. Kappes, Christina Ochsenbauer, Gary J. Nabel, John R. Mascola, and Mark Connors. Antibody-Dependent Cellular Cytotoxicity against Primary HIV-Infected CD4+ T Cells Is Directly Associated with the Magnitude of Surface IgG Binding. J. Virol., 86(16):8672-8680, Aug 2012. PubMed ID: 22674985.
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Song2009
Likai Song, Zhen-Yu J. Sun, Kate E. Coleman, Michael B. Zwick, Johannes S. Gach, Jia-huai Wang, Ellis L. Reinherz, Gerhard Wagner, and Mikyung Kim. Broadly Neutralizing Anti-HIV-1 Antibodies Disrupt a Hinge-Related Function of gp41 at the Membrane Interface. Proc. Natl. Acad. Sci. U.S.A., 106(22):9057-9062, 2 Jun 2009. PubMed ID: 19458040.
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Spencer2021
David A. Spencer, Delphine C. Malherbe, Nestor Vazquez Bernat, Monika Adori, Benjamin Goldberg, Nicholas Dambrauskas, Heidi Henderson, Shilpi Pandey, Tracy Cheever, Philip Barnette, William F. Sutton, Margaret E. Ackerman, James J. Kobie, D. Noah Sather, Gunilla B. Karlsson Hedestam, Nancy L. Haigwood, and Ann J. Hessell. Polyfunctional Tier 2-Neutralizing Antibodies Cloned following HIV-1 Env Macaque Immunization Mirror Native Antibodies in a Human Donor. J Immunol, 206(5):999-1012 doi, Mar 2021. PubMed ID: 33472907
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Spenlehauer2001
C. Spenlehauer, C. A. Gordon, A. Trkola, and J. P. Moore. A luciferase-reporter gene-expressing T-cell line facilitates neutralization and drug-sensitivity assays that use either R5 or X4 strains of human immunodeficiency virus type 1. Virology, 280(2):292--300, 15 Feb 2001. PubMed ID: 11162843.
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Srisurapanon2005
Surangrat Srisurapanon, Suda Louisirirotchanakul, Kwonchit Sumransurp, Monthaswad Ratanasrithong, Thippawan Chuenchitra, Siriporn Jintakatkorn, and Chantapong Wasi. Binding Antibody to Neutralizing Epitope gp41 in HIV-1 Subtype CRF 01\_AE Infection Related to Stage of Disease. Southeast Asian J. Trop. Med. Public Health, 36(1):221-227, Jan 2005. PubMed ID: 15906673.
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Srivastava2002
Indresh K. Srivastava, Leonidas Stamatatos, Harold Legg, Elaine Kan, Anne Fong, Stephen R. Coates, Louisa Leung, Mark Wininger, John J. Donnelly, Jeffrey B. Ulmer, and Susan W. Barnett. Purification and Characterization of Oligomeric Envelope Glycoprotein from a Primary R5 Subtype B Human Immunodeficiency Virus. J. Virol., 76(6):2835-2847, Mar 2002. URL: http://jvi.asm.org/cgi/content/full/76/6/2835. PubMed ID: 11861851.
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Srivastava2005
Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830.
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Srivastava2008
Indresh K. Srivastava, Elaine Kan, Yide Sun, Victoria A. Sharma, Jimna Cisto, Brian Burke, Ying Lian, Susan Hilt, Zohar Biron, Karin Hartog, Leonidas Stamatatos, Ruben Diaz-Avalos, R Holland Cheng, Jeffrey B. Ulmer, and Susan W. Barnett. Comparative Evaluation of Trimeric Envelope Glycoproteins Derived from Subtype C and B HIV-1 R5 Isolates. Virology, 372(2):273-290, 15 Mar 2008. PubMed ID: 18061231.
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L. Stamatatos, S. Zolla-Pazner, M. K. Gorny, and C. Cheng-Mayer. Binding of Antibodies to Virion-Associated gp120 Molecules of Primary-Like Human Immunodeficiency Virus Type 1 (HIV-1) Isolates: Effect on HIV-1 Infection of Macrophages and Peripheral Blood Mononuclear Cells. Virology, 229:360-369, 1997. PubMed ID: 9126249.
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Stamatatos2009
Leonidas Stamatatos, Lynn Morris, Dennis R. Burton, and John R. Mascola. Neutralizing Antibodies Generated during Natural HIV-1 Infection: Good News for an HIV-1 Vaccine? Nat. Med., 15(8):866-870, Aug 2009. PubMed ID: 19525964.
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Stanfield2005
Robyn L. Stanfield and Ian A. Wilson. Structural Studies of Human HIV-1 V3 Antibodies. Hum Antibodies, 14(3-4):73-80, 2005. PubMed ID: 16720977.
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Steckbeck2010
Jonathan D. Steckbeck, Chengqun Sun, Timothy J. Sturgeon, and Ronald C. Montelaro. Topology of the C-Terminal Tail of HIV-1 gp41: Differential Exposure of the Kennedy Epitope on Cell and Viral Membranes. PLoS One, 5(12):e15261, 2010. PubMed ID: 21151874.
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Stephenson2016
Kathryn E. Stephenson and Dan H. Barouch. Broadly Neutralizing Antibodies for HIV Eradication. Curr. HIV/AIDS Rep., 13(1):31-37, Feb 2016. PubMed ID: 26841901.
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Stiegler2001
G. Stiegler, R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 17(18):1757--65, 10 Dec 2001. PubMed ID: 11788027.
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Stiegler2002
Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Heribert Stoiber, Renate Kunert, Nelson L. Michael, Linda L. Jagodzinski, Christoph Ammann, Walter Jäger, Jeffrey Jacobson, Norbert Vetter, and Hermann Katinger. Antiviral Activity of the Neutralizing Antibodies 2F5 and 2G12 in Asymptomatic HIV-1-Infected Humans: A Phase I Evaluation. AIDS, 16(15):2019-2025, 18 Oct 2002. PubMed ID: 12370500.
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Stoiber1996
H. Stoiber, C. Pinter, A. G. Siccardi, A. Clivio, and M. P. Dierich. Efficient Destruction of Human Immunodeficiency Virus in Human Serum by Inhibiting the Protective Action of Complement Factor H and Decay Accelerating Factor (DAF, CD55). J. Exp. Med., 183:307-310, 1996. HIV and HIV-infected cells are not subject to efficient complement-mediated lysis, even in the presence of HIV-specific antibodies. HIV is intrinsically resistant to human complement. Decay accelerating factor (DAF) and human complement factor H (CFH), a humoral negative regulator of complement which binds to gp41 are critical for this resistance. MAb 2F5 can inhibit CHF binding and facilitate complement mediated lysis. PubMed ID: 8551237.
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Sun2008
Zhen-Yu J. Sun, Kyoung Joon Oh, Mikyung Kim, Jessica Yu, Vladimir Brusic, Likai Song, Zhisong Qiao, Jia-huai Wang, Gerhard Wagner, and Ellis L. Reinherz. HIV-1 Broadly Neutralizing Antibody Extracts Its Epitope from a Kinked gp41 Ectodomain Region on the Viral Membrane. Immunity, 28(1):52-63, Jan 2008. PubMed ID: 18191596.
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D. M. Takefman, B. L. Sullivan, B. E. Sha, and G. T. Spear. Mechanisms of Resistance of HIV-1 Primary Isolates to Complement-Mediated Lysis. Virology, 246:370-378, 1998. PubMed ID: 9657955.
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Tang2023
Wenqi Tang, Zhenzhen Yuan, Zheng Wang, Li Ren, Dan Li, Shuhui Wang, Yanling Hao, Jing Li, Xiuli Shen, Yuhua Ruan, Yiming Shao, and Ying Liu. Neutralization Sensitivity and Evolution of Virus in a Chronic HIV-1 Clade B Infected Patient with Neutralizing Activity against Membrane-Proximal External Region. Pathogens, 12(3), 22 Mar 2023. PubMed ID: 36986419.
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Tasca2008
Silvana Tasca, Siu-Hong Ho, and Cecilia Cheng-Mayer. R5X4 Viruses Are Evolutionary, Functional, and Antigenic Intermediates in the Pathway of a Simian-Human Immunodeficiency Virus Coreceptor Switch. J. Virol., 82(14):7089-7099, Jul 2008. PubMed ID: 18480460.
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Thali1994
M. Thali, M. Charles, C. Furman, L. Cavacini, M. Posner, J. Robinson, and J. Sodroski. Resistance to Neutralization by Broadly Reactive Antibodies to the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein Conferred by a gp41 Amino Acid Change. J. Virol., 68:674-680, 1994. A T->A amino acid substitution at position 582 of gp41 conferred resistance to neutralization to 30\% of HIV positive sera (Wilson et al. J Virol 64:3240-48 (1990)). Monoclonal antibodies that bound to the CD4 binding site were unable to neutralize this virus, but the mutation did not reduce the neutralizing capacity of a V2 region MAb G3-4, V3 region MAbs, or gp41 neutralizing MAb 2F5. PubMed ID: 7507184.
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Thenin2012a
Suzie Thenin, Emmanuelle Roch, Tanawan Samleerat, Thierry Moreau, Antoine Chaillon, Alain Moreau, Francis Barin, and Martine Braibant. Naturally Occurring Substitutions of Conserved Residues in Human Immunodeficiency Virus Type 1 Variants of Different Clades Are Involved in PG9 and PG16 Resistance to Neutralization. J. Gen. Virol., 93(7):1495-1505, Jul 2012. PubMed ID: 22492917.
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Tian2002
Y. Tian, C. V. Ramesh, X. Ma, S. Naqvi, T. Patel, T. Cenizal, M. Tiscione, K. Diaz, T. Crea, E. Arnold, G. F. Arnold, and J. W. Taylor. Structure-Affinity Relationships in the gp41 ELDKWA Epitope for the HIV-1 Neutralizing Monoclonal Antibody 2F5: Effects of Side-Chain and Backbone Modifications and Conformational Constraints. J Pept Res, 59(6):264-276, Jun 2002. PubMed ID: 12010517.
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Todd2012
Christopher A. Todd, Kelli M. Greene, Xuesong Yu, Daniel A. Ozaki, Hongmei Gao, Yunda Huang, Maggie Wang, Gary Li, Ronald Brown, Blake Wood, M. Patricia D'Souza, Peter Gilbert, David C. Montefiori, and Marcella Sarzotti-Kelsoe. Development and Implementation of an International Proficiency Testing Program for a Neutralizing Antibody Assay for HIV-1 in TZM-bl Cells. J. Immunol. Methods, 375(1-2):57-67, 31 Jan 2012. PubMed ID: 21968254.
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Tomaras2008
Georgia D. Tomaras, Nicole L. Yates, Pinghuang Liu, Li Qin, Genevieve G. Fouda, Leslie L. Chavez, Allan C. Decamp, Robert J. Parks, Vicki C. Ashley, Judith T. Lucas, Myron Cohen, Joseph Eron, Charles B. Hicks, Hua-Xin Liao, Steven G. Self, Gary Landucci, Donald N. Forthal, Kent J. Weinhold, Brandon F. Keele, Beatrice H. Hahn, Michael L. Greenberg, Lynn Morris, Salim S. Abdool Karim, William A. Blattner, David C. Montefiori, George M. Shaw, Alan S. Perelson, and Barton F. Haynes. Initial B-Cell Responses to Transmitted Human Immunodeficiency Virus Type 1: Virion-Binding Immunoglobulin M (IgM) and IgG Antibodies Followed by Plasma Anti-gp41 Antibodies with Ineffective Control of Initial Viremia. J. Virol., 82(24):12449-12463, Dec 2008. PubMed ID: 18842730.
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Tomaras2010
Georgia D. Tomaras and Barton F. Haynes. Strategies for Eliciting HIV-1 Inhibitory Antibodies. Curr. Opin. HIV AIDS, 5(5):421-427, Sep 2010. PubMed ID: 20978384.
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Tomaras2011
Georgia D. Tomaras, James M. Binley, Elin S. Gray, Emma T. Crooks, Keiko Osawa, Penny L. Moore, Nancy Tumba, Tommy Tong, Xiaoying Shen, Nicole L. Yates, Julie Decker, Constantinos Kurt Wibmer, Feng Gao, S. Munir Alam, Philippa Easterbrook, Salim Abdool Karim, Gift Kamanga, John A. Crump, Myron Cohen, George M. Shaw, John R. Mascola, Barton F. Haynes, David C. Montefiori, and Lynn Morris. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals. J. Virol., 85(21):11502-11519, Nov 2011. PubMed ID: 21849452.
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Tong2012
Tommy Tong, Ema T. Crooks, Keiko Osawa, and James M. Binley. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes. J. Virol., 86(7):3574-3587, Apr 2012. PubMed ID: 22301141.
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A. Trkola, A. B. Pomales, H. Yuan, B. Korber, P. J. Maddon, G. P. Allaway, H. Katinger, C. F. Barbas III, D. R. Burton, D. D. Ho, and J. P. Moore. Cross-Clade Neutralization of Primary Isolates of Human Immunodeficiency Virus Type 1 by Human Monoclonal Antibodies and Tetrameric CD4-IgG. J. Virol., 69:6609-6617, 1995. Three MAbs, IgG1b12, 2G12, and 2F5 tetrameric CD4-IgG2 were tested for their ability to neutralize primary isolates from clades A-F. 2F5 and CD4-IgG2 were able to neutralize within and outside clade B with a high potency. IgG1b12 and 2G12 could potently neutralize isolates from within clade B, but showed a reduction in efficacy outside of clade B. 2F5 neutralization was dependent on the presence of the sequence: LDKW. PubMed ID: 7474069.
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Trkola1998
A. Trkola, T. Ketas, V. N. Kewalramani, F. Endorf, J. M. Binley, H. Katinger, J. Robinson, D. R. Littman, and J. P. Moore. Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Primary Isolates to Antibodies and CD4-Based Reagents Is Independent of Coreceptor Usage. J. Virol., 72:1876-1885, 1998. PubMed ID: 9499039.
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Trkola2005
Alexandra Trkola, Herbert Kuster, Peter Rusert, Beda Joos, Marek Fischer, Christine Leemann, Amapola Manrique, Michael Huber, Manuela Rehr, Annette Oxenius, Rainer Weber, Gabriela Stiegler, Brigitta Vcelar, Hermann Katinger, Leonardo Aceto, and Huldrych F. Günthard. Delay of HIV-1 Rebound after Cessation of Antiretroviral Therapy through Passive Transfer of Human Neutralizing Antibodies. Nat. Med., 11(6):615-622, Jun 2005. PubMed ID: 15880120.
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D. Tudor, M. Derrien, L. Diomede, A.-S. Drillet, M. Houimel, C. Moog, J.-M. Reynes, L. Lopalco, and M. Bomsel. HIV-1 gp41-Specific Monoclonal Mucosal IgAs Derived from Highly Exposed but IgG-Seronegative Individuals Block HIV-1 Epithelial Transcytosis and Neutralize CD4+ Cell Infection: An IgA Gene and Functional Analysis. Mucosal Immunol., 2(5):412-426, Sep 2009. PubMed ID: 19587640.
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Tudor2011
Daniela Tudor and Morgane Bomsel. The Broadly Neutralizing HIV-1 IgG 2F5 Elicits gp41-Specific Antibody-Dependent Cell Cytotoxicity in a FcgammaRI-Dependent Manner. AIDS, 25(6):751-759, 27 Mar 2011. PubMed ID: 21330910.
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Tudor2012
Daniela Tudor, Huifeng Yu, Julien Maupetit, Anne-Sophie Drillet, Tahar Bouceba, Isabelle Schwartz-Cornil, Lucia Lopalco, Pierre Tuffery, and Morgane Bomsel. Isotype Modulates Epitope Specificity, Affinity, and Antiviral Activities of Anti-HIV-1 Human Broadly Neutralizing 2F5 Antibody. Proc. Natl. Acad. Sci. U.S.A., 109(31):12680-12685, 31 Jul 2012. PubMed ID: 22723360.
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P. R. Tulip, C. R. Gregor, R. Z. Troitzsch, G. J. Martyna, E. Cerasoli, G. Tranter, and J. Crain. Conformational Plasticity in an HIV-1 Antibody Epitope. J. Phys. Chem. B, 114(23):7942-7950, 17 Jun 2010. PubMed ID: 20491462.
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O. Iu. Tumanova, V. N. Kuvshinov, M. Sh. Azaev, A. E. Masharskii, N. A. Klimov, A. P. Kozlov, A. A. Il'ichev, and L. S. Sandakhchiev. [Construction of peptide mimetics of an epitope of the human immunodeficiency virus (HIV-1) gp41 protein, recognized by virus-neutralizing antibodies 2F5]. Mol Biol (Mosk), 35(1):146--51, Jan-Feb 2001. Article in Russian. PubMed ID: 11234374.
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I. Turbica, F. Simon, J. M. Besnier, B. LeJeune, P. Choutet, A Goudeau, and F. Barin. Temporal Development and Prognostic Value of Antibody Response to the Major Neutralizing Epitopes of gp120 during HIV-1 Infection. J. Med. Virol., 52:309-315, 1997. PubMed ID: 9210041.
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S. Ugolini, I. Mondor, P. W. H. I Parren, D. R. Burton, S. A. Tilley, P. J. Klasse, and Q. J. Sattentau. Inhibition of Virus Attachment to CD4+ Target Cells Is a Major Mechanism of T Cell Line-Adapted HIV-1 Neutralization. J. Exp. Med., 186:1287-1298, 1997. PubMed ID: 9334368.
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Utachee2009
Piraporn Utachee, Piyamat Jinnopat, Panasda Isarangkura-na-ayuthaya, U. Chandimal de Silva, Shota Nakamura, Uamporn Siripanyaphinyo, Nuanjun Wichukchinda, Kenzo Tokunaga, Teruo Yasunaga, Pathom Sawanpanyalert, Kazuyoshi Ikuta, Wattana Auwanit, and Masanori Kameoka. Phenotypic Studies on Recombinant Human Immunodeficiency Virus Type 1 (HIV-1) Containing CRF01\_AE env Gene Derived from HIV-1-Infected Patient, Residing in Central Thailand. Microbes Infect., 11(3):334-343, Mar 2009. PubMed ID: 19136072.
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vandenKerkhof2013
Tom L. G. M. van den Kerkhof, K. Anton Feenstra, Zelda Euler, Marit J. van Gils, Linda W. E. Rijsdijk, Brigitte D. Boeser-Nunnink, Jaap Heringa, Hanneke Schuitemaker, and Rogier W. Sanders. HIV-1 Envelope Glycoprotein Signatures That Correlate with the Development of Cross-Reactive Neutralizing Activity. Retrovirology, 10:102, 23 Sep 2013. PubMed ID: 24059682.
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vanGils2011
Marit J. van Gils, Evelien M. Bunnik, Brigitte D. Boeser-Nunnink, Judith A. Burger, Marijke Terlouw-Klein, Naomi Verwer, and Hanneke Schuitemaker. Longer V1V2 Region with Increased Number of Potential N-Linked Glycosylation Sites in the HIV-1 Envelope Glycoprotein Protects against HIV-Specific Neutralizing Antibodies. J. Virol., 85(14):6986-6995, Jul 2011. PubMed ID: 21593147.
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vanGils2011a
Marit J. van Gils, Diana Edo-Matas, Emma J. Bowles, Judith A. Burger, Guillaume B. Stewart-Jones, and Hanneke Schuitemaker. Evolution of Human Immunodeficiency Virus Type 1 in a Patient with Cross-Reactive Neutralizing Activity in Serum. J. Virol., 85(16):8443-8438, Aug 2011. PubMed ID: 21653664.
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vanMontfort2007
Thijs van Montfort, Alexey A. Nabatov, Teunis B. H. Geijtenbeek, Georgios Pollakis, and William A. Paxton. Efficient Capture of Antibody Neutralized HIV-1 by Cells Expressing DC-SIGN and Transfer to CD4+ T Lymphocytes. J. Immunol., 178(5):3177-85, 1 Mar 2007. PubMed ID: 17312166.
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vanMontfort2008
Thijs van Montfort, Adri A. M. Thomas, Georgios Pollakis, and William A. Paxton. Dendritic Cells Preferentially Transfer CXCR4-Using Human Immunodeficiency Virus Type 1 Variants to CD4+ T Lymphocytes in trans. J. Viro.l, 82(16):7886-7896, Aug 2008. PubMed ID: 18524826.
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vanMontfort2011
Thijs van Montfort, Mark Melchers, Gözde Isik, Sergey Menis, Po-Ssu Huang, Katie Matthews, Elizabeth Michael, Ben Berkhout, William R. Schief, John P. Moore, and Rogier W. Sanders. A Chimeric HIV-1 Envelope Glycoprotein Trimer with an Embedded Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) Domain Induces Enhanced Antibody and T Cell Responses. J. Biol. Chem., 286(25):22250-22261, 24 Jun 2011. PubMed ID: 21515681.
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Vcelar2007
Brigitta Vcelar, Gabriela Stiegler, Hermann M. Wolf, Wolfgang Muntean, Bettina Leschnik, Saurabh Mehandru, Martin Markowitz, Christine Armbruster, Renate Kunert, Martha M. Eibl, and Hermann Katinger. Reassessment of Autoreactivity of the Broadly Neutralizing HIV Antibodies 4E10 and 2F5 and Retrospective Analysis of Clinical Safety Data. AIDS, 21(16):2161-2170, 18 Oct 2007. PubMed ID: 18090042.
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Veiga2006
Ana Salomé Veiga and Miguel A. R. B. Castanho. The Membranes' Role in the HIV-1 Neutralizing Monoclonal Antibody 2F5 Mode of Action Needs Re-Evaluation. Antiviral Res., 71(1):69-72, Aug 2006. PubMed ID: 16530275.
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Veiga2009
Ana S. Veiga, Leonard K. Pattenden, Jordan M. Fletcher, Miguel A. R. B. Castanho, and Marie Isabel Aguilar. Interactions of HIV-1 Antibodies 2F5 and 4E10 with a gp41 Epitope Prebound to Host and Viral Membrane Model Systems. ChemBioChem, 10(6):1032-1044, 17 Apr 2009. PubMed ID: 19283693.
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Venditto2013
Vincent J. Venditto, Douglas S. Watson, Michael Motion, David Montefiori, and Francis C. Szoka, Jr. Rational Design of Membrane Proximal External Region Lipopeptides Containing Chemical Modifications for HIV-1 Vaccination. Clin Vaccine Immunol, 20(1):39-45, Jan 2013. PubMed ID: 23114698.
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Verkoczy2009
Laurent Verkoczy, M. Anthony Moody, T. Matt Holl, Hilary Bouton-Verville, Richard M. Scearce, Jennifer Hutchinson, S. Munir Alam, Garnett Kelsoe, and Barton F. Haynes. Functional, Non-Clonal IgMa-Restricted B Cell Receptor Interactions with the HIV-1 Envelope gp41 Membrane Proximal External Region. PLoS One, 4(10):e7215, 2009. PubMed ID: 19806186.
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Verkoczy2010
Laurent Verkoczy, Marilyn Diaz, T. Matt Holl, Ying-Bin Ouyang, Hilary Bouton-Verville, S. Munir Alam, Hua-Xin Liao, Garnett Kelsoe, and Barton F. Haynes. Autoreactivity in an HIV-1 Broadly Reactive Neutralizing Antibody Variable Region Heavy Chain Induces Immunologic Tolerance. Proc. Natl. Acad. Sci. U.S.A., 107(1):181-186, 5 Jan 2010. PubMed ID: 20018688.
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Verkoczy2011
Laurent Verkoczy, Yao Chen, Hilary Bouton-Verville, Jinsong Zhang, Marilyn Diaz, Jennifer Hutchinson, Ying-Bin Ouyang, S. Munir Alam, T. Matt Holl, Kwan-Ki Hwang, Garnett Kelsoe, and Barton F. Haynes. Rescue of HIV-1 Broad Neutralizing Antibody-Expressing B Cells in 2F5 VH x VL Knockin Mice Reveals Multiple Tolerance Controls. J. Immunol., 187(7):3785-3797, 1 Oct 2011. PubMed ID: 21908739.
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Verrier2001
F. Verrier, A. Nadas, M. K. Gorny, and S. Zolla-Pazner. Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. J. Virol., 75(19):9177--86, Oct 2001. URL: http://jvi.asm.org/cgi/content/full/75/19/9177. PubMed ID: 11533181.
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Vincent2005
Nadine Vincent, Jean-Claude Tardy, Jean-Michel Livrozet, Frédéric Lucht, Anne Frésard, Christian Genin, and Etienne Malvoisin. Depletion in Antibodies Targeted to the HR2 Region of HIV-1 Glycoprotein gp41 in Sera of HIV-1-Seropositive Patients Treated with T20. J. Acquir. Immune Defic. Syndr., 38(3):254-262, 1 Mar 2005. PubMed ID: 15735441.
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Vincent2008
Nadine Vincent, Amadou Kone, Blandine Chanut, Frédéric Lucht, Christian Genin, and Etienne Malvoisin. Antibodies Purified from Sera of HIV-1-Infected Patients by Affinity on the Heptad Repeat Region 1/Heptad Repeat Region 2 Complex of gp41 Neutralize HIV-1 Primary Isolates. AIDS, 22(16):2075-2085, 18 Oct 2008. PubMed ID: 18832871.
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Virnik2018
Konstantin Virnik, Edmund Nesti, Cody Dail, Aaron Scanlan, Alexei Medvedev, Russell Vassell, Andrew T. McGuire, Leonidas Stamatatos, and Ira Berkower. Live Rubella Vectors Can Express Native HIV Envelope Glycoproteins Targeted by Broadly Neutralizing Antibodies and Prime the Immune Response to an Envelope Protein Boost. Vaccine, 36(34):5166-5172, 16 Aug 2018. PubMed ID: 30037665.
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vonBredow2016
Benjamin von Bredow, Juan F. Arias, Lisa N. Heyer, Brian Moldt, Khoa Le, James E. Robinson, Susan Zolla-Pazner, Dennis R. Burton, and David T. Evans. Comparison of Antibody-Dependent Cell-Mediated Cytotoxicity and Virus Neutralization by HIV-1 Env-Specific Monoclonal Antibodies. J. Virol., 90(13):6127-6139, 1 Jul 2016. PubMed ID: 27122574.
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Vu2006
John R. Vu, Timothy Fouts, Katherine Bobb, Jennifer Burns, Brenda McDermott, David I. Israel, Karla Godfrey, and Anthony DeVico. An Immunoglobulin Fusion Protein Based on the gp120-CD4 Receptor Complex Potently Inhibits Human Immunodeficiency Virus Type 1 In Vitro. AIDS Res. Hum. Retroviruses, 22(6):477-490, Jun 2006. PubMed ID: 16796521.
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Walker2009a
Laura M. Walker, Sanjay K. Phogat, Po-Ying Chan-Hui, Denise Wagner, Pham Phung, Julie L. Goss, Terri Wrin, Melissa D. Simek, Steven Fling, Jennifer L. Mitcham, Jennifer K. Lehrman, Frances H. Priddy, Ole A. Olsen, Steven M. Frey, Phillip W . Hammond, Protocol G Principal Investigators, Stephen Kaminsky, Timothy Zamb, Matthew Moyle, Wayne C. Koff, Pascal Poignard, and Dennis R. Burton. Broad and Potent Neutralizing Antibodies from an African Donor Reveal a new HIV-1 Vaccine Target. Science, 326(5950):285-289, 9 Oct 2009. PubMed ID: 19729618.
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Walker2010
Laura M. Walker, Melissa D. Simek, Frances Priddy, Johannes S. Gach, Denise Wagner, Michael B. Zwick, Sanjay K. Phogat, Pascal Poignard, and Dennis R. Burton. A Limited Number of Antibody Specificities Mediate Broad and Potent Serum Neutralization in Selected HIV-1 Infected Individuals. PLoS Pathog., 6(8), 2010. PubMed ID: 20700449.
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Walker2010a
Laura M. Walker and Dennis R. Burton. Rational Antibody-Based HIV-1 Vaccine Design: Current Approaches and Future Directions. Curr. Opin. Immunol., 22(3):358-366, Jun 2010. PubMed ID: 20299194.
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Wallace2009
Aaron Wallace and Leonidas Stamatatos. Introduction of Exogenous Epitopes in the Variable Regions of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein: Effect on Viral Infectivity and the Neutralization Phenotype. J. Virol., 83(16):7883-7893, Aug 2009. PubMed ID: 19494007.
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Wang2003
Lai-Xi Wang. Bioorganic Approaches towards HIV Vaccine Design. Curr. Pharm. Des., 9(22):1771-87, 2003. PubMed ID: 12871196.
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Wang2005
Zuguang Wang, Zuqiang Liu, Xiwen Cheng, and Ying-Hua Chen. The Recombinant Immunogen with High-Density Epitopes of ELDKWA and ELDEWA Induced Antibodies Recognizing Both Epitopes on HIV-1 gp41. Microbiol. Immunol., 49(8):703-709, 2005. PubMed ID: 16113499.
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Wang2006
Shixia Wang, Ranajit Pal, John R. Mascola, Te-Hui W. Chou, Innocent Mboudjeka, Siyuan Shen, Qin Liu, Stephen Whitney, Timothy Keen, B. C. Nair, V. S. Kalyanaraman, Philip Markham, and Shan Lu. Polyvalent HIV-1 Env Vaccine Formulations Delivered by the DNA Priming Plus Protein Boosting Approach Are Effective in Generating Neutralizing Antibodies against Primary Human Immunodeficiency Virus Type 1 Isolates From Subtypes A, B, C, D and E. Virology, 350(1):34-47, 20 Jun 2006. PubMed ID: 16616287.
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Wang2010
Pengcheng Wang and Xinzhen Yang. Neutralization Efficiency Is Greatly Enhanced by Bivalent Binding of an Antibody to Epitopes in the V4 Region and the Membrane-Proximal External Region within One Trimer of Human Immunodeficiency Virus Type 1 Glycoproteins. J. Virol., 84(14):7114-7123, Jul 2010. PubMed ID: 20463081.
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Wang2011
Ji Wang, Liling Xu, Pei Tong, and Ying-Hua Chen. Mucosal Antibodies Induced by Tandem Repeat of 2F5 Epitope Block Transcytosis of HIV-1. Vaccine, 29(47):8542-8548, 3 Nov 2011. PubMed ID: 21939723.
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Wang2011a
Ji Wang, Pei Tong, Lu Lu, Leilei Zhou, Liling Xu, Shibo Jiang, and Ying-hua Chen. HIV-1 gp41 Core with Exposed Membrane-Proximal External Region Inducing Broad HIV-1 Neutralizing Antibodies. PLoS One, 6(3):e18233, 2011. PubMed ID: 21483871.
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Wang2011b
Suting Wang, Jianhui Nie, and Youchun Wang. Comparisons of the Genetic and Neutralization Properties of HIV-1 Subtype C and CRF07/08\_BC env Molecular Clones Isolated from Infections in China. Virus Res., 155(1):137-146, Jan 2011. PubMed ID: 20875470.
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Wang2012
Shixia Wang, Michael Kishko, Shengqin Wan, Yan Wang, Frank Brewster, Glenda E. Gray, Avye Violari, John L. Sullivan, Mohan Somasundaran, Katherine Luzuriaga, and Shan Lu. Pilot Study on the Immunogenicity of Paired Env Immunogens from Mother-to-Child Transmitted HIV-1 Isolates. Hum. Vaccin. Immunother., 8(11):1638-1647, 1 Nov 2012. PubMed ID: 23151449.
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Wang2013
Wenbo Wang, Jianhui Nie, Courtney Prochnow, Carolyn Truong, Zheng Jia, Suting Wang, Xiaojiang S. Chen, and Youchun Wang. A Systematic Study of the N-Glycosylation Sites of HIV-1 Envelope Protein on Infectivity and Antibody-Mediated Neutralization. Retrovirology, 10:14, 2013. PubMed ID: 23384254.
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Wang2018a
Hongye Wang, Ting Yuan, Tingting Li, Yanpeng Li, Feng Qian, Chuanwu Zhu, Shujia Liang, Daniel Hoffmann, Ulf Dittmer, Binlian Sun, and Rongge Yang. Evaluation of Susceptibility of HIV-1 CRF01\_AE Variants to Neutralization by a Panel of Broadly Neutralizing Antibodies. Arch. Virol., 163(12):3303-3315, Dec 2018. PubMed ID: 30196320.
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Webb2015
Nicholas E. Webb, David C. Montefiori, and Benhur Lee. Dose-Response Curve Slope Helps Predict Therapeutic Potency and Breadth of HIV Broadly Neutralizing Antibodies. Nat. Commun., 6:8443, 29 Sep 2015. PubMed ID: 26416571.
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West2012a
Anthony P. West, Jr., Ron Diskin, Michel C. Nussenzweig, and Pamela J. Bjorkman. Structural Basis for Germ-Line Gene Usage of a Potent Class of Antibodies Targeting the CD4-Binding Site of HIV-1 gp120. Proc. Natl. Acad. Sci. U.S.A., 109(30):E2083-E2090, 24 Jul 2012. PubMed ID: 22745174.
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West2013
Anthony P. West, Jr., Louise Scharf, Joshua Horwitz, Florian Klein, Michel C. Nussenzweig, and Pamela J. Bjorkman. Computational Analysis of Anti-HIV-1 Antibody Neutralization Panel Data to Identify Potential Functional Epitope Residues. Proc. Natl. Acad. Sci. U.S.A., 110(26):10598-10603, 25 Jun 2013. PubMed ID: 23754383.
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Wiehe2018
Kevin Wiehe, Todd Bradley, R. Ryan Meyerhoff, Connor Hart, Wilton B. Williams, David Easterhoff, William J. Faison, Thomas B. Kepler, Kevin O. Saunders, S. Munir Alam, Mattia Bonsignori, and Barton F. Haynes. Functional Relevance of Improbable Antibody Mutations for HIV Broadly Neutralizing Antibody Development. Cell Host Microbe, 23(6):759-765.e6, 13 Jun 2018. PubMed ID: 29861171.
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Willey2008
Suzanne Willey and Marlén M. I. Aasa-Chapman. Humoral Immunity to HIV-1: Neutralisation and Antibody Effector Functions. Trends Microbiol., 16(12):596-604, Dec 2008. PubMed ID: 18964020.
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Wolbank2003
Susanne Wolbank, Renate Kunert, Gabriela Stiegler, and Hermann Katinger. Characterization of Human Class-Switched Polymeric (Immunoglobulin M [IgM] and IgA) Anti-Human Immunodeficiency Virus Type 1 Antibodies 2F5 and 2G12. J. Virol., 77(7):4095-4103, Apr 2003. PubMed ID: 12634368.
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Wu2010
Xueling Wu, Zhi-Yong Yang, Yuxing Li, Carl-Magnus Hogerkorp, William R. Schief, Michael S. Seaman, Tongqing Zhou, Stephen D. Schmidt, Lan Wu, Ling Xu, Nancy S. Longo, Krisha McKee, Sijy O'Dell, Mark K. Louder, Diane L. Wycuff, Yu Feng, Martha Nason, Nicole Doria-Rose, Mark Connors, Peter D. Kwong, Mario Roederer, Richard T. Wyatt, Gary J. Nabel, and John R. Mascola. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1. Science, 329(5993):856-861, 13 Aug 2010. PubMed ID: 20616233.
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Xiang2002
Shi-Hua. Xiang, Peter D. Kwong, Rishi Gupta, Carlo D. Rizzuto, David J. Casper, Richard Wyatt, Liping Wang, Wayne A. Hendrickson, Michael L. Doyle, and Joseph Sodroski. Mutagenic Stabilization and/or Disruption of a CD4-Bound State Reveals Distinct Conformations of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. J. Virol., 76(19):9888-9899, Oct 2002. PubMed ID: 12208966.
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Xiao2000a
Y. Xiao, Y. Zhao, Y. Lu, and Y. H. Chen. Epitope-Vaccine Induces High Levels of ELDKWA-Epitope-Specific Neutralizing Antibody. Immunol. Invest., 29:41-50, 2000. PubMed ID: 10709845.
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Xiao2009
Xiaodong Xiao, Weizao Chen, Yang Feng, Zhongyu Zhu, Ponraj Prabakaran, Yanping Wang, Mei-Yun Zhang, Nancy S. Longo, and Dimiter S. Dimitrov. Germline-Like Predecessors of Broadly Neutralizing Antibodies Lack Measurable Binding to HIV-1 Envelope Glycoproteins: Implications for Evasion of Immune Responses and Design of Vaccine Immunogens. Biochem. Biophys. Res. Commun., 390(3):404-409, 18 Dec 2009. PubMed ID: 19748484.
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Xu2001
W. Xu, B. A. Smith-Franklin, P. L. Li, C. Wood, J. He, Q. Du, G. J. Bhat, C. Kankasa, H. Katinger, L. A. Cavacini, M. R. Posner, D. R. Burton, T. C. Chou, and R. M. Ruprecht. Potent neutralization of primary human immunodeficiency virus clade C isolates with a synergistic combination of human monoclonal antibodies raised against clade B. J Hum Virol, 4(2):55--61, Mar-Apr 2001. PubMed ID: 11437315.
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Xu2002
Weidong Xu, Regina Hofmann-Lehmann, Harold M. McClure, and Ruth M. Ruprecht. Passive Immunization with Human Neutralizing Monoclonal Antibodies: Correlates of Protective Immunity against HIV. Vaccine, 20(15):1956-1960, 6 May 2002. PubMed ID: 11983253.
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Yamamoto2008
Hiroyuki Yamamoto and Tetsuro Matano. Anti-HIV Adaptive Immunity: Determinants for Viral Persistence. Rev. Med. Virol., 18(5):293-303, Sep-Oct 2008. PubMed ID: 18416450.
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Yang1998
G. Yang, M. P. D'Souza, and G. N. Vyas. Neutralizing Antibodies against HIV Determined by Amplification of Viral Long Terminal Repeat Sequences from Cells Infected In Vitro by Nonneutralized Virions. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 17:27-34, 1998. A neutralization assay was developed based on heminested PCR amplification of the LTR (HNPCR) -- LTR-HNPCR consistently revealed HIV DNA and was shown to be a rapid, specific and reliable neutralization assay based on tests with 6 MAbs and 5 HIV isolates. PubMed ID: 9436755.
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Yang2000
Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881.
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Yang2005b
Xinzhen Yang, Svetla Kurteva, Sandra Lee, and Joseph Sodroski. Stoichiometry of Antibody Neutralization of Human Immunodeficiency Virus Type 1. J. Virol., 79(6):3500-3508, Mar 2005. PubMed ID: 15731244.
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Yang2006
Xinzhen Yang, Inna Lipchina, Simon Cocklin, Irwin Chaiken, and Joseph Sodroski. Antibody Binding Is a Dominant Determinant of the Efficiency of Human Immunodeficiency Virus Type 1 Neutralization. J. Virol., 80(22):11404-11408, Nov 2006. PubMed ID: 16956933.
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Yang2013
Guang Yang, T. Matt Holl, Yang Liu, Yi Li, Xiaozhi Lu, Nathan I. Nicely, Thomas B. Kepler, S. Munir Alam, Hua-Xin Liao, Derek W. Cain, Leonard Spicer, John L. VandeBerg, Barton F. Haynes, and Garnett Kelsoe. Identification of Autoantigens Recognized by the 2F5 and 4E10 Broadly Neutralizing HIV-1 Antibodies. J. Exp. Med., 210(2):241-256, 11 Feb 2013. PubMed ID: 23359068.
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Yang2014
Lili Yang and Pin Wang. Passive Immunization against HIV/AIDS by Antibody Gene Transfer. Viruses, 6(2):428-447, Feb 2014. PubMed ID: 24473340.
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Yang2018
Zheng Yang, Xi Liu, Zehua Sun, Jingjing Li, Weiguo Tan, Weiye Yu, and Meiyun Zhang. Identification of a HIV gp41-Specific Human Monoclonal Antibody with Potent Antibody-Dependent Cellular Cytotoxicity. Front. Immunol., 9:2613, 2018. PubMed ID: 30519238.
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Yates2018
Nicole L. Yates, Allan C. deCamp, Bette T. Korber, Hua-Xin Liao, Carmela Irene, Abraham Pinter, James Peacock, Linda J. Harris, Sheetal Sawant, Peter Hraber, Xiaoying Shen, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayapan, Phillip W. Berman, Merlin L. Robb, Giuseppe Pantaleo, Susan Zolla-Pazner, Barton F. Haynes, S. Munir Alam, David C. Montefiori, and Georgia D. Tomaras. HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees. J. Virol., 92(8), 15 Apr 2018. PubMed ID: 29386288.
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Ye2006
Ling Ye, Yuliang Sun, Jianguo Lin, Zhigao Bu, Qingyang Wu, Shibo Jiang, David A. Steinhauer, Richard W. Compans, and Chinglai Yang. Antigenic Properties of a Transport-Competent Influenza HA/HIV Env Chimeric Protein. Virology, 352(1):74-85, 15 Aug 2006. PubMed ID: 16725170.
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Yee2011
Michael Yee, Krystyna Konopka, Jan Balzarini, and Nejat Düzgüneş. Inhibition of HIV-1 Env-Mediated Cell-Cell Fusion by Lectins, Peptide T-20, and Neutralizing Antibodies. Open Virol. J., 5:44-51, 2011. PubMed ID: 21660189.
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York2001
J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697.
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Yuan2005
Wen Yuan, Stewart Craig, Xinzhen Yang, and Joseph Sodroski. Inter-Subunit Disulfide Bonds in Soluble HIV-1 Envelope Glycoprotein Trimers. Virology, 332(1):369-383, 5 Feb 2005. PubMed ID: 15661168.
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Yuan2009
Wen Yuan, Xing Li, Marta Kasterka, Miroslaw K. Gorny, Susan Zolla-Pazner, and Joseph Sodroski. Oligomer-Specific Conformations of the Human Immunodeficiency Virus (HIV-1) gp41 Envelope Glycoprotein Ectodomain Recognized by Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 25(3):319-328, Mar 2009. PubMed ID: 19292593.
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Yuste2006
Eloisa Yuste, Hannah B. Sanford, Jill Carmody, Jacqueline Bixby, Susan Little, Michael B. Zwick, Tom Greenough, Dennis R. Burton, Douglas D. Richman, Ronald C. Desrosiers, and Welkin E. Johnson. Simian Immunodeficiency Virus Engrafted with Human Immunodeficiency Virus Type 1 (HIV-1)-Specific Epitopes: Replication, Neutralization, and Survey of HIV-1-Positive Plasma. J. Virol., 80(6):3030-3041, Mar 2006. PubMed ID: 16501112.
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ZederLutz2001
G. Zeder-Lutz, J. Hoebeke, and M. H. Van Regenmortel. Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies. Eur. J. Biochem., 268(10):2856--66, May 2001. PubMed ID: 11358501.
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Zhang2002
Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155.
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Zhang2005
Geng Zhang, Hong Lu, Yun Lu, ShiBo Jiang, and Ying-Hua Chen. Neutralization of HIV-1 Primary Isolate by ELDKWA-Specific Murine Monoclonal Antibodies. Immunobiology, 210(9):639-645, 2005. PubMed ID: 16323702.
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Zhang2006a
Mei-Yun Zhang, Vidita Choudhry, Igor A. Sidorov, Vladimir Tenev, Bang K Vu, Anil Choudhary, Hong Lu, Gabriela M. Stiegler, Hermann W. D. Katinger, Shibo Jiang, Christopher C. Broder, and Dimiter S. Dimitrov. Selection of a Novel gp41-Specific HIV-1 Neutralizing Human Antibody by Competitive Antigen Panning. J. Immunol. Methods, 317(1-2):21-30, 20 Dec 2006. PubMed ID: 17078964.
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Zhang2007
Mei-Yun Zhang and Dimiter S. Dimitrov. Novel Approaches for Identification of Broadly Cross-Reactive HIV-1 Neutralizing Human Monoclonal Antibodies and Improvement of Their Potency. Curr. Pharm. Des., 13(2):203-212, 2007. PubMed ID: 17269928.
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Zhang2008
Mei-Yun Zhang, Bang K. Vu, Anil Choudhary, Hong Lu, Michael Humbert, Helena Ong, Munir Alam, Ruth M. Ruprecht, Gerald Quinnan, Shibo Jiang, David C. Montefiori, John R. Mascola, Christopher C. Broder, Barton F. Haynes, and Dimiter S. Dimitrov. Cross-Reactive Human Immunodeficiency Virus Type 1-Neutralizing Human Monoclonal Antibody That Recognizes a Novel Conformational Epitope on gp41 and Lacks Reactivity against Self-Antigens. J. Virol., 82(14):6869-6879, Jul 2008. PubMed ID: 18480433.
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Zhang2010
Mei-Yun Zhang, Andrew Rosa Borges, Roger G. Ptak, Yanping Wang, Antony S. Dimitrov, S. Munir Alam, Lindsay Wieczorek, Peter Bouma, Timothy Fouts, Shibo Jiang, Victoria R. Polonis, Barton F. Haynes, Gerald V. Quinnan, David C. Montefiori, and Dimiter S. Dimitrov. Potent and Broad Neutralizing Activity of a Single Chain Antibody Fragment against Cell-Free and Cell-Associated HIV-1. mAbs, 2(3):266-274, May-Jun 2010. PubMed ID: 20305395.
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Zhang2010a
Hong Zhang, Marzena Rola, John T. West, Damien C. Tully, Piotr Kubis, Jun He, Chipepo Kankasa, and Charles Wood. Functional Properties of the HIV-1 Subtype C Envelope Glycoprotein Associated with Mother-to-Child Transmission. Virology, 400(2):164-174, 10 May 2010. PubMed ID: 20096914.
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Zhang2014
Jinsong Zhang, S. Munir Alam, Hilary Bouton-Verville, Yao Chen, Amanda Newman, Shelley Stewart, Frederick H. Jaeger, David C. Montefiori, S. Moses Dennison, Barton F. Haynes, and Laurent Verkoczy. Modulation of Nonneutralizing HIV-1 gp41 Responses by an MHC-Restricted TH Epitope Overlapping Those of Membrane Proximal External Region Broadly Neutralizing Antibodies. J. Immunol., 192(4):1693-1706, 15 Feb 2014. PubMed ID: 24465011.
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Zhang2014a
Yuan Zhang and Celeste Sagui. The gp41(659-671) HIV-1 Antibody Epitope: A Structurally Challenging Small Peptide. J. Phys. Chem. B, 118(1):69-80, 9 Jan 2014. PubMed ID: 24359409.
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Zhang2016
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Wang2019
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Sliepen2019
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Displaying record number 1370
Download this epitope
record as JSON.
MAb ID |
2G12 (c2G12, G12) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
Herman Katinger, Inst. Appl. Microbiol. or Polymun Scientific Inc., Vienna, Austria, |
Epitope |
(Discontinuous epitope)
|
Subtype |
AD |
Ab Type |
gp120 glycosylation sites in C2, C3, C4, and V4, gp120 glycans |
Neutralizing |
L P View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human(IgG1κ) |
Patient |
|
Immunogen |
HIV-1 infection |
Keywords |
acute/early infection, anti-idiotype, antibody binding site, antibody gene transfer, antibody generation, antibody interactions, antibody lineage, antibody polyreactivity, antibody sequence, assay or method development, autoantibody or autoimmunity, autologous responses, binding affinity, brain/CSF, broad neutralizer, cell-line isolated antibody, co-receptor, complement, computational prediction, dendritic cells, drug resistance, dynamics, early treatment, effector function, elite controllers and/or long-term non-progressors, enhancing activity, escape, genital and mucosal immunity, glycosylation, HAART, ART, HIV reservoir/latency/provirus, immunoprophylaxis, immunotherapy, isotype switch, kinetics, memory cells, mimics, mimotopes, mother-to-infant transmission, mutation acquisition, neutralization, NK cells, polyclonal antibodies, rate of progression, responses in children, review, SIV, structure, subtype comparisons, supervised treatment interruptions (STI), therapeutic vaccine, transmission pair, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity, viral fitness and/or reversion |
Notes
Showing 562 of
562 notes.
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2G12: Eighty clusters of overlapping epitopes that could bind to MHC Class II HLA-DR1*01:01 (DR1) allele were identified by LC-MS/MS using a cell-free processing system that incorporated soluble DR1, HLA-DM (DM), cathepsins, and full-length protein antigens (Gag, Pol, Env, Vif, Tat, Rev, and Nef). Sixteen of Env CD4+ T cell epitopes identified in this study, which were primarily located in the vicinity of the gp120/gp41 interface or the CD4bs, were assessed for overlap with bnAb binding footprints. Only unglycosylated KAM432-444 (KAMYAPPISGQIR) overlapped with the binding footprint of V3 glycan-targeting bnAb 2G12.
Sengupta2023
(antibody binding site)
-
2G12: The study describes the generation, crystal structure, and immunogenic properties of a native-like Env SOSIP trimer based on a group M consensus (ConM) sequence. A crystal structure of ConM SOSIP.v7 trimer together with nAbs PGT124 and 35O22 revealed that ConM SOSIP.v7 is structurally similar to other Env trimers. In rabbits, the ConM SOSIP trimer induced serum nAbs that neutralized the autologous Tier 1A virus (ConM from 2004) and a related Tier 1B ConS virus (ConM from 2001). These responses target the trimer apex and were enhanced when the trimers were presented on ferritin nanoparticles. The neutralization of ConM and ConS pseudoviruses was tested against a large panel of nAbs and non-nAbs (2219, 2557, 3074, 3869, 447-52D, 830A, 654-30D, 1008-30D, 1570D, 729-30D, F105, 181D, 246D, 50-69D, sCD4, VRC01, 3BNC117, CH31, PG9, PG16, CH01, PGDM1400, PGT128, PGT121, 10-1074, PGT151, VRC43.01, 2G12, DH511.2_K3, 10E8, 2F5, 4E10); most nAbs were able to neutralize these pseudoviruses. Soluble ConM trimers were able to weakly activate B cells expressing PGT121 and PG16 BCRs but were inactive against those expressing VRC01 and PGT145. In contrast, at the same molar amount of trimers, the ConM SOSIP.v7-ferritin nanoparticles activated all 4 B cells efficiently. Binding of bnAbs 2G12 and PGT145 and non-nAbs F105 and 19b to ConM SOSIP.v7 trimer and SOSIP showed that the ferritin-bound trimer bound more avidly than the soluble trimer. This study shows that native-like HIV-1 Env trimers can be generated from consensus sequences, and such immunogens might be suitable vaccine components to prime and/or boost desirable nAb responses.
Sliepen2019
(neutralization, vaccine antigen design, binding affinity)
-
2G12: Following the VRC018 clinical trial of the BG505 DS-SOSIP immunogen, donor N751 showed the highest BG505-reactive ELISA responses. B cells from this donor were sorted for binding to a novel BG505 trimer construct (BG505 glycan base); 8 clones were identified that bound to glycan-base BG505, and 2 were selected for characterization (2C06 and 2C09). The epitopes of 2C06.01 and 2C09.01 were similar to each other, and have substantial overlap with the epitope of VRC34.01, and lower overlap with two other FP-targeting mAbs, PGT151 and ACS202. Binding of mAbs to BG505 DS-SOSIP was compared with binding to the glycan base construct; some mAbs bound to both BG505 DS-SOSIP and glycan base (PGT145, VRC26.25, VRC01, PGT151, VRC34.01, and 2G12), some bound to neither (PG05, 447-52D, and 2557), and 4 base-binding mAbs bound to BG505 DS-SOSIP, but not to BG505 glycan base (1E6, 5H3, 3H2, and 9B9).
Wang2023
(binding affinity)
-
2G12: A panel of 30 contemporary subtype B pseudoviruses (PSVs) was generated. Neutralization sensitivities of these PSVs were compared with subtype B strains from earlier in the pandemic using 31 nAbs (PG9, PG16, PGT145, PGDM1400, CH02, CH03, CH04, 830A, PGT121, PGT126, PGT128, PGT130, 10-1074, 2192, 2219, 3074, 3869, 447-52D, b12, NIH45-46, VRC01, VRC03, 3BNC117, HJ16, sCD4, 10E8, 4E10, 2F5, 7H6, 2G12, 35O22). A significant reduction in Env neutralization sensitivity was observed for 27 out of 31 nAbs for the contemporary, as compared to earlier-decade subtype B PSVs. A decline in neutralization sensitivity was observed across all Env domains; the nAbs that were most potent early in the pandemic suffered the greatest decline in potency over time. A metaanalysis demonstrated this trend across multiple subtypes. As HIV-1 Env diversification continues, changes in Env antigenicity and neutralization sensitivity should continue to be evaluated to inform the development of improved vaccine and antibody products to prevent and treat HIV-1.
Wieczorek2023
(neutralization, viral fitness and/or reversion)
-
2G12: Pseudoviruses were made from 13 env sequences of subtypes A6 and CRF63_02A6, based on genetic variants of HIV-1 circulating in the Siberian Federal District. Neutralization of these viruses was tested for 8 bnAbs. Most of the pseudoviruses were sensitive to neutralization by VRC01, PGT126, and 10E8, moderately sensitive to PG9 and 4E10, and resistant to 2G12, PG16, and 2F5. All obtained variants of pseudoviruses were CCR5-tropic.
Rudometova2022
(co-receptor, neutralization, subtype comparisons)
-
2G12:This study identified a B cell lineage of bNAbs in an HIV-1 elite post-treatment controller (ePTC; donor: PTC-005002). Circulating viruses in PTC escaped bNAb pressure but remained sensitive to autologous neutralization by other Ab populations. 2G12 was used as a reference control IgG. Inhibition of EPTC112 binding to SOSIP was moderately with 2G12 with blocking range of 28%–15%.
Molinos-Albert2023
(binding affinity)
-
2G12: This study analyzed Env sequences of early HIV-1 clonal variants from 31 individuals from the Amsterdam Cohort Studies with diverse levels of heterologous neutralization at 2-4 years post-seroconversion. A number of Env signatures coincided with neutralization development. These included a statistically shorter variable region 1 and a lower probability of glycosylation. Induction of neutralization was associated with a lower probability of glycosylation at position 332, which is involved in the epitopes of many bnAbs. 2G12 and PGT126 were tested for their ability to block infectivity by patient viruses with predicted glycosylation at N332; the NLS glycosylation motif was associated with resistance to these mAbs more often than the NIS glycosylation motif. Sequence Harmony software identified amino acid changes associated with the development of heterologous neutralization. These residues mapped to various Env subdomains, but in particular to the first and fourth variable region, as well as the underlying α2 helix of the third constant region. These findings imply that the development of heterologous neutralization might depend on specific characteristics of early Env. Env signatures that correlate with the induction of neutralization might be relevant for the design of effective HIV-1 vaccines. Primary virus isolates from 21 of the patients were assayed for neutralization by 11 well-known nAbs (b12, VRC01, 447-52D, 2G12, PGT121, PGT126, PG9, PG16, PGT145, 2F5, 4E10).
vandenKerkhof2013
(glycosylation, neutralization, vaccine antigen design, polyclonal antibodies)
-
2G12: The polyclonal response of human subjects VC20013 and VC10014 demonstrated increasing neutralization breadth against a panel of HIV-1 isolates over time. Full-length functional env genes were cloned longitudinally from these subjects from months after infection through 2.6 to 5.8 years of infection. Motifs associated with the development of breadth in published, cross-sectional studies were found in the viral sequences of both subjects. To test the immunogenicity of envelope vaccines derived from time points obtained during and after broadening of neutralization activity within these subjects, rabbits were coimmunized 4 times with selected multiple gp160 DNAs and gp140-trimeric envelope proteins. In an assay of rabbit polyclonal responses, the most rapid and persistent neutralization of multiclade tier 1 viruses was elicited by envelopes that were circulating in plasma at time points prior to the development of 50% neutralization breadth in both human subjects. The breadth elicited in rabbits was not improved by exposure to later envelope variants. Env immunogen sequences were tested for binding to a panel of well studied mAbs of various binding types (VRC01, HJ16, b12, b6, PG9, PGT121, 2G12, 2F5, F240); all gp140s bound to weak or non-neutralizing antibodies b6 and F240. MAb b6 also bound BG505 SOSIP, while F240 did not, suggesting that cluster I gp41 epitopes, which become exposed during gp120 shedding, are more easily accessed on these trimers than on BG505-SOSIP. These data have implications for vaccine development in describing a target time point to identify optimal env immunogens.
Malherbe2014
(vaccine antigen design, vaccine-induced immune responses, binding affinity, polyclonal antibodies)
-
2G12: This study explored the basis of the neutralization resistance of tier 3 virus 253-11 (subtype CRF02_AG). Virus 253-11 was resistant to neutralization by 17b, b12, VRC03, F105, SCD4, CH12, Z13e1, PG16, PGT145, 2G12, PGT121, PGT126, PGT128, PGT130, 39F, F240, and 35O22; the virus was sensitive to 3BNC117, NIH45-46G54W, VRC01, 10E8, 2F5, 4E10, PG9, VRC26.26, 10-1074, and PGT151. Virus 253-11 was strikingly resistant to most tested antibodies that target V3/glycans, despite possessing key potential N-linked glycosylation sites, especially N301 and N332, needed for the recognition of this class of antibodies. The resistance of 253-11 was not associated with an unusually long V1/V2 loop, nor with polymorphisms in the V3 loop and N-linked glycosylation sites. The 253-11 MPER was rarely recognized by sera, but was more often recognized in a chimera consisting of a HIV-2 backbone with the 253-11 MPER, suggesting steric or kinetic hindrance of the MPER. Mutations in the 253-11 MPER previously reported to increase the lifetime of the prefusion Env conformation (Y681H, L669S), decreased the resistance of 253-11 to several mAbs, presumably destabilizing its otherwise stable, closed trimer structure. A crystal structure of a recombinant 253-11 SOSIP trimer revealed that the heptad repeat helices in gp41 are drawn in close proximity to the trimer axis and that gp120 protomers also showed a relatively compact form around the trimer axis.
Moyo2018
(neutralization, structure)
-
2G12: This study used directed evolution to overcome the instability and heterogeneity of a primary Env isolate (ADA) in order to design better immunogens. HIV-1 virions were subjected to iterative cycles of destabilization and replication to select for Envs with enhanced stability. Several mutations in Env were associated with increased trimer stability, primarily in the heptad repeat regions of gp41 and V1 of gp120. Mutations from the most stable Envs were combined into a variant Env, termed "comb-mut", with superior homogeneity and stability. Comb-mut had greater binding affinity for PGT128, PG9, PG16, 2G12, VRC01, b12, and CD4-IgG2, but decreased binding to 4E10, 2F5, b6, 19b, 17b, 7B2, and D50. Comb-mut was more sensitive to neutralization by PG9. One specific mutation (K574) was shown to decrease the neutralization IC50 of mAbs b12, 2F5, 4E10, b6, 2G12, 8K8 and inhibitors sCD4, T-20, and PF-68742. Several of the Env substitutions were shown to stabilize Env spikes from HIV-1 clades A, B, and C. Spike stabilizing mutations may be useful in the development of Env immunogens that stably retain native, trimeric structure.
Leaman2013
(mimics, neutralization, vaccine antigen design, binding affinity)
-
2G12: Persistent (VP-1) and Non-persistent (VP-2) viruses were compared in a longitudinal study of a cross-reactive neutralizing serum-possessing patient, Patient B (H19554) over 9 years. Persisting VP-1 viral clones had more mutations in variable loops V1V2 and constant region C3 of Env, particularly in the number of PNGS (potential N-linked glycosylation sites) in V1V2. While VP-1 in vitro virus chimeras showed slower replication kinetics than VP-2, there was no neutralization sensitivity change based on whether they were R5 or X4 variants. The gp160 Env was longer in the VP-2 population; but both VP-1 and VP-2 chimeras were resistant to bnAb 2G12.
vanGils2011a
(glycosylation, mutation acquisition, escape)
-
2G12: Native, well-ordered, soluble mimetics of the Env trimer from subtypes B (JRFL) and C (16055) were obtained from genetically identical samples of heterogeneous mixture of disordered Env SOSIPs. Negative selection by non-nAbs was used to remove disordered oligomers, leaving well-ordered trimers that were able to bind sCD4, a panel of bnAbs that bind CD4bs, and PGT15 which is a bnAb that binds only cleavage-dependent, well-ordered, Env trimer. Several biophysical techniques were used to interrogate the structure of the purified subtype B and C trimers. Trimer antigenicity was assessed by bio-layer interferometry against F105-like non-neutralizing Abs, and some bnAbs in solution. Glycan-targeting (around N332) Ab 2G12 recognizes both the subtype B JRFL trimers as well as subtype C 16055 trimers that lack N-linked glycan at N332 but the off-rate is faster; and 2G12 cannot neutralize subtype C trimers.
Guenaga2015
(vaccine antigen design, subtype comparisons, structure)
-
2G12: This paper describes the development and characterization of soluble, cleaved SOSIP gp140 Env trimers using a JR-FL background. In addition to a stabilizing disulfide bond, mediated by engineered mutations A501C and T605C that are also present in SOS gp140 proteins, SOSIP gp140 proteins have an I559P mutation (aka “IP”) that increases trimer stability. Further analyses suggested that I559P destabilizes the N-terminal helix necessary for the six-helix bundle structure in the postfusion conformation. Immunoprecipitation assays with mAbs CD4-IgG2, b12 (aka IgG1b12), 17b, 2F5, 2.2B and 4D4 demonstrated that I559P did not alter expected structural epitopes when compared to SOS gp140 proteins. Neutralizing mAb 2G12 was able to bind efficiently to its mannose-dependent gp120 epitope on both SOS and SOSIP gp140 proteins.
Sanders2002a
(vaccine antigen design)
-
2G12: The study characterized viral evolution and changes in neutralizing activity and sensitivity of a long-term non-progressing patient (GX2016EU01) with HIV-1 CRF07_BC infection. Four plasma samples were derived from the patient between 2016 and 2020, and 59 full-length env gene fragments were obtained, revealing that potential N-linked glycosylation sites in V1 and V5 significantly increased over time. While 24 Env-pseudotyped viruses from the patient remained sensitive to autologous plasma, all were resistant to bNAbs 2G12, PGT121, and PGT135. The pseudoviruses were sensitive to 10E8, VRC01, and 12A21, but became more resistant to these bnAbs and to autologous plasma at later timepoints. The neutralization breadth of plasma from all 4 sequential samples was 100% against the global HIV-1 reference panel. Immune escape mutants resulted in increased resistance to bNAbs targeting different epitopes. The study identified known mutations F277W in gp41 and previously uncharacterized mutation S465T in V5 which may be associated with increased viral resistance to bNAbs.
Wang2022
(autologous responses, glycosylation, mutation acquisition, neutralization, escape, rate of progression, polyclonal antibodies)
-
2G12: This study examined whether HIV-1-specific bnAbs are capable of cross-neutralizing simian immunodeficiency viruses (SIVs) from chimpanzees (n=11) or western gorillas (n=1). BnAbs directed against the epitopes at the CD4 binding site (VRC01, VRC03, VRC-PG04, VRC-CH03, VRC-CH31, F105, b13, NIH45-46G54W, 45-46m2, 45-46m7), V3 (10-1074, PGT121, PGT128, PGT135, and 2G12), and gp41-gp120 interface (8ANC195, 35O22, PGT151, PGT152, PGT158) failed to neutralize SIVcpz and SIVgor strains. V2-directed bNabs (PG9, PG16, PGT145) as well as llama-derived heavy-chain only antibodies recognizing the CD4 binding site or gp41 epitopes (JM4, J3, 3E3, 2E7, 11F1F, Bi-2H10) were either completely inactive or neutralized only a fraction of SIVcpz strains. In contrast, neutralization of SIVcpz and SIVgor strains was achieved with low-nanomolar potency by one antibody targeting the MPER region of gp41 (10E8), as well as functional CD4 and CCR5 receptor mimetics (eCD4-Ig, eCD4-Igmim2, CD4-218.3-E51, CD4-218.3-E51-mim2), mono- and bispecific anti-human CD4 mAbs (iMab, PG9-iMab, PG16-iMab, LM52, LM52-PGT128), and CCR5 receptor mAbs (PRO140, PRO140-10E8). Importantly, the latter antibodies blocked virus entry not only in TZM-bl cells but also in Cf2Th cells expressing chimpanzee CD4 and CCR5, and neutralized SIVcpz in chimpanzee CD4+ T cells. These findings provide new insight into the protective capacity of anti-HIV-1 bnAbs and identify candidates for further development to combat SIV infection.
Barbian2015
(neutralization, SIV, binding affinity)
-
2G12: A recombinant native-like Env SOSIP trimer, AMC009, was developed based on viral founder sequences of elite neutralizer H18877. The subtype B AMC009 Env was defined as a Tier 2 virus based on a neutralization assay against well known nAbs (VRC01, 3BNC117, CH31, CH01, PG9, PG16, PGDM1400, 10-1074, PGT128, PGT121, PGT151, VRC34.01, 2G12, 2F5, 4E10, DH511.2.K3_4, 10E8, and the mAb mixture CH01-31).The AMC009 SOSIP protein formed stable native-like trimers that displayed multiple bnAb epitopes. Its overall structure was similar to that of BG505 SOSIP.664, and it resembled one from another elite neutralizer, AMC011, in having a dense and complete glycan shield. When tested as immunogens in rabbits, AMC009 trimers did not induce autologous neutralizing antibody responses efficiently, while the AMC011 trimers did so very weakly, outcomes that may reflect the completeness of their glycan shields. The AMC011 trimer induced antibodies that occasionally cross-neutralized heterologous tier 2 viruses, sometimes at high titer. Cross-neutralizing antibodies were more frequently elicited by a trivalent combination of AMC008, AMC009, and AMC011 trimers, all derived from subtype B viruses. Each of these three individual trimers could deplete the nAb activity from rabbit sera. Mapping the polyclonal sera by electron microscopy revealed that antibodies of multiple specificities could bind to sites on both autologous and heterologous trimers.
Schorcht2020
(neutralization, vaccine-induced immune responses, structure)
-
2G12: The study assessed the breadths and potencies of 14 bnAbs against 36 viruses reactivated from peripheral blood CD4+ T cells from ARV-treated HIV-infected individuals by using paired neutralization and infected cell binding assays. Infected cell binding correlated with virus neutralization for 10 of 14 antibodies (VRC01, VRC07-523, 3BNC117, N6, PGT121, 10-1074, PGDM1400, PG9, 10E8, and 10E8v4-V5R-100cF). For example, the correlation for 3BNC117 had r=0.82 and P<0.0001. Heterogeneity was observed, however, with a lack of significant correlation for 2G12, CAP256.VRC26.25, 2F5, and 4E10. The study also performed paired infected cell binding and ADCC assays by using two reservoir virus isolates in combination with 9 bNAbs, and the results were consistent with previous studies indicating that infected cell binding is moderately predictive of ADCC activity for bNAbs with matched Fc domains. These data provide guidance on the selection of antibodies for clinical trials.
Ren2018
(effector function, neutralization, binding affinity, HIV reservoir/latency/provirus)
-
2G12: 3 clonally-related autologously-neutralizing mAbs (43A, 43A1, and 43A2), isolated from rabbit 5743 which was co-immunized with BG505- and B41-based SOSIP soluble trimers [Klasse2016, PMID: 27627672], bind to an immunodominant epitope in V1 overlapping the bnAb N332 glycan supersite without interacting with glycans. In a BG505 SOSIP.664 binding assay, mAbs 43A, 43A1, and 43A2, individually at 2-50 μg/ml concentrations, competed at various levels with mAb 2G12 with 30-35%, 58-62% and 57-67% residual binding, respectively.
Nogal2020
(antibody interactions)
-
2G12: The authors review Fc effector functions, which cooperatively with Fab neutralization functions, could be used passively as immunotherapeutic or immunoprophylactic agents of HIV reservoir control or even infection prevention. One effector function, antibody-dependent complement-mediated lysis (ADCML), is seen with IgG1 and IgG3 anti-V1/V2 glycan bnAbs, PG9, PG16, PGT145; but not with 2F5, 4E10, 2G12, VRC01 and 3BNC117 unless they are delivered with anti-regulators of complement activation (RCA) antibodies. Another effector function, antibody-dependent cellular cytotoxicity (ADCC) can slow disease progression by NK-mediated degranulation of infected cells that are coated by bnAbs whose Fc region is recognized by the low affinity NK receptor, FcγRIIIA (or CD16). Strong ADCC was induced by NIH45-46, 3BNC117, 10-1074, PGT121 and 10E8, with intermediate activity for PG16 and VRC01, but no ADCC activation for 12A12, 8ANC195 and 4E10. A final effector function, antibody-dependent phagocytosis (ADP) also eliminates infected cells but through phagocytosis mediated by Fc portions of coating anti-HIV antibodies interacting with other FcγR (or FcαR) on the surface of granulocytes, monocytes or macrophages. This protective mode is less well studied but bnAbs like VRC01 have been engineered to increase phagocytosis by neutrophils. Protein engineering of bispecifics against the surface of infected or reservoir virus cells has potential in the future.
Danesh2020
(antibody interactions, assay or method development, complement, effector function, immunoprophylaxis, neutralization, immunotherapy, early treatment, review, broad neutralizer, HIV reservoir/latency/provirus)
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2G12: Env clones were obtained from donor CBJC515 plasma. The neutralization of these clones was tested against 3 donor serum samples (2005, 2006, 2008) and 6 bnAbs (10E8, 2G12, PGT121, PGT135, VRC01, 12A21). In phylogeny, the sequences clustered into 2 major clusters. Cluster I viruses vanished in 2006 and then appeared as recombinants in 2008. In Cluster II viruses, the V1 length and N-glycosylation sites increased over the four years of the study period. Most viruses were sensitive to concurrent and subsequent autologous plasma, and to bNAbs 10E8, PGT121, VRC01, and 12A21, but all viruses were resistant to PGT135. Overall, 90% of Cluster I viruses were resistant to 2G12, while 94% of Cluster II viruses were sensitive to 2G12. The study confirmed that HIV-1 continued to evolve even in the presence of bnAbs, and two virus clusters in this donor adopted different escape mechanisms under the same humoral immune pressure.
Hu2021
(autologous responses, glycosylation, neutralization, escape, polyclonal antibodies)
-
2G12: HIV-1 env genes were sequenced from 16 mother/infant transmitting pairs. Infant transmitted-founder (T/F) and representative maternal non-transmitted Env variants were identified and used to generate pseudoviruses for paired maternal plasma neutralization analysis. Eighteen out of 21 (85%) infant T/F Env pseudoviruses were neutralization resistant to paired maternal plasma, while all infant T/F viruses were neutralization sensitive to a panel of HIV-1 broadly neutralizing antibodies (2G12, CH01, PG9, PG16, PGT121, PGT126, DH429, b12, VRC01, NIH45-46, CH31, 4E10, 2F5, 10E8, DH512) and variably sensitive to heterologous plasma neutralizing antibodies. Antibody mixture CH01/31 was used as a positive control for neutralization. The infant T/F pseudoviruses were overall more neutralization resistant to paired maternal plasma in comparison to pseudoviruses from maternal non-transmitted variants. These findings suggest that autologous neutralization of circulating viruses by maternal plasma antibodies select for neutralization-resistant viruses that initiate peripartum transmission, raising the speculation that enhancement of this response at the end of pregnancy could reduce infant HIV-1 infection risk.
Kumar2018
(neutralization, acute/early infection, mother-to-infant transmission, transmission pair)
-
2G12: Improvements to the standardization of the HIV-1 pseudovirus production procedure by implementing an automated system for aliquoting of HIV-1 pseudovirus stocks up to liter-scale are described. The automated platform and the aliquoting process were validated on as accuracy, precision, specificity and robustness. Lot-to-lot variations and virus stock integrity were assessed through two parallel neutralization assays run with the automatically aliquoted HIV pseudovirus and a manually aliquoted reference virus of the same type, by using five control reagents: sCD4, b12, 2F5, 4E10 and TriMab consisting of 2G12, IgG1b12 and 2F5.
Schultz2018
(assay or method development, neutralization)
-
2G12: Novel Env clones of subtypes G (n=15) and F (n=7) were produced and tested for neutralization and coreceptor usage. All 15 subtype G-enveloped pseudoviruses were resistant to neutralization by MAbs b12 and 2G12, while a majority were neutralized by 2F5 and 4E10. All 7 subtype F pseudoviruses were resistant to 2F5 and b12, 6 were resistant to 2G12, and 6 were neutralized by 4E10. Coreceptor usage testing revealed that 21 of 22 envelopes were CCR5-tropic, including all 15 subtype G envelopes, 7 of which were from patients with CD4 T cell counts <200/ml. TriMab (a mixture of b12 + 2G12 + 2F5) neutralized only four (27%) viruses, and this activity correlated with that of the 2F5 component. These results confirm the broadly neutralizing activity of 4E10 on envelope clones across all tested group M clades, including subtypes G and F, reveal the resistance of most subtype F pseudoviruses to broadly neutralizing MAbs b12, 2G12, and 2F5, and suggest that, similarly to subtype C, CXCR4 tropism is uncommon in subtype G, even at advanced stages of infection.
Revilla2011
(neutralization, subtype comparisons)
-
2G12: Since cross-reactive antibodies can interfere in immunoassays, HIV-1 mAbs were tested for binding to the SARS-COV-2 spike (S) protein (SARS-COV-2 S cross-reactivity). The following 9 gp120-epitope binding HIV-1 mAbs are cross-reactive with COV-2 S: 2G12, PGT121, PGT126, PGT128, PGT145, PG9, PG16, 10-1074, and 35O22. CD4bs Abs VRC01 and VRC03 are not cross-reactive. Cross-reactivity of the 9 HIV-1 Abs was through glycoepitopes. Glycan-dependent, V3-loop-binding PGT126 and PGT128 as well as 2G12 were the strongest binders of COV-2 S and were found to be immunoreactive but incapable of neutralization or antibody-dependent enhancement (ADE).
Mannar2021
(antibody interactions, effector function, glycosylation, computational prediction, antibody polyreactivity)
-
2G12: IgA and IgG bNAbs of 3 distinct B cell lineages were characterized in a viremic controller (pt7). Two lineages comprised only IgG+ or IgA+ blood memory B cells; the third combined both IgG and IgA clonal variants. BNAb 7-269 in the IgA-only lineage displayed the highest neutralizing capacity despite limited somatic mutation. Immunotherapy with 7-269 in humanized mice delayed viral rebound. AD8-infected cell killing by primary human natural killer (NK) cells via ADCC was observed with all pt7 bNAbs binding strongly to target cells and expressed as IgGs, except for 7-155. BNAbs in all three lineages targeted the N332 glycan supersite. Epitope mapping showed that all pt7 IgA and IgG bNAbs target the high-mannose patch centered on the N332 glycan without interacting with the V3 loop base, which contrasts with numerous bNAbs targeting the N332 supersite. The cryo-EM structure of 7-269 in complex with BG505 SOSIP revealed an epitope mainly composed of sugar residues comprising the N332 and N295 glycans; onto which 7-269 positions itself in a structurally similar way to 2G12. Binding and cryo-EM structural analyses showed that antibodies from the two other lineages interact mostly with glycans N332 and N386. Hence, multiple B cell lineages of IgG and IgA bNAbs focused on a unique HIV-1 site of vulnerability can codevelop in HIV-1 viremic controllers. Other antibodies used as controls included 10-188, 3BNC117, PGT121, PGT135, 10-1074, BG8, BG18, and SF12.
Lorin2022
(antibody binding site, structure)
-
2G12: Analyses of all PDB HIV1-Env trimer (prefusion, closed) structures fulfilling certain parameters of resolution were performed to classify them on the basis of (a) antibody class which was informed by parental B cells as well as structural recognition, and (b) Env residues defining recognized HIV epitopes. Structural features of the 206 HIV epitope and bNAb paratopes were correlated with functional properties of the breadth and potency of neutralization against a 208-strain panel. Broadly nAbs with >25% breadth of neutralization belonged to 20 classes of antibodies with a large number of protruding loops and high degree of somatic hypermutation (SHM). Analysis of recognized HIV epitopes placed the bNAbs into 6 categories (viz. V1V2, glycan-V3, CD4-binding site, silent face center, fusion peptide and subunit interface). The epitopes contained high numbers of independent sequence segments and glycosylated surface area. 2G12-Env formed a distinct group within the Glycan-V3 category, Class 2G12 due to its unique VH domain structure. Data for 2G12 complexed to BG505 DS-SOSIP trimer and VRC03 as a cryo-EM electron-density map was solved and deposited as EMD-8981. 2G12 epitope residues on Env were defined as residue 411 and glycans N295, N332, N339, and N392 from the cryo-EM reconstruction.
Chuang2019
(antibody binding site, antibody interactions, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)
-
2G12: Rabbits were immunized with a DNA vaccine encoding JR-CSF gp120. Five sera with potent autologous neutralizing activity were selected and compared with a human neutralizing plasma (Z23) and monoclonal antibodies targeting various regions of gp120 (VRC01, b12, b6, F425, 2F5, 2G12, and X5). The rabbit sera contained different neutralizing activities dependent on C3 and V5, C3 and V4, or V4 regions of the glycan-rich outer domain of gp120. All sera showed enhanced neutralizing activity toward an Env variant that lacked a glycosylation site in V4. The JR-CSF gp120 epitopes recognized by the sera were distinct from those of the mAbs. The activity of one serum required specific glycans that are also important for 2G12 neutralization, and this serum blocked the binding of 2G12 to gp120. The findings show that different fine specificities can achieve potent neutralization of HIV-1, yet this strong activity does not result in improved breadth.
Narayan2013
(neutralization, polyclonal antibodies)
-
2G12: The study compared well-characterized nAbs (2G12, b12, VRC01, 10E8, 17b) with 4 mAbs derived from a Japanese patient (4E9C, 49G2, 916B2, 917B11) in their neutralization and ADCC activity against viruses of subtypes B and CRF01. CRF01 viruses were less susceptible to neutralization by 2G12 and b12, while VRC01 was highly effective in neutralizing CRF01 viruses. 49G2 showed better neutralization breadth against CRF01 than against B viruses. CRF01_AE viruses from Japan also showed a slightly higher susceptibility to anti-CD4i Ab 4E9C than the subtype B viruses, and to CRF01_AE viruses from Vietnam. Neutralization breadth of other anti-CD4i Abs 17b, 916B2 and 917B11 was low against both subtype B and CRF01_AE viruses. Anti-CD4bs Ab 49G2, which neutralized only 22% of the viruses, showed the broadest coverage of Fc-mediated signaling activity against the same panel of Env clones among the Abs tested. The CRF01_AE viruses from Japan were more susceptible to 49G2-mediated neutralization than the CRF01_AE viruses from Vietnam, but Fc-mediated signaling activity of 49G2was broader and stronger in the CRF01_AE viruses from Vietnam than the CRF01_AE viruses from Japan.
Thida2019
(effector function, neutralization, subtype comparisons)
-
2G12: The Chinese HIV Reference Laboratory produced 124 pseudoviruses from patients with subtype B, BC, and CRF01 infections. These viruses were assigned to tiers based on their neutralization by a panel of patient sera. Their neutralization sensitivities were also measured against a panel of well-characterized mAbs (2F5, b12, 2G12, 4E10, 10E8, VRC01, VRC-CH31, CH01, PG9, PG16, PGT121, PGT126).
Nie2020
(assay or method development, neutralization)
-
2G12: Novel Env pseudoviruses were derived from 22 patients in China infected with subtype CRF01_AE viruses. Neutralization IC50 was determined for 11 bNAbs: VRC01, NIH45-46G54W, 3BNC117, PG9, PG16, 2G12, PGT121, 10-1074, 2F5, 4E10, and 10E8. The CRF01_AE pseudoviruses exhibited different susceptibility to these bNAbs. Overall, 4E10, 10E8, and 3BNC117 neutralized all 22 env-pseudotyped viruses, followed by NIH45-46G54W and VRC01, which neutralized more than 90% of the viruses. 2F5, PG9, and PG16 showed only moderate breadth, while the other three bNAbs neutralized none of these pseudoviruses. Specifically, 10E8, NIH45-46G54Wand 3BNC117 showed the highest efficiency, combining neutralization potency and breadth. Mutations at position 160, 169, 171 were associated with resistance to PG9 and PG16, while loss of a potential glycan at position 332 conferred insensitivity to V3-glycan-targeting bNAbs. These results may help in choosing bNAbs that can be used preferentially for prophylactic or therapeutic approaches in China.
Wang2018a
(assay or method development, neutralization, subtype comparisons)
-
2G12: The authors selected an optimal panel of diverse HIV-1 envelope glycoproteins to represent the antigenic diversity of HIV globally in order to be used as antigen candidates. The selection was based on genetic and geographic diversity, and experimentally and computationally evaluated humoral responses. The eligibility of the envelopes as vaccine candidates was evaluated against a panel of antibodies for breadth, affinity, binding and durability of vaccine-elicited responses. The antigen panel was capable of detecting the spectrum of V2-specific antibodies that target epitopes from the V2 strand C (V2p), the integrin binding motif in V2 (V2i), and the quaternary epitope at the apex of the trimer (V2q).
Yates2018
(vaccine antigen design, vaccine-induced immune responses, binding affinity)
-
2G12: Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized. Cross-linking/mass spectrometry to evaluate the conformations of functional membrane Env and sgp140 SOSIP.664 has been reported. Differences were detected in the gp120 trimer association domain and C terminus and in the gp41 HR1 region which can guide the improvement of Env glycoprotein preparations and potentially increase their effectiveness as a vaccine. 2G12 broadly neutralized HIV-1AD8 full-length and cytoplasmic tail-deleted Envs.
Castillo-Menendez2019
(vaccine antigen design, structure)
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2G12: HIV Env glycoproteins were expressed by incorporation into live attenuated rubella viral vectors strain RA27/3. These vectors can stably express Env core derived glycoproteins ranging in size up to 363 amino acids from HIV clade C strain 426c. By themselves, the vectors elicited modest Ab titers to the Env insert. But the combination of rubella/env prime followed by a homologous protein boost gave a strong response. Cell lysates infected with different rubella/env vectors were immunoprecipitated with 2G12, which binds total Env protein, regardless of native folding.
Virnik2018
(vaccine antigen design)
-
2G12: Two conserved tyrosine (Y) residues within the V2 loop of gp120, Y173 and Y177, were mutated individually or in combination, to either phenylalanine (F) or alanine (A) in several strains of diverse subtypes. In general, these mutations increased neutralization sensitivity, with a greater impact of Y177 over Y173 single mutations, of double over single mutations, and of A over F substitutions. The Y173A Y177A double mutation in HIV-1 BaL increased sensitivity to most of the weakly neutralizing MAbs tested (2158, 447-D, 268-D, B4e8, D19, 17b, 48d, 412d) and even rendered the virus sensitive to non-neutralizing antibodies against the CD4 binding site (F105, 654-30D, and b13). In the case of V2 mAb 697-30D, residue Y173 is part of its epitope, and thus abrogates its binding and has no effect on neutralization; the Y177A mutant alone did increase neutralization sensitivity to this mAb. When the double mutant was tested against bnAbs, there was a large decrease in neutralization sensitivity compared to WT for many bnAbs that target V1, V2, or V3 (PG9, PG16, VRC26.08, VRC38, PGT121, PGT122, PGT123, PGT126, PGT128, PGT130, PGT135, VRC24, CH103). The double mutation had lesser or no effect on neutralization by one V3 bnAb (2G12) and by most bnAbs targeting the CD4 binding site (VRC01, VRC07, VRC03, VRC-PG04, VRC-CH31, 12A12, 3BNC117, N6), the gp120-gp41 interface (35O22, PGT151), or the MPER (2F5, 4E10, 10E8).
Guzzo2018
(antibody binding site, neutralization)
-
2G12: Without SOSIP changes, cleaved Env trimers disintegrate into their gp120 and gp41-ectodomain (gp41_ECTO) components. This study demonstrates that the gp41_ECTO component is the primary source of this Env metastability and that replacing wild-type gp41_ECTO with BG505 gp41_ECTO of the uncleaved prefusion-optimized design is a general and effective strategy for trimer stabilization. A panel of 11 bNAbs, including the N332 supersite recognized by PGT121, PGT128, PGT135, and 2G12, was used to assess conserved neutralizing epitopes on the trimer surface, and the main result was that the substitution was found to significantly improve trimer binding to bNAbs VRC01, PGT151, and 35O22, with P values (paired t test) of 0.0229, 0.0269, and 0.0407, respectively.
He2018
(antibody interactions, glycosylation, vaccine antigen design)
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2G12: To reduce local V2 flexibility and improve the binding of V2-dependent bNAbs and germline precursor bNAbs, the authors designed BG505 SOSIP.664 trimer variants whose V1 and V2 domains were stabilized by introducing disulfide bonds either within the V2 loop or between the V1 and V2 loops. The resulting SOSIP trimer variants — E153C/K178C, E153C/K178C/G152E and I184C/E190C — have improved reactivity with V2 bNAbs and their inferred germline precursors and are more sensitive to neutralization by V2 bNAbs. Compared with BG505 SOSIP.664, the E153C/R178C V1-V2 disulfide mutant bound the VRC01, PGT151, and 2G12 slightly less well and the G152E compensatory mutation improved VRC01, PGT151, and 2G12 binding. However, sensitivity to antibodies 2G12 and PGT151 was not affected for either mutant virus E153C/K178C/G152E or I184C/E190C.
deTaeye2019
(neutralization, vaccine antigen design, binding affinity)
-
2G12: This study looks at the role of somatic mutations within antibody variable and framework regions (FWR) in bNAbs and how these mutations alter thermostability and neutralization as the Ab lineage reaches maturation. The emergence and selection of different mutations in the complementarity-determining and framework regions are necessary to maintain a balance between antibody function and stability. The study shows that all major classes of bNAbs (DH270, CH103, CH235, VRC01, PGT lineage etc.) have lower thermostability than their corresponding inferred UCA antibodies. Fab interdomain flexibility mutations are selected early in Ab development.
Henderson2019
(neutralization, antibody lineage, broad neutralizer)
-
2G12: Two HIV-1-infected individuals, VC10014 and VC20013, were monitored from early infection until well after they had developed broadly neutralizing activity. The bNAb activity developed about 1 year after infection and mapped to a single epitope in both subjects. Isolates from each subject, taken at five different time points, were tested against monoclonal bNAbs: VRC01, B12, 2G12, PG9, PG16, 4E10, and 2F5. In subject VC10014, the bNAb activity developed around 1 year postinfection and targeted an epitope that overlaps the CD4-BS and is similar to (but distinct from) bNAb HJ16. In the case of VC20013, the bNAb activity targeted a novel epitope in the MPER that is critically dependent on residue 677 (mutation K677N).
Sather2014
(neutralization, broad neutralizer)
-
2G12: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of nAb responses compared with Env 459C alone.
Bricault2019
(antibody binding site, neutralization, vaccine antigen design, computational prediction, broad neutralizer)
-
2G12: The influence of a V2 State 2/3-stabilizing Env mutation, L193A, on ADCC responses mediated by sera from HIV-1-infected individuals was evaluated. Conformations spontaneously sampled by the Env trimer at the surface of infected cells had a significant impact on ADCC. 2G12 was used as a conformation-independent antibody.
Prevost2018
(effector function)
-
2G12: Polyreactive properties of natural and artificially engineered HIV-1 bNAbs were studied, with almost 60% of the tested HIV-1 bNAbs (including this one) exhibiting low to high polyreactivity in different immunoassays. A previously unappreciated polyreactive binding for PGT121, PGT128, NIH45-46W, m2, and m7 was reported. Binding affinity, thermodynamic, and molecular dynamics analyses revealed that the co-emergence of enhanced neutralizing capacities and polyreactivity was due to an intrinsic conformational flexibility of the antigen-binding sites of bNAbs, allowing a better accommodation of divergent HIV-1 Env variants.
Prigent2018
(antibody polyreactivity)
-
2G12: A systems glycobiology approach was applied to reverse engineer the relationship between bNAb binding and glycan effects on Env proteins. Glycan occupancy was interrogated across every potential N-glycan site in 94 recombinant gp120 antigens. Using a Bayesian machine learning algorithm, bNAb-specific glycan footprints were identified and used to design antigens that selectively alter bNAb antigenicity. The novel synthesized antigens unsuccessfully bound to target bNAbs with enhanced and selective antigenicity.
Yu2018
(glycosylation, vaccine antigen design)
-
2G12: A panel of bnAbs were studied to assess ongoing adaptation of the HIV-1 species to the humoral immunity of the human population. Resistance to neutralization is increasing over time, but concerns only the external glycoprotein gp120, not the MPER, suggesting a high selective pressure on gp120. Almost all the identified major neutralization epitopes of gp120 are affected by this antigenic drift, suggesting that gp120 as a whole has progressively evolved in less than 3 decades.
Bouvin-Pley2014
(neutralization)
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2G12: The first cryo-EM structure of a cross-linked vaccine antigen was solved. The 4.2 Å structure of HIV-1 BG505 SOSIP soluble recombinant Env in complex with a bNAb PGV04 Fab fragment revealed how cross-linking affects key properties of the trimer. SOSIP and GLA-SOSIP trimers were compared for antigenicity by ELISA, using a large panel of mAbs previously determined to react with BG505 Env. Non-NAbs globally lost reactivity (7-fold median loss of binding), likely because of covalent stabilization of the cross-linked ‘closed’ form of the GLA-SOSIP trimer that binds non-NAbs weakly or not at all. V3-specific non-NAbs showed 2.1–3.3-fold reduced binding. Three autologous rabbit monoclonal NAbs to the N241/N289 ‘glycan-hole’ surface, showed a median ˜1.5-fold reduction in binding. V3 non-NAb 4025 showed residual binding to the GLA-SOSIP trimer. By contrast, bNAbs like 2G12 broadly retained reactivity significantly better than non-NAbs, with exception of PGT145 (3.3-5.3 fold loss of binding in ELISA and SPR).
Schiffner2018
(vaccine antigen design, binding affinity, structure)
-
2G12: This study describes the generation of CHO cell lines stably expressing the following vaccine Env Ags: CRF01_AE A244 Env gp120 protein (A244.AE) and 6240 Env gp120 protein (6240.B). The antigenic profiles of the molecules were assessed with a panel of well-characterized mAbs recognizing critical epitopes and glycosylation analysis confirming previously identified sites and revealing unknown sites at non-consensus motifs. A244.AE gp120 showed low level of binding to 2G12 in ELISA EC50 and Surface Plasmon Resonance (SPR) assays. 6240.B gp120 exhibited binding to 2G12.
Wen2018
(glycosylation, vaccine antigen design)
-
2G12: Assays of poly- and autoreactivity demonstrated that broadly neutralizing NAbs are significantly more poly- and autoreactive than non-neutralizing NAbs. 2G12 is neither autoreactive nor polyreactive.
Liu2015a
(autoantibody or autoimmunity, antibody polyreactivity)
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2G12: A panel of 14 pseudoviruses of subtype CRF01_AE was developed to assess the neutralization of several neutralizing antibodies (b12, PG9, PG16, 4E10, 10E8, 2F5, PGT121, PGT126, 2G12). Neutralization was assessed in both TZM-bl and A3R5 cell-based assays. Most viruses were more susceptible to mAb-neutralization in A3R5 than in the TZM-bl cell-based assay. The increased neutralization sensitivity observed in the A3R5 assay was not linked to the year of virus transmission or to the stages of infection, but chronic viruses from the years 1990-92 were more sensitive to neutralization than the more current viruses, in both assays.
Chenine2018
(assay or method development, neutralization, subtype comparisons)
-
2G12: The immunologic effects of mutations in the Env cytoplasmic tail (CT) that included increased surface expression were explored using a vaccinia prime/protein boost protocol in mice. After vaccinia primes, CT- modified Envs induced up to 7-fold higher gp120-specific IgG, and after gp120 protein boosts, they elicited up to 16-fold greater Tier-1 HIV-1 neutralizing antibody titers.
Hogan2018
(vaccine antigen design)
-
2G12: SOSIP.664 trimer was modified at V3 positions 306 and 308 by Leucine substitution to create hydrophobic interactions with the tryptophan residue at position 316 and the V1V2 domain. These modifications stabilized the resulting SOSIP.v5.2 S306L R308L trimers. In vivo, the induction of V3 non-NAbs was significantly reduced compared with the SOSIP.v5.2 trimers. S306L plus R308L paired substitutions had no effect on the trimer reactivity of 2G12.
deTaeye2018
(broad neutralizer)
-
2G12: Repetitive immunization of macaques over 3 years with an Env expressing V3-high mannose glycan, CON-S gp140CFI, elicited plasma antibodies neturalizing HIV-1 expressing high mannose glycans only. NAb DH501 was isolated and found to possess a structure where 3 VH chain CDRs formed a cavity into which the HIV-1 Env V3-glycan could insert. Rhesus DH501 possessed characteristics of V3-glycan bNAb precursors but its binding to M.CON-S gp140CFI was blocked 70% by 2G12.
Saunders2017
(vaccine-induced immune responses, structure)
-
2G12: Nanodiscs (discoidal lipid bilayer particles of 10-17 nm surrounded by membrane scaffold protein) were used to incorporate Env complexes for the purpose of vaccine platform generation. The Env-NDs (Env-NDs) were characterized for antigenicity and stability by non-NAbs and NAbs. Most NAb epitopes in gp41 MPER and in the gp120:gp41 interface were well exposed while non-NAb cell surface epitopes were generally masked. Anti-gp120 glycan NAb 2G12, had a Kd of 10.16 nM and bound the Env-ND well.
Witt2017
(vaccine antigen design, binding affinity)
-
2G12: DS-SOSIP.4mut (4mut) was identified as the most immunogenic and stable of 4 engineered, soluble, closed prefusion HIV-1 Env trimers. 4mut contained 4 mutations (M154, M300, M302 and L320) designed to form hydrophobic interactions between V1V1 and V3 loops. After V3-negative selection, V3-glycan-targeted mAb 2G12 recognized 4mut, the other 3 designed trimers (DS-SOSIP.6mut containing 4mut mutations, Y177W and I420M, DS-SOSIP.I423F and DS-SOSIP.A316W), and related trimers DS-SOSIP and BG505 SOSIP.664. The latter had the lowest binding affinity. Each DS-SOSIP variant was able to elicit trimer-specific responses ,comparable to BG505 SOSIP.664, in guinea pigs after 4 immunizations, but none elicited heterologous neutralizing activity. Crystal structures were generated for 4mut and 6mut.
Chuang2017
(vaccine antigen design, vaccine-induced immune responses)
-
2G12: Three strategies were applied to perturb the structure of Env in order to make the protein more susceptible to neutralization: exposure to cold, Env-activating ligands, and a chaotropic agent. A panel of mAbs (E51, 48d, 17b, 3BNC176, 19b, 447-52D, 39F, b12, b6, PG16, PGT145, PGT126, 35O22, F240, 10E8, 7b2, 2G12) was used to test the neutralization resistance of a panel of subtype B and C pseudoviruses with and without these agents. Both cold and CD4 mimicking agents (CD4Ms) increased the sensitivity of some viruses. The chaotropic agent urea had little effect by itself, but could enhance the effects of cold or CD4Ms. Thus Env destabilizing agents can make Env more susceptible to neutralization and may hold promise as priming vaccine antigens.
Johnson2017
(vaccine antigen design)
-
2G12: Man9-V3, a synthetic minimal immunogen designed to reflect the HIV-1 native Env V3-glycan bNAb epitope, binds memory B cells and V3-glycan bNAbs as well as germline bNAbs. Man9-V3 was used to isolate a bNAb from an HIV-1+ subject and also induce V3-glycan-targeting antibodies in rhesus macaques. Using the crystal structure of PGT128-gp120 Env OD (outer domain), Man9-V3 glycopeptide was synthesized based on Clade B JRFL with deletion of residues 305-320, retention of P321 and stabilization of disulfide bridge C296-C331. High mannose-glycans presented on Man9-V3 were appropriately spaced for binding to 2G12.
Alam2017
(antibody binding site)
-
2G12: Env from of a highly neutralization-resistant isolate, CH120.6, was shown to be very stable and conformationally-homogeneous. Its gp140 trimer retains many antigenic properties of the intact Env, while its monomeric gp120 exposes more epitopes. Thus trimer organization and stability are important determinants for occluding epitopes and conferring resistance to antibodies. Among a panel of 21 mAbs, CH120.6 was resistant to neutralization by all non-neutralizing and strain-specific mAbs, regardless of the location of their epitopes. It was weakly neutralized by several broadly-neutralizing mAbs (VRC01, NIH45-46, 12A12, PG9, PG16, PGT128, 4E10, and 10E8), and well neutralized by only 2 (PGT145 and 10-1074).
Cai2017
(neutralization)
-
2G12: Mice twice-primed with DNA plasmids encoding HIV-1 gp120 and gag and given a double boost with HIV-1 virus-like particles (VLPs) i.e. DDVV immunization, elicited Env-specific antibody responses as well as Env- and Gag-specific CTL responses. In vivo electroporation (EP) was used to increase breadth and potency of response. Human anti-gp120 2G12 was used to prove that the VLP spike included the broad neutralization epitope recognized by it.
Huang2017a
(therapeutic vaccine, variant cross-reactivity)
-
2G12: A panel of mAbs (2G12, VRC01, HJ16, 2F5, 4E10, 35O22, PG9, PGT121, PGT126, 10-1074) was tested to compare their efficacy in cell-free versus cell-cell transmission. Almost all bNAbs (with the exception of anti-CD4 mAb Leu3a) blocked cell-free infection with greater potency than cell-cell infection, and showed greater potency in neutralization of cell-free viruses. The lower effectiveness on neutralization was particularly pronounced for transmitted/founder viruses, and less pronounced for chronic and lab-adapted viruses. The study highlights that the ability of an antibody to inhibit cell-cell transmission may be an important consideration in the development of Abs for prophylaxis.
Li2017
(immunoprophylaxis, neutralization)
-
2G12: Compared to patient-derived mAbs, vaccine-elicited mAbs are often less able to neutralize the virus, due to a less-effective angle of approach to the Env spike. This study engineered an immunogen consisting of the gp120 core in complex with a CD4bs mAb, 17b. Rabbits immunized with this antigen displayed earlier affinity maturation and better virus neutralization compared to those immunized with the gp120 core alone. VRC01 and 2G12 bound to the the 17b-gp120 complex more avidly than to the gp120 core alone.
Chen2016b
(antibody binding site, vaccine antigen design, vaccine-induced immune responses, structure)
-
2G12: The amino acid at gp120 position 375 is embedded in the Phe43 cavity, which affects susceptibility to ADCC. Most M-group strains of HIV-1 have serine at position 375, but CRF01 typically has histidine, which is a bulky residue. MAbs 2G12 and 10E8 were not affected by changes in residue 375, while recognition by CD4i mAbs 17b and A32 was increased by mutations of residue 375 to histidine or tryptophan. Participants in the AIDSVAX vaccine trial were infected by CRF01, and a significant part of the efficacy of this vaccine rested on ADCC responses. The ADCC response of MAbs derived from AIDSVAX participants (CH29, CH38, CH40, CH51, CH52, CH54, CH77, CH80, CH81, CH89, CH91, CH94) was dependent on the presence of 375H and greatly decreased by the presence of 375S.
Prevost2017
(effector function, vaccine-induced immune responses)
-
2G12: This review focuses on the potential role of HIV-1-specific NAbs in preventing HIV-1 infection. Several NAbs have provided protection from infection in SHIV challenge studies in primates: b12, VRC01, VRC07-523LS, 3BNC117, PG9, PGT121, PGT126, 10-1074, 2G12, 4E10, 2F5, 10E8.
Pegu2017
(immunoprophylaxis, review)
-
2G12: Prevalence, breadth, and potency of NAb responses in 98 CRF07_BC-infected individuals using a multi-subtype panel of 30 tier 2-3 Env-pseudotyped viruses were identified and the neutralization pattern of CRF07_BC-infected people was compared with that of subtype B'-infected individuals in China. 18% of 98 plasma samples neutralized >80% of viruses, and 53% neutralized >50%, suggesting the presence of broadly NAbs. CRF07_BC-infected individuals generated higher but less broad neutralization titers against intra-subtype viruses than subtype B'-infected individuals with longer infection length, indicating the transition from narrow autologous to broad heterologous neutralization over time. Neutralization activity of the top six plasmas from each cohort was attributable to the IgG fraction, and half of them developed CD4 binding site antibody reactivity. VRC01 and 2G12 were used as controls.
Hu2017
(broad neutralizer)
-
2G12: This study investigated Ab binding abilities of saccharide ligands and the effects of the inner water molecules of ligand–Ab complexes. 2G12 complexes with saccharide ligands were studied by modeling to estimate how inner water molecules of the protein affect the dynamics of the complexes as well as the ligand–Ab interaction. This indicates that D -fructose’s strong affinity to the Ab was partly due to the good retentiveness of solvent water molecules of the ligand and its stability of the ligand’s conformation and relative position in the active site.
Ueno-Noto2016
(antibody binding site, antibody interactions)
-
2G12: The results confirm that Nef and Vpu protect HIV-1-infected cells from ADCC, but also show that not all classes of antibody can mediate ADCC. Anti-cluster-A antibodies are able to mediate potent ADCC responses, whereas anti-coreceptor binding site antibodies are not. Position 69 in gp120 is important for antibody-mediated cellular toxicity by anti-cluster-A antibodies. The angle of approach of a given class of antibodies could impact its capacity to mediate ADCC. MAb 2G12 was used as a CD4-independent outer-domain-recognizing antibody to show that more Env is present on the cell surface in cells infected with Vpu-deleted HIV.
Ding2015
(effector function)
-
2G12: The ability of neutralizing and nonneutralizing mAbs to block infection in models of mucosal transmission was tested. Neutralization potency did not fully predict activity in mucosal tissue. CD4bs-specific bNAbs, in particular VRC01, blocked HIV-1 infection across all cellular and tissue models. MPER (2F5) and outer domain glycan (2G12) bNAbs were also efficient in preventing infection of mucosal tissues, while bNAbs targeting V1-V2 glycans (PG9 and PG16) were more variable. Non-nAbs alone and in combinations, were poorly protective against mucosal infection. The protection provided by specific bNAbs demonstrates their potential over that of nonneutralizing antibodies for preventing mucosal entry. 2G12 was selected to represent mAbs of the outer domain glycan class.
Cheeseman2017
(genital and mucosal immunity, immunoprophylaxis)
-
2G12: This study investigated the ability of native, membrane-expressed JR-FL Env trimers to elicit NAbs. Rabbits were immunized with virus-like particles (VLPs) expressing trimers (trimer VLP sera) and DNA expressing native Env trimer, followed by a protein boost (DNA trimer sera). N197 glycan- and residue 230- removal conferred sensitivity to Trimer VLP sera and DNA trimer sera respectively, showing for the first time that strain-specific holes in the "glycan fence" can allow the development of tier 2 NAbs to native spikes. All 3 sera neutralized via quaternary epitopes and exploited natural gaps in the glycan defenses of the second conserved region of JR-FL gp120. Fig S7 showed that gp120 monomer and gp140F trimer both interfered with mAb 2G12 neutralization, but 2G12 was unable to inhibit CD4bs NAb binding.
Crooks2015
(glycosylation, neutralization)
-
2G12: Nedd8 activation enzyme inhibitor, MLN4924, partially blocks Vpu activity through CD4 downregulation. Host antiviral factor BST2, however, is not inhibited and so reversal of Vpu activity is partial, exposing CD4-induced eptiopes that recruit ADCC-mediated host defense. Ab 2G12 which recognizes a CD4-independent epitope was used to show that even under best conditions, MLN4924 only minimally increases the binding of 2G12 to Env.
Tokarev2015
(effector function)
-
2G12: New antibodies were isolated from 3 patients: Donor 14 (PDGM11, PGDM12, PGDM13, PGDM14), Donor 82 (PGDM21), and Donor 26 (PGDM31). These bnAbs bound both the GDIR peptide (Env 324-327) and the high-mannose patch glycans, enabling broad reactivity. N332 glycan was absolutely required for neutralization, while N301 glycan modestly affected neutralization. Removing N156 and N301 glycans together while retaining N332 glycan abrogated neutralization for PGDM12 and PGDM21. Neutralization by PGDM11-14 bnAbs depended on R327A and H330A substitutions and neutralization by PGDM21 depended on D325A and H330A substitutions. G324A mutation resulted in slight loss of neutralization for both antibody families. In comparison, 2G12 and PGT135 did not show any dependence on residues in the 324GDIR327 region for neutralization activity, although PGT135 did show dependence on H330.
Sok2016
(antibody binding site, glycosylation)
-
2G12: Env residue N197 on the BG505-SOSIP trimer was mutated to test the effect of its glycosylation on the binding kinetics of CD4BS and other mAbs. Removal of the glycan had little effect on the overall structure of the molecule. Its removal resulted in increased binding of CD4 and CD4BS antibodies (VRC01, VRC03, V3-3074), but little effect on bNAbs targeting other epitopes (PG9, PG16, PGT145, 17b, A32, 2G12, PGT121, PGT126). Two CD4BS-binding antibodies tested (b12, F105) had insufficient breadth to bind the BG505-SOSIP trimer. Removal of the N197 glycan may allow for the development of better SOSIP immunogens, particularly to elicit CD4BS-specific Abs.
Liang2016
(glycosylation, vaccine antigen design)
-
2G12: This study produced Env SOSIP trimers for clades A (strain BG505), B (strain JR-FL), and G (strain X1193). Based on simulations, the MAb-trimer structures of all MAbs tested needed to accommodate at least one glycan, including both antibodies known to require specific glycans (PG9, PGT121, PGT135, 8ANC195, 35O22) and those that bind the CD4-binding site (b12, CH103, HJ16, VRC01, VRC13). A subset of monoclonal antibodies bound to glycan arrays assayed on glass slides (VRC26.09, PGT121, 2G12, PGT128, VRC13, PGT151, 35O22), while most of the antibodies did not have affinity for oligosaccharide in the context of a glycan array (PG9, PGT145, PGDM1400, PGT135, b12, CH103, HJ16, VRC16, VRC01, VRC-PG04, VRC-CH31, VRC-PG20, 3BNC60, 12A12, VRC18b, VRC23, VRC27, 1B2530, 8ANC131, 8ANC134, 8ANC195).
Stewart-Jones2016
(antibody binding site, glycosylation, structure)
-
2G12: This study assessed the ADCC activity of antibodies of varied binding types, including CD4bs (b6, b12, VRC01, PGV04, 3BNC117), V2 (PG9, PG16), V3 (PGT126, PGT121, 10-1074), oligomannose (2G12), MPER (2F5, 4E10, 10E8), CD4i (17b, X5), C1/C5 (A32, C11), cluster I (240D, F240), and cluster II (98-6, 126-7). ADCC activity was correlated with binding to Env on the surfaces of virus-infected cells. ADCC was correlated with neutralization, but not always for lab-adapted viruses such as HIV-1 NLA-3.
vonBredow2016
(effector function)
-
2G12: This review summarizes representative anti-HIV MAbs of the first generation (2G12, b12, 2F5, 4E10) and second generation (PG9, PG16, PGT145, VRC26.09, PGDM1400, PGT121, PGT124, PGT128, PGT135, 10-1074, VRC01, 3BNC117, CH103, PGT151, 35O22, 8ANC195, 10E8). Structures, epitopes, VDJ usage, CDR usage, and degree of somatic hypermutation are compared among these antibodies. The use of SOSIP trimers as immunogens to elicit B-cell responses is discussed.
Burton2016
(review, structure)
-
2G12: Two stable homogenous gp140 Env trimer spikes, Clade A 92UG037.8 Env and Clade C C97ZA012 Env, were identified. 293T cells stably transfected with either presented fully functional surface timers, 50% of which were uncleaved. A panel of neutralizing and non-neutralizing Abs were tested for binding to the trimers. Glycan Ab 2G12 bound cell surface gp160 weakly and strongly bound it without its C-terminal (gp160ΔCT), whether in the presence of sCD4 or not. It was unable to neutralize the 92UG037.8 HIV-1 isolate.
Chen2015
(neutralization, binding affinity)
-
2G12: PGT145 was used to positively isolate a subtype B Env trimer immunogen, B41 SOSIP.664-D7324, that exists in two conformations, closed and partially open. bNAbs tested against the trimer were able to neutralize the B41 pseudovirus with a wide range of potencies. All tested non-NAbs did not neutralize B41 (IC50 >50µg/ml). OD glycan bNAb, 2G12, neutralized and bound B41 pseudovirus and trimer.
Pugach2015
-
2G12: A comprehensive antigenic map of the cleaved trimer BG505 SOSIP.664 was made by bNAb cross-competition. Epitope clusters at the CD4bs, quaternary V1/V2 glycan, N332-oligomannose patch and new gp120-gp41 interface and their interactions were delineated. Epitope overlap, proximal steric inhibition, allosteric inhibition or reorientation of glycans were seen in Ab cross-competition. Thus bNAb binding to trimers can affect surfaces beyond their epitopes. 2G12 non-reciprocally out-competed PGT135 and PGT136, all N332-outer domain (OD) glycan oligomannose patch bNAbs.
Derking2015
(antibody interactions, neutralization, binding affinity, structure)
-
2G12: Two clade C recombinant Env glycoprotein trimers, DU422 and ZM197M, with native-like structural and antigenic properties involving epitopes for all known classes of bNAbs, were produced and characterized. These Clade C trimers (10-15% of which are in a partially open form) were more like B41 Clade B trimers which have 50-75% trimers in the partially open configuration than like B505 Clade B trimers, almost 100% in the closed, prefusion state. The Clade C trimers are reactive with bNAb 2G12, which was used to purify antigenically high quality, native-like trimers. OD-glycan binding 2G12 however, was not able to neutralize the equivalent pseudotyped viruses for either trimer.
Julien2015
(assay or method development, structure)
-
2G12: Env trimer BG505 SOSIP.664 as well as the clade B trimer B41 SOSIP.664 were stabilized using a bifunctional aldehyde (glutaraldehye, GLA) or a heterobifunctional cross-linker, EDC/NHS with modest effects on antigenicity and barely any on biochemistry or structural morphology. ELISA, DSC and SPR were used to test recognition of the trimers by bNAbs, which was preserved and by weakly NAbs or non-NAbs, which was reduced. Cross-linking partially preserves quaternary morphology so that affinity chromatography by positive selection using quaternary epitope-specific bNAabs, and negative selection using non-NAbs, enriched antigenic characteristics of the trimers. Mannose patch-specific gp120-binding bNAb, 2G12, was conformationally insensitive to mild denaturation during ELISA and bound timers.
Schiffner2016
(assay or method development, binding affinity, structure)
-
2G12: The native-like, engineered trimer BG505 SOSIP.664 induced potent NAbs against conformational epitopes of neutralization-resistant Tier-2 viruses in rabbits and macaques, but induced cross-reactive NAbs against linear V3 epitopes of neutralization-sensitive Tier-1 viruses. A different trimer, B41 SOSIP.664 also induced strong autologous Tier-2 NAb responses in rabbits. Sera from only 2/20 BG505 SOSIP.664-D7324 trimer-immunized rabbits were capable of inhibiting N332 glycan-dependent 2G12 binding to outer domain glycans.
Sanders2015
(antibody generation, neutralization, binding affinity, polyclonal antibodies)
-
2G12: A new trimeric immunogen, BG505 SOSIP.664 gp140, was developed that bound and activated most known neutralizing antibodies but generally did not bind antibodies lacking neuralizing activity. This highly stable immunogen mimics the Env spike of subtype A transmitted/founder (T/F) HIV-1 strain, BG505. Anti-OD glycan bNAb 2G12 neutralized BG505.T332N, the pseudoviral equivalent of the immunogen BG505 SOSIP.664 gp140, and was shown to recognize and bind the immunogen too.
Sanders2013
(assay or method development, neutralization, binding affinity)
-
2G12: This review discusses the application of bNAbs for HIV treatment and eradication, focusing on bnAbs that target key epitopes, specifically: 2G12, 2F5, 4E10, VRC01, 3BNC117, PGT121, VRC26.08, VRC26.09, PGDM1400, and 10-1074. Antibodies 2G12, 2F5, and 4E10 were among the first bnAbs available for clinical testing, and a cocktail of these 3 Abs was assessed in human trials.
Stephenson2016
(immunotherapy, review)
-
2G12: This study described a natural interaction between Abs and mucin protein, especially, MUC16 that is enhanced in chronic HIV infection. Agalactosylated (G0) Abs demonstrated the highest binding to MUC16. Binding of Abs to epithelial cells was diminished following MUC16 knockdown, and the MUC16 N-linked glycans were critical for binding.These point to a novel opportunity to enrich Abs at mucosal sites by targeting Abs to MUC16 through changes in Fc glycosylation, potentially blocking viral movement. In 2G12 differential G0 content was linked to MUC16 binding supporting a role for G0 glycosylation in preferential MUC16 binding, independent of antigen specificity (Fig: S4).
Gunn2016
(antibody interactions, glycosylation)
-
2G12: A mathematical model was developed to predict the Ab concentration at which antibody escape variants outcompete their ancestors, and this concentration was termed the mutant selection window (MSW). The MSW was determined experimentally for 12 pairings of diverse HIV strains against 7 bnAbs (b12, 2G12, PG9, PG16, PGT121, PGT128, 2F5). The neutralization of 2G12 was assayed against JRFL-N332S (resistant strain) and JRFL (sensitive strain).
Magnus2016
(neutralization, escape)
-
2G12: The study detailed binding kinetics of the interaction between BG505 SOSIP.664 trimer or its variants (gp120 monomer; first study of disulfide-stabilized variant gp120-gp41ECTO protomer) and several mAbs, both neutralizing (VRC01, PGV04, PG9, PG16, PGT121, PGT122, PGT123, PGT145, PGT151, 2G12) and non-neutralizing (b6, b12, 14e, 19b, F240). Glycan-binding 2G12 bound similarly to monomer and trimer and marginally better to protomer.
Yasmeen2014
(antibody binding site, assay or method development)
-
2G12: 2G12 was expressed in transgenic rice endosperm to evaluate the potential of rice seeds as a vehicle for inexpensive microbicide production. Although the heavy chain was predominantly aglycosylated, the heavy and light chains assembled into functional antibodies with more potent HIV-neutralizing activity than other plant-derived forms of 2G12 bearing typical high-mannose or plant complex-type glycans. Assembled antibody accumulated predominantly in protein storage vacuoles but also induced the formation of novel, spherical storage compartments surrounded by ribosomes indicating that they originated from the endoplasmic reticulum.
Vamvaka2016
-
2G12: Neutralization breadth in 157 antiretroviral-naive individuals infected for less than 1 year post-infection was studied and compared to a cohort of 170 untreated chronic patients. A range of neutralizing activities was observed with a panel of six recombinant viruses from five different subtypes. Some sera were broadly reactive, predominantly targeting envelope epitopes within the V2 glycan-dependent region. The Env neutralization breadth was positively associated with time post infection. 2G12 has been used as a control in detection of glycan-dependent HIV-1 neutralizing sera.
Sanchez-Merino2016
(neutralization, acute/early infection)
-
2G12: Ten mAbs were isolated from a vertically-infected infant BF520 at 15 months of age. Ab BF520.1 neutralized pseudoviruses from clades A, B and C with a breadth of 58%, putting it in the same range as second-generation bNAbs derived from adults, but its potency was lower. BF520.1 was shown to target the base of the V3 loop at the N332 supersite. Outer domain glycan-binding, first generation mAb, 2G12 when compared had a geometric mean of IC50=2.43 µg/ml for 2/12 viruses it neutralized at a potency of 17%. The infant-derived antibodies had a lower rate of somatic hypermutation (SHM) and no indels compared to adult-derived anti-V3 mAbs. This study shows that bnAbs can develop without SHM or prolonged affinity maturation.
Simonich2016
(antibody binding site, neutralization, responses in children, structure)
-
2G12: The neutralization of 14 bnAbs was assayed against a global panel of 12 or 17 Env pseudoviruses. From IC50, IC80, IC90, and IC99 values, the slope of the dose-response curve was calculated. Each class of Ab had a fairly consistent slope. Neutralization breadth was strongly correlated with slope. An IIP (Instantaneous Inhibitory Potential) value was calculated, based on both the slope and IC50, and this value may be predictive of clinical efficacy. 2G12, a high mannose (HM) cluster bnAb belonged to a group with slopes ˜1.
Webb2015
(neutralization)
-
2G12: The study's goal was to produce modified SOSIP trimers that would reduce the exposure - and, by inference, the immunogenicity - of non-NAb epitopes such as V3. The binding of several modified SOSIP trimers was compared among 12 neutralizing (PG9, PG16, PGT145, PGT121, PGT126, 2G12, PGT135, VRC01, CH103, CD4, IgG2, PGT151, 35O22) and 3 non-neutralizing antibodies (14e, 19b, b6). The V3 non-NAbs 447-52D, 39F, 14e, and 19b bound less well to all A316W variant trimers compared to wild-type trimers. Mice and rabbits immunized with modified, stabilized SOSIP trimers developed fewer V3 Ab responses than those immunized with native trimers.
deTaeye2015
(antibody binding site)
-
2G12: HIV-1 strains were isolated from 60 patients infected with CRFs 01_AE, 07_BC, and 08_BC. Eight CRF01 strains that produced high-titer Env pseudoviruses were studied further. All were sensitive to neutralization by VRC01, PG9, PG16, and NIH45-46, but insensitive to 2G12. Of the 8 strains, 7 lacked glycans at Env 295 or 332, or both, suggesting that these glycosylation sites play a role in 2G12 binding and neutralization.
Chen2016
(neutralization, subtype comparisons)
-
2G12: A large cross-sectional study of sera from 205 ART-naive patients infected with different HIV clades was tested against a panel of 219 cross-clade Env-pseudotyped viruses. Their neutralization was compared to the neutralization of 10 human bNAbs (10E8, 4E10, VRC01, PG9, PGT145, PGT128, 2F5, CH01, b12, 2G12) tested with a panel of 119 Env-pseudotyped viruses. Results from b12 and 2G12 suggested that these bnAbs may not be as broadly neutralizing as previously thought. 2G12 neutralized 20% of the 199 viruses tested, whereas a previous study had estimated this value at 41%.
Hraber2014
(neutralization)
-
2G12: A flow-cytometry-based assay allowed non-radioactive measurement of ADCC-mediated elimination of HIV-1 gp120 envelope glycoprotein (Env)-coated target cells. This assay relies on staining target and effector cells with different dyes, which allows precise gating and permits the calculation of the number of surviving target cells by normalization to flow-cytometry particles.
Richard2014
(anti-idiotype, assay or method development, effector function)
-
2G12: This study describes a new level of complexity in antibody recognition of the mixed glycan-protein epitopes of the N332 region of HIV gp120. A combination of three antibody families that target the high-mannose patch can lead to 99% neutralization coverage of a large panel of viruses containing the N332/334 glycan site and up to 66% coverage for viruses that lack the N332/334 glycan site. PGT121, PGT128 and PGT135 families were studied. 2G12 was used as control since its binding is N332-dependent but it is less potent and broad in neutralization, recognizes glycans solely, and has a unique domain-exchanged structure.
Sok2014a
(antibody interactions, glycosylation)
-
2G12: Incomplete neutralization may decrease the ability of bnAbs to protect against HIV exposure. In order to determine the extent of non-sigmoidal slopes that plateau at <100% neutralization, a panel of 24 bnMAbs targeting different regions on Env was tested in a quantitative pseudovirus neutralization assay on a panel of 278 viral clones. All bNAbs had some viruses that they neutralized with a plateau <100%, but those targeting the V2 apex and MPER did so more often. All bnMAbs assayed had some viruses for which they had incomplete neutralization and non-sigmoidal neutralization curves. bNAbs were grouped into 3 groups based on their neutralization curves: group 1 antibodies neutralized more than 90% of susceptible viruses to >95% (PGT121-123, PGT125-128, PGT136, PGV04); group 2 was less effective, resulting in neutralization of 60-84% of susceptible viruses to >95% (b12, PGT130-131, PGT135, PGT137, PGT141-143, PGT145, 2G12, PG9); group 3 neutralized only 36-60% of susceptible viruses to >95% (PG16, PGT144, 2F5, 4E10). Among the panel tested, antibodies b12, 2G12, PGT136, and PGT137 had relatively few viruses neutralized with an IC50 <1 ug/ml.
McCoy2015
(neutralization)
-
2G12: The neutralization abilities of Abs were enhanced by bioconjugation with aplaviroc, a small-molecule inhibitor of virus entry into host cells. Diazonium hexafluorophosphate was used. The conjugated Abs blocked HIV-1 entry through two mechanisms: by binding to the virus itself and by blocking the CCR5 receptor on host cells. Chemical modification did not significantly alter the potency and the pharmacokinetics. Improvements in potency over the parent Ab was ∼3-fold for 2G12-aplaviroc against the JR-FL isolate.
Gavrilyuk2013
(neutralization)
-
2G12: Galactosyl ceramide (Galcer), a glycosphingolipid, is a receptor for the HIV-1 Env glycoprotein. This study has mimicked this interaction by using an artificial membrane containing synthetic Galcer and recombinant HIV-1 Env proteins to identify antibodies that would block the HIV-1 Env-Galcer interaction. HIV-1 ALVAC/AIDSVAX vaccinee-derived MAbs specific for the gp120 C1 region blocked Galcer binding of a transmitted/founder HIV-1 Env gp140. The antibody-dependent cellular cytotoxicity-mediating CH38 IgG and its natural IgA isotype were the most potent blocking antibodies.2G12 did not block Env-Galcer binding.
Dennison2014
(antibody binding site, antibody interactions, effector function, glycosylation)
-
2G12: This review surveyed the Vectored Immuno Prophylaxis (VIP) strategy, which involves passive immunization by viral vector-mediated delivery of genes encoding bnAbs for in vivo expression. Recently published studies in humanized mice and macaques were discussed as well as the pros and cons of VIP towards clinical applications to control HIV endemics. A single injection of AAV8 vector achieved peak Ab production in serum at week 6 and offered moderate protection. 2G12 (˜250 μg/mL) yielded partial protection.
Yang2014
(immunoprophylaxis, review, antibody gene transfer)
-
2G12: The ability of bNAbs to inhibit the HIV cell entry was tested for b12, VRC01,VRC03, PG9, PG16, PGT121, 2F5, 10E8, 2G12. Among them, PGT121, VRC01, and VRC03 potently inhibited HIV entry into CD4+ T cells of infected individuals whose viremia was suppressed by ART.
Chun2014
(immunotherapy)
-
2G12: Pairwise combinations of 6 NAbs (4E10, 2F5, 2G12, b12, PG9, PG16) were tested for neutralization of pseudoviruses and transmitted/founder viruses. Each of the NAbs tested targets a different region of gp120 or gp41. Some pairwise combinations enhanced neutralization synergistically, suggesting that combinations of NAbs may enhance clinical effectiveness.
Miglietta2014
(neutralization)
-
2G12: The study compared various factors affecting the accessibility of epitopes for antibodies targeting the V2 integrin (V2i) region, versus the V3 region. CD4 treament of BaL and JRFL pseudoviruses increased their neutralization sensitivity to V3 MAbs, but not to V2i MAbs. Viruses grown in a glycosidase inhibitor were more sensitive to neutralization by V3, but not V2i, MAbs. Increasing the time of virus-MAb interaction increased virus neutralization by some V2i MAbs and all V3 MAbs. The structural dynamics of V2i and V3 epitopes has important effects in neutralization. Some experiments also included CD4BS antibodies b12, 2G12 and NIH45-46.
Upadhyay2014
-
2G12: Dimeric 2G12 is much more potent than the monomeric form. This study compared monomeric and dimeric 2G12 by examination of crystal structures and electron microscopy. The greater potency and breadth of the dimeric form were attributed to intermolecular domain exchange, flexibility, and the avidity effects of bivalent binding.
Wu2013
(structure)
-
2G12: Cross-group neutralization of HIV-1 isolates from groups M, N, O, and P was tested with diverse patient sera and bNAbs PG9, PG16, 4E10, b12, 2F5, 2G12, VRC01, VRC03, and HJ16. The primary isolates displayed a wide spectrum of sensitivity to neutralization by the human sera, with some cross-group neutralization clearly observed. Among the bNAbs, only PG9 and PG16 showed any cross-group neutralization. The group N prototype strain YBF30 was highly sensitive to neutralization by PG9, and the interaction between their key residues was confirmed by molecular modeling. The conservation of the PG9/PG16 epitope within groups M and N suggests its relevance as a vaccine immunogen.
Braibant2013
(neutralization, variant cross-reactivity)
-
2G12: The binding affinity of 2G12 for sugar molecules associated with glycans was tested through computer modeling. Affinity for D-fructose was greater than for D-mannose.
Koyama2014
(binding affinity)
-
2G12: The structure of 2G12 in association with Env trimer from HIV strain BG505-SOSIP was characterized. The 2G12 epitope overlaps with several other bNAbs that target the N332 supersite of vulnerability. Glycans N295, N392, and N339 are centrally located within the footprint of the antibody, while N448 and N386 are on the periphery. 2G12 may block membrane fusion by inducing steric hindrance upon primary receptor binding, thus abrogating Env's interaction with coreceptors.
Murin2014
(structure)
-
2G12: 2G12 was one of 10 MAbs used to study chronic vs. consensus vs. transmitted/founder (T/F) gp41 Envs for immunogenicity. Consensus Envs were the most potent eliciters of response but could only neutralize tier 1 and some tier 2 viruses. T/F Envs elicited the greatest breadth of NAb response; and chronic Envs elicited the lowest level and narrowest response. This Glycan binding Nab bound well at <10 nM to 3/5 chronic Envs, 4/6 Consensus Envs and 4/7 T/F Envs.
Liao2013c
(antibody interactions, binding affinity)
-
2G12: The infectious virion (iVirions) capture index (IVCI) of different Abs have been determined. bnAbs captured higher proportions of iVirions compared to total virus particles (rVirions) indicating the capacity, breadth and selectively of bnAbs to capture iVirions. IVCI was additive with a mixture of Abs, providing proof of concept for vaccine-induced effect of improved capacity. bnAb 2G12 showed significantly high IVCI >1.0, but did not capture HIV subtype B T/F CH040, subtype C CH185.C, or subtype A/E AE.92TH023.
Liu2014
(binding affinity)
-
2G12: Study evaluated 4 gp140 Env protein vaccine immunogens derived from an elite neutralizer donor VC10042, an HIV+ African American male from Vanderbilt cohort. Env immunogens, VC10042.05, VC10042.05RM, VC10042.08 and VC10042.ela, elicited high titers of cross-reactive Abs recognizing V1/V2 regions. All the Env protein except VC10042.ela bound to 2G12, but none of the parental Env were neutralized by 2G12.
Carbonetti2014
(elite controllers and/or long-term non-progressors, vaccine-induced immune responses)
-
2G12: The effect of low pH and HIV-1 Abs which increased the transcytosis of the virus by 20 fold, has been reported. This enhanced transcytosis was due to the Fc neonatal receptor (FcRn), which facilitates HIV-1's own transmission by usurping Ab responses directed against itself. Both infectious and noninfectious viruses were transcytosed by 2G12.
Gupta2013
-
2G12: This study examined how the conserved gp120-gp41 association site adapts to glycan changes that are linked to neutralization sensitivity, using a DSR mutant virus, K601D. K601D has a defective gp120-association, and was sequentially passaged in peripheral blood mononuclear cells to select for suppressor mutations. Mutations 136 and/or glycan 142 increased the sensitivity of T138N and ΔN.
Drummer2013
(antibody interactions, glycosylation)
-
2G12: Clade A Env sequence, BG505, was identified to bind to bNAbs representative of most of the known NAb classes. This sequence is the best natural sequence match (73%) to the MRCA sequence from 19 Env sequences derived from PG9 and PG16 MAbs' donor. A point mutation at position L111A of BG505 enabled more efficient production of a stable gp120 monomer, preserving the major neutralization epitopes. The antisera produced by this adjuvanted formulation of gp120 competed with bnAbs from 3 classes of non-overlapping epitopes. 2G12 bound to BG505L111A monomer, but failed to neutralize BG505 pseudovirus.
Hoffenberg2013
(antibody interactions)
-
2G12: The neutralization profile of 1F7, a human CD4bs mAb, is reported and compared to other bnNAbs. 1F7 exhibited extreme potency against primary HIV-1, but limited breadth across clades. 2G12 neutralized 33% of a cross-clade panel of 157 HIV-1 isolates (Fig. S1) while 1F7 neutralized only 20% of the isolates.
Gach2013
(neutralization)
-
2G12: This study reported the Ab binding titers and neutralization of 51 patients with chronic HIV-1 infection on supressive ART for 3 yrs. A high titer of Ab against gp120, gp41, and MPER was found. Patient sera were evaluated for binding against recombinant gp120JR-FL mutants lacking either the V1/V2 loop or the V3 loop. Significantly higher end point binding titers and HIV1JR-FL neutralization were noticed in patients with >10 compared to <10 yrs of detectable HIV RNA. 2G12 was used as a CD4b Ab control.
Gach2014
(neutralization, HAART, ART)
-
2G12: This study reports the development of a new cell-line (A3R5)-based highly sensitive Ab detection assay. This T-lymphoblastoid cell-line stably expreses CCR5 and recognizes CCR5-tropic circulating strains of HIV-1. A3R5 cells showed greater neutralization potency compared to the current cell-line of choice TZM-bl. 2G12 was used as a reference Ab in neutralization assay comparing A3R5 and TZM-bl.
McLinden2013
(assay or method development)
-
2G12: The crystal structure of PGT135 with gp120, CD4 and Fab 17b was analyzed to study how PGT135 recognizes its Asn332 glycan-dependent epitope. The combined structural studies of PGT 135, PGT 128 and 2G12 show this Asn332-dependent epitope is highly accessible and much more extensive than initially appreciated, allowing for multiple binding modes and varied angles of approach, thus representing a supersite of vulnerability for antibody neutralization.
Kong2013
(structure)
-
2G12: This is a review of identified bNAbs, including the ontogeny of B cells that give rise to these antibodies. Breadth and magnitude of neutralization, unique features and similar bNAbs are listed. 2G12 is a V3-glycan Ab, with breadth 18%, IC50 4.85 μg per ml, and its unique feature is glycan-only recognition.
Kwong2013
(review)
-
2G12: A32 and 2G12 MAbs were used to trigger ADCC activity and to show that HIV Nef and Vpu protect HIV-infected CD4+ T cells from ADCC through down-modulation of CD4 and BST2.
Pham2014
(effector function)
-
2G12: A highly conserved mechanism of exposure of ADCC epitopes on Env is reported, showing that binding of Env and CD4 within the same HIV-1 infected cell effectively exposes these epitopes. The mechanism might explain the evolutionary advantage of downregulation of cell surface CD4v by the Vpu and Nef proteins. 2G12 was used in CD4 coexpression and competitive binding assay. Results showed a strong correlation of deletion of vpu gene and 2G12 binding.
Veillette2014
(effector function)
-
2G12: The ability of MAb A32 to recognize HIV-1 Env expressed on the surface of infected CD4(+) T cells as well as its ability to mediate antibody-dependent cellular cytotoxicity (ADCC) activity was investigated. This study demonstrates that the epitope defined by MAb A32 is a major target on gp120 for plasma ADCC activity. 2G12 was used as a control and A32 showed >3 fold higher ADCC activity than 2G12.
Ferrari2011a
(effector function)
-
2G12: Env pseudo-typed viruses generated from 7 transmitting and 4 non-transmitting mothers and their children were studied to identify phenotypes that associate with the risk of mother to child transmission. There were no differences in neutralization with 2F5, 2G12, 4E10 and b12, but transmitting mothers had higher autologous NAb responses against gp120/gp41, suggesting that strong autologous neutralization activity can associate with risk of transmission and be in fact detrimental.
Baan2013
(neutralization, mother-to-infant transmission)
-
2G12: A statistical model selection method was used to identify a global panel of 12 reference Env clones among 219 Env-pseudotyped viruses that represent the spectrum of neutralizing activity seen with sera from 205 chronically HIV-1-infected individuals. This small final panel was also highly sensitive for detection of many of the known bNAbs, including this one. The small panel of 12 Env clones should facilitate assessments of vacine-elicited NAbs.
Decamp2014
(assay or method development)
-
2G12: A panel of NAbs and non-neutralizing Abs (NoNAbs) displaying the highest Fc γR-mediated inhibitory activity and significant ADCC were selected and formulated in a microbicidal gel and tested for their antiviral activity against SHIVSF162P3 vaginal challenge in non-human primates. Combination of 2G12, 2F5 and 4E10 fully prevented vaginal transmission. Two NoNAbs 246-D and 4B3 had no impact on viral acquisition, but reduced plasma viral load.
Moog2014
(effector function, SIV)
-
2G12: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 2G12 is discussed as the C2, C3, C4 and V4 glycation sites-targeting neutralizing anti-gp120 mAb exhibiting ADCC activity and having a discontinuous epitope.
Pollara2013
(effector function, review)
-
2G12: "Neutralization fingerprints" for 30 neutralizing antibodies were determined using a panel of 34 diverse HIV-1 strains. 10 antibody clusters were defined: VRC01-like, PG9-like, PGT128-like, 2F5-like, 10E8-like and separate clusters for b12, CD4, 2G12, HJ16, 8ANC195. This mAb belongs to 10E8-like cluster.
Georgiev2013
(neutralization)
-
2G12: This paper reported the nature of junk Env glycan that undermine the development of Ab responses against gp120/gp41 trimers and evaluated enzyme digestion as a way to remove aberrant Env to produce "trimer VLPs". 2G12 with its high-mannose glycan profile showed binding to gp160ER, considered as VLP-contaminant.
Crooks2011
(glycosylation)
-
2G12: This study described a potential novel conformational epitope that is present in a subtype C infected subject during early infection. This epitope was recognized by three different B cell receptors and elicited both glycan dependent and independent MAbs. This also showed the power of a single strategically placed amino acid change in viral escape. 2G12 was discussed as a BnAb directed against glycan in describing the role of "glycan shield" in viral escape.
Lynch2011a
(glycosylation, escape, cell-line isolated antibody)
-
2G12: The role of NK cells and NK cell receptor polymorphisms in the assessment of HIV-1 neutralization is reported. 2G12 was used in viral inhibition assay as a control to compare NK cells participation and activity.
Brown2012
(neutralization, NK cells)
-
2G12: This study describes an ˜11 Angstrom cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and gp41 subunits form a cage like structure with an interior void surrounding the trimer axis which restricts Ab access. 2G12 was used in ELISA to asses the recognition of the purified Env glycoproteins and recognized a high-mannose glycan array on the gp120 outer domain.
Mao2012
(structure)
-
2G12: The sera of 20 HIV-1 patients were screened for ADCC in a novel assay measuring granzyme B (GrB) and T cell elimination and reported that complex sera mediated greater levels of ADCC than anti-HIV mAbs. The data suggested that total amount of IgG bound is an important determinant of robust ADCC which improves the vaccine potency. 2G12 was used as an anti-gp120 to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets.
Smalls-Mantey2012
(assay or method development, effector function)
-
2G12: Isolation of VRC06 and VRC06b MAbs from a slow progressor donor 45 is reported. This is the same donor from whom bnMAbs VRC01, VRC03 and NIH 45-46 were isolated and the new MAbs are clonal variants of VRC03. 2G12 was used as a glycan specific Ab and as a negative control to compare binding specificity of VRC06.
Li2012
-
2G12: Immunogenicity of gp120 immunogens from two pairs of clade B and two pairs of clade C mother-to-child transmitted HIV-1 variants was studied in rabbits. While high level Env-specific antibody responses were elicited by all immunogens, their abilities to NAb responses differed and neutralization-resistant variants elicited broader NAb. Each of the six Env antigens resistant to 2G12 lacked at least one of the four Potential N-Linked Glycosylation sites (PNGS) important for 2G12 binding.
Wang2012
(mother-to-infant transmission)
-
2G12: Protective potency of PGT121 was evaluated in vivo in rhesus macaques. PGT121 efficiently protected against high-dose challenge of SHIV SF162P3 in macaques. Sterilizing immunity was observed in 5/5 animals administered 5 mg/kg antibody dose and in 3/5 animals administered 0.2 mg/kg, suggesting that a protective serum concentration for PG121 is in the single-digit mg/mL. PGT121was effective at serum concentration 600-fold lower than for 2G12 and 100-fold lower than for b12.
Moldt2012a
(immunoprophylaxis)
-
2G12: The unbinding kinetics of the gp120-2G12, Man(4)-2G12, and Man(5)-2G12 interactions were measured by single-molecule force spectroscopy. This is the first single-molecule study aimed at dissecting the carbohydrate-antibody recognition of the gp120-2G12 interaction. The study confirmed crystallographic models that show both the binding of the linear Man(4) arm to 2G12 and also the multivalent gp120 glycan binding to 2G12.
Martines2012
(binding affinity)
-
2G12: Three mouse B cell lines expressing domain-exchanged 2G12 WT, the non-domain-exchanged 2G12 I19R variant, and 2G12 gl as IgM B cell receptors (BCRs) were used to determine the potential of carbohydrate immunogens to elicit Y-shaped or domain-exchanged antibodies in vivo. HIV envelope glycoproteins and candidate glycoconjugate vaccines were compared for their ability to activate these B cell lines. Several of these immunogens were able to activate both 2G12 WT and 2G12 I19R B cell lines, and the discrete cluster of oligomannose glycans could selectively activate the domain-exchanged 2G12 WT cells. None of the immunogens tested were able to activate the germ line 2G12 B cells. The engineered B cell lines were more sensitive than standard ELISA binding assays and may help in the design of immunogens that elicit 2G12-like domain-exchanged antibodies in vivo.
Doores2013
(assay or method development, glycosylation)
-
2G12: A computational tool (Antibody Database) identifying Env residues affecting antibody activity was developed. As input, the tool incorporates antibody neutralization data from large published pseudovirus panels, corresponding viral sequence data and available structural information. The model consists of a set of rules that provide an estimated IC50 based on Env sequence data, and important residues are found by minimizing the difference between logarithms of actual and estimated IC50. The program was validated by analysis of MAb 8ANC195, which had unknown specificity. Predicted critical N-glycosylation for 8ANC195 were confirmed in vitro and in humanized mice. The key associated residues for each MAb are summarized in the Table 1 of the paper and also in the Neutralizing Antibody Contexts & Features tool at Los Alamos Immunology Database.
West2013
(glycosylation, computational prediction)
-
2G12: Identification of broadly neutralizing antibodies, their epitopes on the HIV-1 spike, the molecular basis for their remarkable breadth, and the B cell ontogenies of their generation and maturation are reviewed. Ontogeny and structure-based classification is presented, based on MAb binding site, type (structural mode of recognition), class (related ontogenies in separate donors) and family (clonal lineage). This MAb's classification: gp120 glycan-V3 site, type glycans and domain swapping, 2G12 class, 2G12 family.
Kwong2012
(review, structure, broad neutralizer)
-
2G12: This review discusses the new research developments in bnAbs for HIV-1, Influenza, HCV. Models of the HIV-1 Env spike and of Influenza visrus spike with select bnAbs bound are shown.
Burton2012
(review)
-
2G12: Somatic hypermutations are preferably found in CDR loops, which alter the Ab combining sites, but not the overall structure of the variable domain. FWR of CDR are usually resistant to and less tolerant of mutations. This study reports that most bnAbs require somatic mutations in the FWRs which provide flexibility, increasing Ab breadth and potency. To determine the consequence of FWR mutations the framework residues were reverted to the Ab's germline counterpart (FWR-GL) and binding and neutralizing properties were then evaluated. 2G12, which recognizes carbohydrates, was among the 17 bnAbs which were used in studying the mutations in FWR. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 2G12.
Klein2013
(neutralization, structure, antibody lineage)
-
2G12: Antigenic properties of 2 biochemically stable and homogeneous gp140 trimers (A clade 92UG037 and C clade CZA97012) were compared with the corresponding gp120 monomers derived from the same percursor sequences. The trimers had nearly all the antigenic properties expected for native viral spikes and were markedly different from monomeric gp120. 2G12 bound trimers and monomers equally well, indicating that the epitope is fully accessible in both forms.
Kovacs2012
(antibody binding site, neutralization, binding affinity)
-
2G12: Crystal structure and mechanistic analysis of 2F5-gp41 complex is reported. b12 has been referred as a BnAb directed against the exterior gp120 envelope glycoprotein.
Ofek2004
(antibody interactions, structure)
-
2G12: Glycan shield of HIV Env protein helps to escape the Ab recognition. Several of the PGT BnAbs interact directly with the HIV glycan coat. Crystal structures of Fabs PGT127 and PGT128 showed that the high neutralizing potency was mediated by cross-linking Env trimers on the viral surface. 2G12 was discussed in terms of recognizing terminal dimannose and binding to glycan coat.
Pejchal2011
(glycosylation, structure, broad neutralizer)
-
2G12: Intrinsic reactivity of HIV-1, a new property regulating the level of both entry and sensitivity to Abs has been reported. This activity dictates the level of responsiveness of Env protein to co-receptor, CD4 engagement and Abs. 2G12 has been used as a control CD4BS binding Ab in neutralization assays.
Haim2011
(antibody interactions)
-
2G12: Glycan Asn332-targeting broadly cross-neutralizing (BCN) antibodies were studied in 2 C-clade infected women. The ASn332 glycan was absent on infecting virus, but the BCN epitope with Asn332 evolved within 6 months though immune escape from earlier antibodies. Plasma from the subject CAP177 neutralized 88% of a large multi-subtype panel of 225 heterologous viruses, whereas CAP 314 neutralized 46% of 41 heterologous viruses but failed to neutralize viruses that lack glycan at 332. CAP177 or CAP314 clones were not sensitive to 2G12.
Moore2012
(neutralization, escape)
-
2G12: This study reports the isolation of a panel of Env vaccine elicited CD4bs-directed macaque mAbs and genetic and functional features that distinguish these Abs from CD4bs MAbs produced during chronic HIV-1 infection. 2G12 was used as a negative control Abs in competitive binding assay with non human primates mAbs.
Sundling2012
(vaccine-induced immune responses)
-
2G12: The goal of this study was to improve the humoral response to HIV-1 by targeting trimeric Env gp140 to B cells. The gp140 was fused to a proliferation-inducing ligand (APRIL), B cell activation factor (BAFF) and CD40 ligand (CD40L). These fusion proteins increased the expression of activation-induced-cytidine deaminase (AID) responsible for somatic hypermutation, Ab affinity maturation, and Ab class switching. The Env-APRIL induced high anti-Env responses against tier1 viruses. 2G12 was used in BN-PAGE trimer shift assay.
Melchers2012
(neutralization)
-
2G12: Existing structural and sequence data was analyzed. A set of signature features for potent VRC01-like (PVL) and almost PVL abs was proposed and verified by mutagenesis. 2G12 has been referred in discussing the breadth and potency of antiCD4 abs.
West2012a
(antibody lineage)
-
2G12: Synthesis of an engineered soluble heterotrimeric gp140 is described. These gp140 protomers were designed against clade A and clade B viruses. The heterotrimer gp140s exhibited broader anti-tier1 isolate neutralizing antibody responses than homotrimer gp140. 2G12 was used to determine and compare the immunogenicity of homo and heterotrimers gp140s. 2G12 didn't exhibit any difference in binding to homotrimeric clade A and clade B gp140 binding.
Sellhorn2012
(vaccine antigen design)
-
2G12: This paper showed that nAb 2G12, which binds to gp120 N glycans with α (1,2)-linked mannose termini and inhibits replication after passive transfer to patients, neutralizes by slowing entry of adsorbed virus. It is suggested that 2G12 competitively inhibits interactions between gp120 V3 loop and the tyrosine sulfate containing amino terminus, thus reducing assembly of complexes that catalyze entry.
Platt2012
(antibody interactions, glycosylation)
-
2G12: The use of computationally derived B cell clonal lineages as templates for HIV-1 immunogen design is discussed. 2G12 has been discussed in terms of immunogenic and functional characteristics of representative HIV-1 BnAbs and their reactions to antigens.
Haynes2012
(antibody interactions, memory cells, vaccine antigen design, review, antibody polyreactivity, broad neutralizer)
-
2G12: Polyclonal B cell responses to conserved neutralization epitopes are reported. Cross-reactive plasma samples were identified and evaluated from 308 subjects tested. 2G12 was used as a control mAb in the comprehensive set of assays performed. Plasma samples C1-0763 and C1-0219 showed comparable activities with 2G12 in competition ELISA.
Tomaras2011
(neutralization, polyclonal antibodies)
-
2G12: Role of envelope deglycosylation in enhancing antigenicity of HIV-1 gp41 epitopes is reported. The mechanism of induction of broad neutralizing Abs is discussed. The hypothesis of presence of "holes" in the naive B cell repertoires for unmutated B cell receptor against HIV-1 Env was tested. The authors inferred that glycan interferences control the binding of unmutated ancestor Abs of broad neutralizing mAb to Env gp41.
Ma2011
(glycosylation, neutralization)
-
2G12: The rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1 is discussed in relation to understanding of vaccine recognition sites, the structural basis of interaction with HIV-1 env and vaccine developmental pathways. 2G12 has been mentioned regarding the recognition of high-mannose glycans
Kwong2011
(antibody binding site, glycosylation, neutralization, vaccine antigen design, review)
-
2G12: A single-cell Ab cloning method is described to isolate neutralizing Abs using truncated gp160 transfected cells as bait. Among the 15 Abs reported, only two are found to be broadly neutralizing and bind to a novel conformational HIV-1 spike epitope. 2G12 was used as a control in neutralizing assay.
Klein2012
(neutralization)
-
2G12: Several antibodies including 10-1074 were isolated from B-cell clone encoding PGT121, from a clade A-infected African donor using YU-2 gp140 trimers as bait. These antibodies were segregated into PGT121-like (PGT121-123 and 9 members) and 10-1074-like (20 members) groups distinguished by sequence, binding affinity, carbohydrate recognition, neutralizing activity, the V3 loop binding and the role of glycans in epitope formation. 2G12 was used as a control in virus neutralization assay. Detail information on the binding and neutralization assays are described in the figures S2-S11.
Mouquet2012a
(glycosylation, neutralization, binding affinity)
-
2G12: YU2 gp140 bait was used to characterize 189 new MAbs representing 51 independent IgG memory B cell clones from 3 clade A or B HIV infected patients exhibiting broad neutralizing activity. 2G12 has been used as a positive control for epitope mapping and evaluating these anti-gp-140 antibodies and a non-sensitive control to DMR/AAA triple mutation.
Mouquet2011
(neutralization)
-
2G12: A panel of glycan deletion mutants was created by point mutation into HIV gp160, showing that glycans are important targets on HIV-1 glycoproteins for broad neutralizing responses in vivo. Enrichment of high mannose N-linked glycan(HM-glycan) of HIV-1 glycoprotein enhanced neutralizing activity of sera from 8/9 patients. 2G12 was used as a control.
Lavine2012
(neutralization)
-
2G12: Ab-driven escape and Ab role in infection control and prevention are reviewed. Main focus is on NAbs, but Ab acting through effector mechanisms are also discussed. 2G12 which was isolated in 1996 and discussed in the context of developing broadly cross-neutralizing antibodies.
Overbaugh2012
(escape, review)
-
2G12: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared. 2G12 bound gp120 and Env-VLPs equivalently. There was no significant correlation between E168K+N189A WT VLP binding and 2G12 neutralization, while trimer VLP ELISA binding and neutralization exhibited a significant correlation. BN-PAGE shifts using digested E168K + N189A WT trimer VLPs exhibited prominence compared to WT VLPs.
Tong2012
(neutralization, binding affinity)
-
2G12: The ability of several broadly neutralizing antibodies that bind gp10 or gp41 to inhibit cell-cell fusion between Clone69TRevEnv cells induced to express the viral envelope proteins, gp120/gp41 and highly CD4-positive SupT1 cells was investigated. Little or no inhibitory effect on cell-cell fusion was observed. MAbs b12, m14 IgG and 2G12 had moderate inhibitory activity; MAbs 4E10 and 2F5 had no inhibitory activity.
Yee2011
(antibody interactions)
-
2G12: Plasma from 14 R5-tropic SHIV-infected macaques was screened for broadly neutralizing activity. A macaque with highly potent cross-clade plasma NAb response was identified. Longitudinal studies showed that the development of broad and autologous NAb responses occurred coincidentally in this animal. Serum-mapping studies, using pseudovirus point mutants and antigen adsorption assays, indicated that the plasma bNAbs are specific for epitopes that include carbohydrates and are critically dependent on the glycan at position 332 of Env gp120. MAb 2G12 was used for comparison.
Walker2011a
(neutralization, polyclonal antibodies)
-
2G12: The role of V1V2 in the resistance of HIV-1 to neutralizing Abs was studied using a panel of neutralization-sensitive and -resistant HIV-1 variants and through exchanging regions of Env between neutralization-sensitive and -resistant viruses. An increase in the length of the V1V2 loop and/or the number of potential N-linked glycosylation sites (PNGS) in that same region of Env was directly involved in the neutralization resistance. The virus that was sensitive to neutralization by autologous serum was also sensitive to neutralization by MAbs b12, 2G12, 2F5, and 4E10, while the virus that was resistant to neutralization by autologous serum was also resistant to neutralization by all of these antibodies except MAb 2G12.
vanGils2011
(glycosylation, neutralization, escape)
-
2G12: A standardized proficiency testing program for measurements of HIV-1-specific NAbs in the TZM-bl assay was developed. Three rounds of optimization involving 21 different test laboratories were required to design the final proficiency testing kit. MAbs b12, 2G12, 2F5, 4E10 and TriMab (b12+2G12+2F5) were used for testing.
Todd2012
(assay or method development)
-
2G12: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors.
Peressin2011
(genital and mucosal immunity, dendritic cells)
-
2G12: The reactivity profiles of MAbs 4E10, 2F5 and 2G12 to those of four pathogenic autoAbs derived from patients with antiphospholipid-syndrome (APS), and to serum from a patient with systemic lupus erythematosus (SLE) were compared using an autoantigen microarray comprising 106 connective tissue disease-related autoantigens. The reactivity profiles of bNt anti-HIV-1 MAbs were distinct from those of pathogenic autoAbs.
Singh2011
(antibody polyreactivity)
-
2G12: Broadly neutralizing antibodies circulating in plasma were studied by affinity chromatography and isoelectric focusing. The Abs fell in 2 groups. One group consisted of antibodies with restricted neutralization breadth that had neutral isoelectric points. These Abs bound to envelope monomers and trimers versus core antigens from which variable loops and other domains have been deleted. Another minor group consisted of broadly neutralizing antibodies consistently distinguished by more basic isoelectric points and specificity for epitopes shared by monomeric gp120, gp120 core, or CD4-induced structures. The pI values estimated for neutralizing plasma IgGs were compared to those of human anti-gp120 MAbs, including 5 bnMAbs (PG9, PG16, VRC01, b12, and 2G12), 2 narrowly neutralizing MAbs (17b and E51), and 3 nonneutralizing MAbs (A32, C11, and 19e). bnMAbs VRC01, 2G12 and b12 had basic pIs (8.1 to >9).
Sajadi2012
(polyclonal antibodies)
-
2G12: Small sized CD4 mimetics (miniCD4s) were engineered. These miniCD4s by themselves are poorly immunogenic and do not induce anti-CD4 antibodies. Stable covalent complexes between miniCD4s and gp120 and gp140 were generated through a site-directed coupling reaction. These complexes were recognized by CD4i antibodies as well as by the HIV co-receptor CCR5 and elicited CD4i antibody responses in rabbits. A panel of MAbs of defined epitope specificities, was used to analyze the antigenic integrity of the covalent complexes using capture ELISA. MAb 2G12 was used to normalize the concentration of gp140 vs gp140-miniCD4 complex.
Martin2011
(mimics, binding affinity)
-
2G12: Sensitivity to neutralization was studied in 107 full-length Env molecular clones from multiple risk groups in various locations in China. Neutralization sensitivity to plasma pools and bNAbs was not correlated. MAbs 2F5 and G12 failed to neutralize almost all viruses in the C/07/08/B'C subtype group. 2F5 was potent in neutralizing viruses in subtype B′ and CRF01_AE, while 2G12, could only neutralize a 6/9 of subtype B′ viruses and none of the CRF01_AE viruses. 23/24 2G12-resistant viruses lacked the glycan at position 295 or 332 or both.
Shang2011
(glycosylation, neutralization, subtype comparisons)
-
2G12: The long-term effect of broadly bNAbs on cell-free HIV particles and their capacity to irreversibly inactivate virus was studied. MPER-specific MAbs potently induced gp120 shedding upon prolonged contact with the virus, rendering neutralization irreversible. The kinetic and thermodynamic requirements of the shedding process were virtually identical to those of neutralization, identifying gp120 shedding as a key process associated with HIV neutralization by MPER bNAbs. Neutralizing and shedding capacity of 7 MPER-, CD4bs- and V3 loop-directed MAbs were assessed against 14 divergent strains. Neutralization with 2G12 was reversible, as 2G12 immediately lost the majority of neutralization activity once access antibody was removed. 2G12 induced 30-60% shedding with 5/14 probed viruses, suggesting that although not a potent shedding inducer, 2G12 can not be considered incapable of inducing shedding.
Ruprecht2011
(neutralization, kinetics)
-
2G12: Circulating HIV-1 virion-immune complexes (ICs), present in approximately 90% of acute subjects were quantified, and the levels and antibody specificity to those in chronic infection were compared. Similar to a nonneutralizing anti-gp41 MAb 7B2, purified plasma IgG from acute HIV-1 subjects bound both infectious and noninfectious virions. This was in contrast to the neutralizing antibody 2G12 MAb that bound predominantly infectious virions.
Liu2011c
(binding affinity)
-
2G12: Gold nanoparticles coated with self-assembled monolayers of synthetic oligomannosides [manno-gold glyconanoparticles (GNPs)], which are present in gp120, bound 2G12 with high affinity and interfered with 2G12/gp120 binding. GNPs coated with a linear tetramannoside could block the 2G12-mediated neutralization of a replication-competent virus under conditions that resemble the ones in which normal serum prevents infection of the target cell.
Marradi2011
(glycosylation, neutralization)
-
2G12: Deglycosylations were introduced into the 24 N-linked glycosylation sites of a R5 env MWS2 cloned from semen. Mutants N156-T158A, N197-S199A, N262-S264A and N410-T412A conferred decreased infectivity and enhanced sensitivity to a series of antibodies and entry inhibitors. Mutant N156-T158A showed enhanced neutralization sensitivity to MAb 17b in the absence of soluble CD4, suggesting that deglycosylation in these sites on gp120 may be beneficial for the exposure of a CD4 induced epitope which only exists in the CD4-liganded form of gp120.
Huang2012
(glycosylation, neutralization)
-
2G12: This study analyzed the neutralization sensitivity of sequential HIV-1 primary isolates during their natural evolution in 5 subtype B and CRF02_AG HIV-1 infected drug naive individuals to 13 anti-HIV-1 MAbs (including this MAb) directed at epitopes in the V2, V3, CD4bd and carbohydrates. Patient viruses evolved to become more sensitive to neutralization by MAbs directed at epitopes at V2, V3 and CDbd, indicating that cross sectional studies are inadequate to define the neutralization spectrum of MAb neutralization with primary HIV-1 isolates.
Haldar2011
(neutralization)
-
2G12: This is a detailed systematic study of the molecular recognition of five synthetic oligomannosides 1–5 in solution by the antibody 2G12 by using ligand-based NMR techniques, specifically saturation transfer difference (STD) NMR spectroscopy and transferred NOE experiments.
Enriquez-Navas2011
(glycosylation, structure)
-
2G12: The sensitivity to PG9 and PG16 of pseudotyped viruses was analysed carrying envelope glycoproteins from the viral quasispecies of three HIV-1 clade CRF01_AE-infected patients. It was confirmed that an acidic residue or a basic residue at position 168 in the V2 loop is a key element determining the sensitivity to PG9 and PG16. In addition, evidence is provided of the involvement of a conserved residue at position 215 of the C2 region in the PG9/PG16 epitopes. B clones were tested against 2G12 MAb recognizing a conformational glycan-dependent epitope on gp120 but 2G12 was not used for the CRF01_AE clones since all of them lacked the N332 residue, which constitutes one of the essential N-glycosylation sites of the 2G12 epitope. 2G12 sensitivity of B clones remained comparable, with only one resistant clone, 5008CL3, which became moderately sensitive.
Thenin2012a
(neutralization)
-
2G12: Given the potential importance of cell-associated virus during mucosal HIV-1 transmission, sensitivity of bNAbs targeting HIV-1 envelope surface unit gp120 (VRCO1, PG16, b12, and 2G12) and transmembrane domain gp41 (4E10 and 2F5) was examined for both cell-free and mDC-mediated infections of TZM-bl and CD4+ T cells. It was reported that higher gp120-bNAb concentrations, but not gp41-directed bNAb concentrations, are required The IC50 and IC90 for anti-gp120–directed bNAb 2G12, were significantly higher for almost all mDC-mediated virus transmission (Lai, NL4-3, Lai/Balenv), compared with cell-free HIV-1 infection.to inhibit mDC-mediated virus spread, compared with cell-free transmission. Only cell-free and mDC-mediated infection of 89.6 virus particles demonstrated no significant IC50 difference against 2G12. 2G12 did not readily bind mDCs in the absence of virus. Around 18% of the mDC–T cell synaptic junctions displayed colocalization of Gag-eGFP VLPs with 2G12. Furthermore, 2G12 did not localize at DC–T cell synaptic junctions in the absence of Gag-eGFP VLPs.
Sagar2012
(neutralization, binding affinity)
-
2G12: To overcome the many limitations of current systems for HIV-1 virus-like particle (VLP) production, a novel strategy was developed to produce HIV-1 VLP using stably transfected Drosophila S2 cells by cotransfecting S2 cells with plasmids encoding an envelope glycoprotein (consensus B or consensus C), a Rev-independent Gag (Pr55) protein, and a Rev protein, along with a pCoBlast selection marker. Except for antigenic epitope PG16, all other broadly neutralizing antigenic epitopes 2G12, b12, VRC01, and 4E10 tested are preserved on spikes of HIV-1 VLP produced by S2 clones.
Yang2012
(assay or method development, neutralization)
-
2G12: In order to increase recognition of CD4 by Env and to elicit stronger neutralizing antibodies against it, two Env probes were produced and tested - monomeric Env was stabilized by pocket filling mutations in the CD4bs (PF2) and trimeric Env was formed by appending trimerization motifs to soluble gp120/gp14. PF2-containing proteins were better recognized by bNMAb against CD4bs and more rapidly elicited neutralizing antibodies against the CD4bs. Trimeric Env, however, elicited a higher neutralization potency that mapped to the V3 region of gp120.
Feng2012
(neutralization)
-
2g12: A way to produce conformationally intact, deglycosylated soluble, cleaved recombinant Env trimers by inhibition of the synthesis of complex N-glycans during Env production, followed by treatment with glycosidases under conditions that preserve Env trimer integrity is described to facilitate crystallography and immunogenicity studies. As expected, the glycan-dependent 2G12 did not bind to the deglycosylated trimers.
Depetris2012
(glycosylation, binding affinity)
-
2G12: The sera of 113 HIV-1 seroconverters from three cohorts were analyzed for binding to a set of well-characterized gp120 core and resurfaced stabilized core (RSC3) protein probes, and their cognate CD4bs knockout mutants. 2G12 bound strongly to RSC3, RSC3/G367R and RSC3 Δ3711, weakly bound to RSC3 Δ3711/P363N, very weakly bound to gp120 core and did not bind to gp120 core D368R.
Lynch2012
(binding affinity)
-
2G12: Sensitivity to bNAbs of primary R5 HIV-1 isolates sequentially obtained before and after AIDS onset was studied. End-stage disease HIV R5 isolates were more sensitive to neutralization by TriMab, an equimolar mix of the IgGb12, 2F5 and 2G12 antibodies, than R5 isolates from the chronic phase. The increased sensitivity correlated with low CD4+ T cell count at time of virus isolation and augmented viral infectivity. Envs from end-stage R5 variants had increased positive surface charge and reduced numbers of potential N-linked glycosylation sites (PNGS). These molecular changes in Env also correlated to sensitivity to neutralization by the individual 2G12 MAb. Molecular modeling suggested that the glycosylation sites lost at end-stage disease are located in close proximity to the 2G12 epitope.
Borggren2011
(glycosylation, neutralization)
-
2G12: To test whether HIV-1 particle maturation alters the conformation of the Env proteins, a sensitive and quantitative imaging-based Ab-binding assay was used to probe the conformations of full-length and cytoplasmic tail (CT) truncated Env proteins on mature and immature HIV-1 particles. Binding of MPER-specific MAb Z13e1 to immature particles was greater than to mature virions and the increase was abolished by truncation of the gp41 CT. Z13e1 bound immature particles approximately 1.5 to 2 times as well as mature particles when the median binding signals were compared indicating that the recognized neutralization-sensitive epitopes undergo conformational masking during HIV-1 particle maturation.
Joyner2011
(binding affinity)
-
2G12: Humoral responses to specific, linear gp41 epitopes were that were already known to be the target of broadly neutralizing antibodies were compared in a cohort of sub-Saharan mother-child pairs. TriMab positive-control Abs (2F5, 2G12, and b12) neutralized all viruses tested: the subtype B laboratory strains SF162 (R5-B) and IIIB (X4-B), and the low-sensitivity subtype C strains, primary isolates DU172 and DU156 (both R5-C). The TriMab control inhibited strain DU156 when all neutralization assays were performed on the DU156 HIV isolate (C-R5) with cord blood specimens from EUN babies.
Diomede2012
(neutralization, mother-to-infant transmission, subtype comparisons)
-
2G12: The possibility to construct a polyepitope B-cell immunogen (TBI-2g12) containing linear mimetics of conformational epitopes and its immunogenic properties was examined. The aim was to select the most active peptide mimetic recognized by MAb 2G12 and to construct the protein immunogen by attaching the selected peptide mimotope VGAFGSFYRLSVLQS to a protein carrier. It was shown that the TBI-2g12 as well as the original TBI induce antibodies, that recognize HIV-1 proteins, TBI protein using ELISA and immunoblotting. Though only anti-TBI-2g12 serum recognized the synthetic peptide mimotope VGAFGSFYRLSVLQS, whereas the antibodies against original TBI don’t recognize it. The neutralization assay demonstrated that serum antibodies of the mice immunized with TBI-2g12 possess virus neutralizing activity suggesting that principal epitope responsible for virus neutralizing activity was formed from VGAFGSFYRLSVLQS peptide in the structure of TBI-2g12 protein.
Karpenko2012
(mimotopes, neutralization)
-
2G12: 162 full-length envelope (env) clones were generated from plasma RNA obtained from 5 HIV-1 Clade B infected mother-infant pairs and their V1-V5 genotypes and phylogeny were extensively characterized. All clones from three infants were resistant to 2G12 and exhibited mutations eliminating one of five PNGS implicated in 2G12 binding. Most maternal clones from these pairs exhibited similar levels of 2G12 resistance, and displayed the corresponding mutations.
Kishko2011
(neutralization, mother-to-infant transmission)
-
2G12: HIV-1 adaptation to neutralization by MAbs VRC01, PG9, PG16 was studied using HIV-1 variants from historic (1985-1989) and contemporary (2003-2006) seroconverters. 2G12 was included for comparison and neutralized 5% of contemporary viruses at IC50 < 1 μ g/ml and 14% at IC50 < 5 μ g/ml. TriMab construct, consisting of MAbs b12, 2F5 and 2G12 in equal concentrations, showed the highest neutralization correlation with 2F5 and little similarity with 2G12.
Euler2011
(neutralization)
-
2G12: The neutralization potency of PG9, PG16, VRC01 and PGV04 was approximately 10-fold greater than that of MAbs b12, 2G12, 2F5 and 4E10.
Falkowska2012
(neutralization)
-
2G12: Neutralizing antibody repertoires of 4 HIV-infected donors with remarkably broad and potent neutralizing responses were probed. 17 new monoclonal antibodies that neutralize broadly across clades were rescued. All MAbs exhibited broad cross-clade neutralizing activity, but several showed exceptional potency. Although 2G12 neutralized 32% of 162 isolates at IC50<50 μg/ml, it was almost 100-fold less potent than several new antibodies PGT 121-123 and 125-128, for which the median antibody concentration required to inhibit HIV activity by 50% or 90% (IC50 and IC90 values) was almost 100-fold lower than that of b12, 2G12 and 4E10.
Walker2011
(neutralization)
-
2G12: Studies were conducted to determine whether differences in immunogenic potential exist between two previously reported primary Env antigens (Clade B primary Env antigens LN40 and B33) with closely related gene sequences and completely different phenotypic features. The B33 Env is resistant to MAb 2G12, while the LN40 Env, having the opposite phenotype of B33, is sensitive to MAb 2G12.
Vaine2011
(neutralization)
-
2G12: HIV-1 subtype C env genes from 19 mother-infant pairs: 10 transmitting in utero (IU) and 9 transmitting intrapartum (IP) were analyzed. A severe genetic bottleneck during transmission was confirmed in all pairs. Compared to the maternal viral population, viruses transmitted IP tended to have shorter variable loops and fewer putative N-linked glycosylation sites than viruses transmitted IU. The pseudotyped viruses displayed some sensitivity to 4E10 and soluble CD4 but were resistant to 2G12, 2F5, and IgG1b12.
Russell2011
(glycosylation, neutralization, mother-to-infant transmission)
-
2G12: The influence of potential N-linked glycosylation site (PNGS) N302 on 2G12 sensitivity was assessed based on chimeric envelope genes created by swapping the V1V2 domains of the two env clones. Both the exchange of the V1V2 domain and the introduction of the PNGS at N302 on the 2G12-sensitive clone induced a significant decrease in sensitivity to 2G12. In contrast, the reverse V1V2 exchange and the removal of the PNGS at N302 on the 2G12-resistant clone increased sensitivity to 2G12, confirming the influence of these regions on 2G12 sensitivity. It suggests that both the V1V2 loop and an additional PNGS in V3 might limit access to the 2G12 epitope.
Chaillon2011
(glycosylation, neutralization, structure)
-
2G12: To elicit 2G12-like Ab response it was shown that Manα1→2Man motif was the primary carbohydrate neutralization determinant of HIV-1 that elicited Abs to the self oligomannose glycans. While 2G12 is known to bind to this motif, the specificity of the mannan immune serum (ΔMnn1: S. cerevisiae deficient in the α1→3 mannosyltransferase gene) seemed narrower than some alternative modes of binding postulated for 2G12. ΔMnn1 immune sera revealed fine carbohydrate specificity to Manα1→2Man units, closely matching that of 2G12. The sera also appeared to tolerate the presence of D1 glucosylation indicating perhaps a somewhat wider degree of monosaccharide or linkage specificity compared to 2G12.
Dunlop2010
(antibody binding site)
-
2G12: The development and characterization of a tier 1 R5 SHIV, termed SHIV-1157ipEL is reported. SHIV-1157ipEL is a chimera of the "early", neutralization-sensitive SHIV-1157ip envelope and the "late", neutralization-resistant engineered backbone of SHIV-1157ipd3N4. Molecular modeling revealed a possible mechanism for the increased neutralization resistance of SHIV-1157ipd3N4 Env: V2 loops hindering access to the CD4 binding site, shown experimentally with NAb b12. Sequence analysis performed of the SHIV-1157ipEL-p showed a loss of N295, a key amino acid residue in the epitope of 2G12 that caused SHIV-1157ipEL to become resistant to 2G12. 2G12 only neutralized SHIV-SF162P4 out of the 4 C clade and 2 B clade SHIV strains tested.
Siddappa2010
(neutralization, vaccine antigen design, subtype comparisons)
-
2G12: Purified MAb 2G12, produced by transient expression in Nicotiana benthamiana using replicating and non-replicating systems based on deleted versions of Cowpea mosaic virus (CPMV) RNA-2, was expressed and characterized based on biochemical properties, in vitro activity and neutralization capabilities. The plant derived purified 2G12 (delRNA-2 + RNA-1 or CPMV-HT) was not as pure as CHO-produced 2G12 (reference standard) although no significant differences were observed between 2G12 produced by delRNA-2 with RNA-1 or by CPMV-HT. Also, 2G12 glycosylation was not greatly affected by the presence of RNA-1 or CPMV-HT. The binding activity of plant derived 2G12 was slightly lower than CHO-produced 2G12 although its neutralization capability was similar to that of CHO-produced 2G12.
Sainsbury2010
(glycosylation, neutralization, binding affinity)
-
2G12: This review discusses current understanding of Env neutralization by antibodies in relation to epitope exposure and how this insight might benefit vaccine design strategies. This MAb is in the list of current MAbs with notable cross-neutralizing activity.
Pantophlet2010
(neutralization, variant cross-reactivity, review)
-
2G12: This review outlines the general structure of the gp160 viral envelope, the dynamics of viral entry, the evolution of humoral response, the mechanisms of viral escape and the characterization of broadly neutralizing Abs. The review discusses the special structure of 2G12 which allows it to overcome the glycan masking strategy that HIV-1 uses to protect itself from antibody recognition. It is noted also that 2G12 can neutralize a significant number of primary isolates from clade B, but is less effective against non-clade B viruses and is not active against most clade C. 2G12 provided protection in macaques against SHIV.
Gonzalez2010
(neutralization, variant cross-reactivity, escape, review)
-
2G12: The expression and characterization of different glycoforms of V3-Fc fusion protein along with its binding to HIV-neutralizing Abs 2G12 and 447-52D was examined. The binding affinity of 2G12 was significantly high for the high-mannose type glycoforms of V3-Fc (V3-Fc-HM, V3-Fc-M9 and the two mutants:N301A and Fc-N297A) following a quick association/dissociation kinetic process, although it was not measurable for the complex type glycoform V3-Fc-CT. The affinity to 2G12 was reduced more by removal of the N-glycan at the N301 site than at the N297 site. Very high affinity to 2G12 was observed for gp120 with extremely slow dissociation rate.
Yang2010a
(glycosylation, binding affinity)
-
2G12: This review discusses recent rational structure-based approaches in HIV vaccine design that helped in understanding the link between Env antigenicity and immunogenicity. This MAb is mentioned in the context of immunogens based on the epitopes recognized by bNAbs. 2G12 adopts an unusual domain exchanged structure to recognize a conserved cluster of oligomannose residues on the outer domain of gp120 and has provided a basis for the design of immunogens to target the HIV-1 glycan shield.
Walker2010a
(neutralization, review)
-
2G12: 37 Indian clade C HIV-1 Env clones obtained at different time points from five patients with recent infection, were studied in neutralization assays for sensitivities to their autologous plasma antibodies and mAbs. All Env variants were resistant to 2G12, except those obtained from IVC-3 patient. This resistance was associated with the absence of N-linked glycosylation site at position 295 at the N-terminal base of V3 loop. The sensitivity of IVC-3 clones was due to the presence of N295, atypical of clade C.
Ringe2010
(neutralization)
-
2G12: This review discusses strategies for design of neutralizing antibody-based vaccines against HIV-1 and recent major advances in the field regarding isolation of potent broadly neutralizing Abs.
Sattentau2010
(review)
-
2G12: The effect of absence and presence of sCD4 on accessibility and binding of HIV-1 gp41 MPER-binding epitopes on CCR5-tropic pseudoviruses from five different clades to the mAbs was studied. The 2G12 N-sites 295, 332, 339, 386, 392 were examined. 2G12 showed high binding affinity to pseudoviruses from clade A (epitope mutant:tWFDIs), clade B (NWFDIT) and clade D (NWFsIT), and very low binding affinity to clade A (NWFDIs), clade B (sWFsIT), clade C (sWFsIT), clade D (NWFsIT) and clade CRF01_AE (NWFDIT) and no binding to clade C (sWFsIT) and clade CRF01_AE (NWFDIs).
Peachman2010a
(variant cross-reactivity, binding affinity, subtype comparisons)
-
2G12: Most of the 34 Env-pseudotyped viruses from HIV-1 CRF01_AE - infected plasma samples collected in China could efficiently infect target cells in the presence of high concentrations of 2G12 MAb. Only 1/34 viruses showed low 2G12 susceptibility and all viruses lacked one or more glycans at positions critical for 2G12 neutralization.
Nie2010
(glycosylation, neutralization)
-
2G12: This review discusses the studies done on poly-reactive antibodies (binding to two different epitopes), and the importance of polyreactivity. Low polyreactivity has been reported for 2G12.
Pluckthun2010
(review, antibody polyreactivity)
-
2G12: A lentiviral vector encoding the heavy and light chains of 2G12 was transduced in the primary human B cells and directed production of 2G12. NOD/SCID/γc mice were transplanted with human hematopoetic stem cells (hu-HSC) transduced with the vector and the animals were inoculated with HIV-1. Mice engrafted with the 2G12-transducted cells displayed a 70-fold reduction in plasma RNA levels and a 200-fold reduction in HIV-1 infected spleen cells compared to control mice, indicating inhibition of in vivo HIV infection by this gene therapy approach.
Joseph2010
-
2G12: This paper shows that a highly neutralization-resistant virus is converted to a neutralization sensitive virus with a rare single mutation D179N in the C-terminal portion of the V2 domain for several antibodies. 2G12, however, did not neutralize any of the mutants tested.
ORourke2010
(neutralization, variant cross-reactivity)
-
2G12: MAb m9 showed superior neutralization potency compared to 2G12 in a TZM-bl assay, where it neutralized all 15 isolates compared to 2G12 that neutralized only 4 clade B isolates but not clade A or C isolates.
Zhang2010
(neutralization)
-
2G12: A side-by-side comparison was performed on the quality of Ab responses in humans elicited by three vaccine studies focusing on Env-specific Abs. Minimal presence of 2G12-like Abs was detected in the three vaccine trials. 17% of sera from the HVTN 203 trial, 0% of sera from the HVTN 041 trial, and 24% of sera from the DP6-001 trial were able to outcompete binding to 2G12 MAb.
Vaine2010
(antibody interactions)
-
2G12: This review focuses on recent vaccine design efforts and investigation of broadly neutralizing Abs and their epitopes to aid in the improvement of immunogen design. NAb epitopes, NAbs response to HIV-1, isolation of novel mAbs, and vaccine-elicited NAb responses in human clinical trials are discussed in this review.
Mascola2010
(review)
-
2G12: Naturally occurring human and experimentally induced murine and rabbit GBV-C E2 Abs were studied for their ability to neutralize diverse HIV-isolates and showed that broadly neutralizing HIV Abs were elicited on immunization of rabbits with GBV-C E2. MAb 2G12 neutralized R5 and dual R5-X4 HIV-1 isolates of subtypes A and B in primary human PBMCs. The TriMAb control including 2G12 did not neutralize the HIV-1 R5 isolate in TZM-bl cells but did in PBMCs.
Mohr2010
(neutralization)
-
2G12: A mathematical framework is designed to determine the number of Abs required to neutralize a single trimer called the stoichiometry of trimer neutralization. 15 different virus antibody combinations divided into five groups based on antibody binding sites were used in the designed model. 2G12 is in a group by itself as it recognizes a carbohydrate-dependent epitope on gp120. The number of 2G12 Abs needed to neutralize a single trimer was estimated as 1 with 97 percent probability.
Magnus2010
-
2G12: BanLec is a lectin isolated from the fruit of bananas that was shown to inhibit HIV-1 isolates of different subtypes and tropisms. Pretreatment of gp120 with BanLec inhibited recognition by 2G12 in a dose-dependent manner, indicating that BanLec inhibits HIV-1 by binding to high-mannose structures also recognized by 2G12.
Swanson2010
-
2G12: Four human anti-phospholipid mAbs were reported to inhibit HIV-1 infection of human PBMC's by binding to monocytes and releasing soluble chemokines. The ability of different anti-phospholid mAbs to inhibit pseudovirus infection was studied. Four out of nine anti-phospholid mAbs inhibited HIV-1 infectivity in PBMC-based virus infection inhibition assay where a mixture of mAbs 2F5, IgG1b12, and 2G12 (TriMab) was used as a positive control.
Moody2010
(neutralization)
-
2G12: A naturally occurring dimeric form of 2G12 was shown to have increased neutralization potency and increased ADCC activity compared to the monomeric form of 2G12. An ADCC-enhancing double mutation improved the ADCC activity of 2G12 monomer more than 2G12 dimer.
Klein2010a
(effector function)
-
2G12: Targeted neutralizing epitopes have been identified based on the change in sensitivity to neutralization due to variations in known immunoepitopes studied in 17 subjects. The glycan removal by N332S mutant from gp120 outer domain decreased the neutralization of gp160 by 2G12. In addition, the N332S mutant escaped neutralization by two patient sera.
Nandi2010
(neutralization, escape)
-
2G12: Molecular modeling was used to construct a 3D model of an anti-gp120 RNA aptamer, B40t77, in complex with gp120. Externally exposed residues of gp120 that participated in stabilizing interaction with the aptamer were mutated. Binding of 2G12 to gp120 was inhibited by B40t77, which is suggested to be due to distant conformational changes of gp120 induced by the aptamer.
Joubert2010
(binding affinity, structure)
-
2G12: A yeast glycosylation mutant was created to expose numerous terminal Man1,2-Man residues. Although the yeast did not bind to 2G12, immunization of rabbits resulted in sera containing Manα1,2-Manα1,2-Man-specific Abs that cross-reacted with Env glycoproteins from HIV-1 subtypes A, B and C.
Luallen2010
(glycosylation, vaccine antigen design)
-
2G12: 2G12 was shown to capture virion particles completely devoid of HIV-1 Env. Virus capture assay was modified with added incubation of virions and MAbs in solution followed by removal of unbound MAbs, which nearly eliminated the Env-independent binding by this Ab. This modification also allowed for relative affinity of 2G12 for virions to be quantified. There was an overall reduction in the efficiency of capture of molecular clones (MC) relative to pseudotyped virions by 2G12. In addition, trimeric JR-FL MC was captured more efficiently by 2G12 than nontrimeric Envs from JR-CSF MC virus.
Leaman2010
(assay or method development, binding affinity)
-
2G12: The role of HIV-1 envelope spike density on the virion and the effect it has on MAb avidity, and neutralization potencies of MAbs presented as different isotypes, are reviewed. Engineering approaches and design of immunogens able to elicit intra-spike cross-linking Abs are discussed.
Klein2010
(review)
-
2G12: 18 unique Env clones of subtype C HIV-1 derived from six African countries and Scotland were tested for their neutralization susceptibility by 2G12. 2G12 neutralized only one of the isolates.
Koh2010a
(neutralization)
-
2G12: Glycoconjugates were designed consisting of four- and eight-valent high-mannose HIV-1 related oligosaccharides clustered onto flexible polyamidoamine (PAMAM) dendrons and subsequently conjugated to well-characterized nontoxic diphtheria toxin mutant CRM197 as a carrier. The multivalent presentation of oligomannoses increased the avidity to 2G12. Antisera of mice and rabbits immunized with the glycoconjugates failed to recognize recombinant HIV-1 proteins.
Kabanova2010
(glycosylation, vaccine antigen design, binding affinity)
-
2G12: The effect of presence and absence of V1 loop was assessed using two approaches: remove V1 loop from the soluble trimeric gp140 construct (ΔV1SF162gp140) and second, substitute the V1 loop on SF162gp140 construct with four different V1 loops from 89.6, YU2, JRFL, and HxB2 (heterologous HIV-1 viruses). Deletion or substitution of V1 loop did not affect neutralization by 2G12 and there was only a small change in binding affinity to 2G12. D368R modification to SF162gp120 did not affect the binding by 2G12, although it abrogated neutralization by 2G12 at lower MAb concentrations.
Ching2010
(neutralization, binding affinity)
-
2G12: A hybrid nonself sugar was designed based on the crystal structure of D-fructose in complex with 2G12 Fab to elicit high 2G12 Ab response based on much enhanced (9 times) affinity of 2G12 for D-fructose compared to D-mannose. Introduction of nonself modifications into the D1 arm of high-mannose sugars led to additional interactions of nonself modifications to the 2G12 binding site resulting in enhanced antigenicity. The nonself glycan enhanced 2G12 binding compared to the self glycan, and the antibodies generated in immunized rabbits cross-reacted with the self glycan present in different conjugates, but did not bind the self D1 glycan motif when present on gp120.
Doores2010c
(glycosylation, binding affinity)
-
2G12: The effect of HIV-1 complement opsonization on 2G12 activity was evaluated in three instances: HIV-1 transcytosis through epithelial cells, HIV-1 attachment on immature monocyte derived dendritic cells (iMDDC), and infectivity of iMDDC. 2G12 was not able to inhibit HIV-1 transcytosis. 2G12 inhibited the attachment of non-opsonised HIV to iMDDC but had no effect on the opsonized HIV-1 attachment. 2G12 was able to inhibit production of both opsonized and non-opsonized HIV-1 in iMDDCs.
Jenabian2010
(complement)
-
2G12: A germ line version of 2G12 was constructed that was not domain exchanged and did not detectably bind to gp120. Introducing increasing number of substitutions to germ line 2G12 resulted in domain exchanged wild type form of this Ab. Only 5-7 crucial substitutions were found necessary to induce considerable domain exchange of germ line 2G12; Ih19, Rh57, Eh75, Rh39, Ah14, Vh84 and Ph113.
Huber2010
(antibody binding site)
-
2G12: Clustering analysis was performed to find patterns of neutralization reactivity for the dataset of 103 patients sera against 20 viruses. The clustering by five MAbs (including 2G12) against the 20 isolates was less statistically robust than that with serum titers, resulting in three clusters for both cases. The membership in an isolate cluster defined by serum titers was compared with its sensitivity to every MAb to understand the relationship of serum and MAb reactivity. Membership in all the three clusters did not correlate with sensitivity to 2G12.
Doria-Rose2010
(neutralization)
-
2G12: The sensitivity of subtype C viruses to lectins GRFT, CV-N and SVN was analysed and compared to that of subtype A and B viruses which showed same sensitivity by all three viruses for all the three lectins. It was also examined whether lectin binding interfered with the access to the 2G12 epitope and there was competition among the compounds for virus capture. GRFT and CV-N inhibited the virus capture more effectively than SVN. Virus capture by 2G12 was inhibited for all three viruses using same amount of lectin concentrations. The results suggested overlap of 2G12 epitope with the binding sites of all the three lectins.
Alexandre2010
(binding affinity)
-
2G12: Addition of bacterial endotoxin (LPS) had no effect on the potency of 2G12 neutralization in TZM-bl assay but addition of LPS in PBMC assay increased neutralization potency of 2G12. Endotoxin contamination was shown to mediate release of antiviral chemokines in PBMCs and is thus suggested to be able to cause false-positive results in PBMC-based neutralization assays.
Geonnotti2010
(neutralization)
-
2G12: In order to overcome problems of the PBMC-based neutralization assay a novel approach was developed utilizing a platform based on Renilla luciferase (LucR) expressing HIV-1 proviral backbone. Env-IMC-LucR reporter viruses expressing HIV-1 envs from different virus strains were incubated with NAbs, such as 2G12, and used to infect donor PBMCs. The inhibition was assessed by measuring virus-encoded LucR activity in the cell lysates. There was a dosage dependent effect of 2G12 on virus infectivity. Variation in sensitivity to 2G12 was observed among different donor PBMCs, and this high variability was suggested to be a real biological effect attributable to use of different donor PBMCs, rather than assay-to-assay variability.
Edmonds2010
(assay or method development, neutralization)
-
2G12: The identity of N-linked glycans from primary isolates of subtypes A, B and C was studied. Results showed highly conserved virus-specific glycan profile devoid of medial Golgi-mediated processing. When mutant viruses with glycosylation site deletions that disrupt the 2G12 epitope were analyzed, there was a modest decrease of Man8-9GlcNAc2 glycans, but the overall profile remained unperturbed. This confirmed the sensitivity of 2G12 for a small subset of Manα1-2Man glycans.
Doores2010b
(glycosylation)
-
2G12: Subtype B HIV-1 variants from historical seroconverters (individuals that seroconverted between 1985 and 1989) were equally sensitive to neutralization by 2G12 as variants isolated from contemporary seroconverters (ndividuals that seroconverted between 2003 and 2006).
Bunnik2010a
(neutralization, dynamics)
-
2G12: 17b was linked with sCD4 and the construct was tested for its neutralization breadth and potency. sCD4-17b showed significantly greater neutralization breadth and potency compared to 2G12, neutralizing 100% of HIV-1 primary isolates of subtypes A, B, C, D, F, CRF01_AE and CRF02_AG, while 2G12 neutralized some isolates of subtypes B and D. Unlike sCD4-17b, 2G12 was not equivalently active against virus particles generated from different producer cell types.
Lagenaur2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: A set of Env variants with deletions in V1/V2 was constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Sensitivity of the evolved ΔV1V2 viruses was evaluated to study accessibility of their neutralization epitopes. 2G12 neutralized and bound to both cleaved and uncleaved ΔV1V2 variants more potently compared to the wild type virus, indicating better accessibility of the 2G12 epitope when the V1V2 domain is deleted.
Bontjer2010
(neutralization, binding affinity)
-
2G12: Five different glycoforms of 2G12, generated in wild type and glycoengineered plants and in Chinese hamster ovary cells, were used to investigate the impact of Ab Fc glycosylation on the antiviral activity of the Ab. All five 2G12 glycoforms had similar binding profiles to cells expressing FcγRI, FcγRIIa or FcγRIIb. In contrast, two glycoforms of 2G12 lacking fucose showed significantly enhanced binding to cells expressing FcγRIIIa, compared to 2G12 glycoforms carrying core fucose. The two non-fucosylated forms of 2G12 also showed stronger antiviral activity against HIV-1 and SIV in ADCVI-assays compared to the fucosylated forms of 2G12.
Forthal2010
(glycosylation, binding affinity)
-
2G12: A single amino acid substitution (I19R) was used to produce a nondomain-exchanged variant of 2G12 (2G12 I19R). 2G12 I19R was able to recognize the same mannose motifs on recombinant gp120, synthetic glycoconjugates, and on Candida albicans as the wild type 2G12. However, 2G12 I19R was unable to recognize the cluster of mannose motifs in the context of HIV envelope trimer, and was unable to neutralize 2G12-sensitive HIV-1 pseudovirions. Crystallographic structure of 2G12 I19R showed that this Ab and the wild type 2G12 have identical Fab binding units but that they display dramatically different juxtapositioning of their variable versus constant regions. These differences lead to remarkably different binding characteristics.
Doores2010a
(glycosylation, neutralization, binding affinity, structure)
-
2g12: Various UV-activatable azido- and iodo-based hydrophobic compounds have been studied for their ability to inactivate HIV-1 virus while preserving their surface antigenic structures. The virus was inactivated by treating it with azido-containing hydrophobic compounds and UV irradiation. The preservation of known neutralizing epitopes on the viral surface of treated virus was tested using the known neutralizing Abs. There was no significant effect on 2g12 recognition and capture of the virus treated with azido-compounds and irradiated with UV for 2 or 15 minutes compared to the untreated virus, hence no damage to its epitopes.
Belanger2010
(binding affinity)
-
2G12: This review discusses recent research done to improve the production, quality, and cross-reactivity of binding Abs, neutralizing Abs, monoclonal Abs with broad neutralizing activity, antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-dependent cell-mediated viral inhibition (ADCVI), and catalytic Abs. Studies focusing on several aspects of BNAb roles in vaccine development, and studies done to better understand the broad binding capacity of BNAbs are reviewed.
Baum2010
(effector function, neutralization, review)
-
2G12: Parent and GnTI (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps) viruses were equally sensitive to neutralization by 2G12, indicating that replacement of complex glycans does not affect the already exposed 2G12 epitope on the silent domain of the virus. Absence of the glycan at residue N301 (N301Q mutant virus) had no effect on 2G12 neutralization. Viruses subjected to removal of outer domain glycans by Endo H treatment were recognized less efficiently by 2G12.
Binley2010
(glycosylation, neutralization)
-
2G12: Pseudoviruses containing Env mutations (V255E, S375N or A433T), which were in vitro selected with the small CD4-mimicking compound NBD-556, showed the same neutralization sensitivities as the wild type virus to 2G12.
Yoshimura2010
(mimics, neutralization)
-
2G12: Neutralizing sensitivity of L669S mutant virus to 2G12 was not significantly different from the neutralizing sensitivity of the wild type virus.
Shen2010
(neutralization)
-
2G12: Neutralization potency of 2G12 was compared to that of HK20 scFv in TZM-based assay using 45 Tier 1 and Tier 2 HIV isolates. 2G12 neutralized 12/45 isolates. In addition, 2G12 was used in TriMab, together with 2F5 and b12, to examine neutralization of 9 clade A, B, C, D and E isolates in PBMC assay. Here, TriMab neutralized 7 isolates with 2 not determined.
Sabin2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: Using a humanized mouse model it was shown that passively transferred 2G12 dimer was more potent than 2G12 monomer at preventing CD4 T cell loss and suppressing increase in viral load in mice challenged with JR-CSF virus. 100µg/ml of combined 2G12 monomer and dimer significantly reduced the severity of HIV-1 infection in mice with high-dose challenge, but this 2G12 dose resulted in escape mutations at the N295 residue. Providing 2G12 dimers continuously at 5-25µg/ml by IgG tumor backpacks in mice resulted in effective protection against HIV-1, while complete escape to 2G12 neutralization was not observed.
Luo2010
(immunoprophylaxis, neutralization, escape, immunotherapy)
-
2G12: B cell depletion in an HIV-1 infected patient using rituximab led to a decline in NAb titers and rising viral load. Recovery of NAb titers resulted in control of viral load, and the newly emerged virus population was examined. The common ancestor of this new viral population showed evidence of positive selection and presence of N339E mutation, which inhibited neutralization by 2G12 fourfold. However, there was no binding competition between patient sera and 2G12.
Huang2010
(antibody interactions, escape)
-
2G12: The role of several N-glycosylation sites in 2G12 binding and neutralization was investigated on Envs of LN40 and B33 strains. Glycans at N295, N332, N386 and N392 were critical for 2G12 binding and neutralization. Substitutions in Envs which affect CD4 binding were also shown to have a strong effect on 2G12 neutralization. These residues were within and proximal to CD4bs but not involved in glycosylation. Increased avidity to CD4 did not correlate with 2G12 sensitivity, indicating that the determinants within CD4bs may act to reorient glycans on gp120.
Duenas-Decamp2010
(antibody binding site, glycosylation, neutralization, kinetics, binding affinity)
-
2G12: Unlike for b12, decreasing neutralization sensitivity during the course of infection was not observed for 2G12 in 15 patients studied. Changes in three amino acid residues (154, 178 and 389) were found to confer resistance to b12, but they did not increase resistance of LAI strain to 2G12 neutralization.
Bunnik2010
(neutralization)
-
2G12: Fusion of CD4 with 2G12 scFv resulted in CD4-scFv2G12 reagent with neutralization potency improved by inclusion of an IgG Fc region and by linkage of CD4 to the heavy chain of 2G12. The resulting CD4hc-IgG12G12 was, like 2G12, expressed as a mixture of monomers and dimers. CD4hc-IgG12G12 dimers showed comparable neutralization potencies with 2G12, and CD4hc-IgG12G12 monomers showed enhanced neutralization potencies. Unlike 2G12, CD4hc-IgG12G12 had the ability to neutralize some clade C HIV-1 strains.
West2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: The specificities and structural analyses of 2G12 binding to Env are reviewed. This review also summarizes data on the evolution of HIV neutralizing Abs, principles of Env immunogen design to elicit broadly neutralizing Abs, and future critical areas of research for development of an Ab-based HIV vaccine.
Hoxie2010
(vaccine antigen design, review)
-
2G12: Three 2G12 heavy chain mutants with multiple germ line amino acid substitutions in the VDJ region were created to investigate the mechanism of domain swapping in 2G12. There were qualitative structural differences between 2G12 mutants and 2G12 wild type, and the mutants failed to neutralize or to capture free virus. Structural analyses revealed that the domain-exchanged configuration of 2G12 was fostered by single or combined effects of 4 amino acid side chains that help stabilize the elbow region (H113). The proline at H113 was not required for the domain swapping capability of 2G12. 2G12-3H6 mutant, which had the whole Vh region exchanged with that of another Ab (3H6), lacked domain swapping capability, indicating that CDR3 and J region are not sufficient to promote Vh domain exchange.
Gach2010
(neutralization, binding affinity, structure)
-
2G12: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 2G12 neutralization activity was compared to the three new broadly neutralizing mAbs. 2G12 did not compete for binding to gp120 with any of the new mAbs. 2G12 neutralized 67% of Tier 1 and 23% of Tier 2 viruses, the neutralization of Tier 2 viruses being inferior to that of the new MAb HJ16. 2G12 rarely neutralized clade C isolates.
Corti2010
(neutralization)
-
2G12: 433 Abs were cloned from HIV envelope-binding memory B cells from 6 patients with broadly neutralizing sera. The Abs had neutralizing activity directed against several epitopes on gp120 and the majority neutralized Tier 1 viruses. Tier-2 neutralization was observed only with mixtures of MAbs, but only at high concentrations. 2G12 was used as a control and it neutralized 4/5 Tier 1 and 4/5 Tier 2 viruses.
Scheid2009
(neutralization)
-
2G12: Exogenous epitope tags were introduced in different parts of three variable regions, V1, V2 and V4, of two HIV isolates, SF162 and SF33. Almost all SF162 and SF33 tagged Envs were as susceptible to neutralization by 2G12 as the wild type, except V4-tagged Envs, which were significantly more resistant to neutralization by this Ab compared to wild type. However, V4-tagged Envs were recognized by 2G12.
Wallace2009
(antibody binding site, neutralization)
-
2G12: This review discusses obstacles to elicitation of protective NAbs, recent data on viral epitopes vulnerable to broadly NAbs, qualitative and quantitative implications of NAb response for vaccine development, and possible future areas of investigation to improve understanding of Env structure and stimulation of appropriate B cell responses.
Stamatatos2009
(review)
-
2G12: The structure and dynamic of the virion spike and the 2G12 epitope are discussed. Challenges to eliciting broadly neutralizing anticarbohydrate response, such as weak protein-carbohydrate interactions and small size of glycan patches for Ab binding, are reviewed. 2G12 domain swapping solution to these problems and the implication of the data for immunogen design are discussed.
Schief2009
(antibody binding site, review)
-
2G12: TZM-bl and PBMC systems were compared to investigate the influence of target cell environment on HIV entry inhibition. The sensitivity of TZM-bl system was confirmed by inhibitory capacity of 2G12, 2F5 and b12. Virus entry increased on addition of polycation additives, but neither concentration nor type of polycation had a significant impact on the inhibitory activity of 2G12. 2G12 was shown to be significantly less active on TZM-bl cells, where it failed to inhibit 12 viruses, while it failed to inhibit 9 viruses in PBMC assay. HIV isolates were less sensitive to inhibition by 2G12, 2F5 and 4E10, with up to 100-fold lower sensitivity in the TZM-bl assay.
Rusert2009
(assay or method development, neutralization)
-
2G12: To examine the antigenicity of a defined Ab epitope on the functional envelope spike, a panel of chimeric viruses engrafted at different positions with the hemagglutinin (HA) epitope tag was constructed. The neutralization sensitivity of the all but three HA-tagged viruses to 2G12 was similar to the neutralization sensitivity of wild type virus to this Ab. The three viruses with HA-tag insertions in the V4 region were more resistant to 2G12 than the wild type virus.
Pantophlet2009
(neutralization)
-
2G12: This review summarizes targets of autologous neutralizing Abs (AnAbs) in early and chronic infections. V1V2 is a frequent target of AnAbs, while V4 and V5 have marginal role and anti-V3 Abs do not contribute to autologous neutralization. In addition to variable regions, C3 is a neutralization target in subtype C viruses, and is thought to interact with V4. gp41 is thought to have marginal effect as a target of AnAbs, with only one study showing 4E10-resistant variants suggesting escape from AnAbs targeting this region. AnAb specificities and sequential development, and their role in preventing superinfection is also reviewed. The relatively high Ab titer required for prevention of superinfection and control of viremia, and the low inhibitory potential of b12, 2F5, 4E10 and 2G12 compared to antiretroviral drugs is discussed.
Moore2009
(autologous responses, review)
-
2G12: This review describes obstacles that have been encountered in the development of an HIV-1 vaccine that induces broadly neutralizing Abs, and unusual features of existing broadly neutralizing Abs, such as 2G12. Importance of identification and characterization of new epitopes, and of B-cell stimulation, is discussed.
Montefiori2009
(review)
-
2G12: An overview of the different expression strategies to over produce HIV neutralizing Abs, including 2G12, in plants. The attention is specially focused on expression strategies of Nef protein.
Marusic2009
(review)
-
2G12: Env clones of 6 out of 12 viruses were shown to be highly sensitive to neutralization by 2G12 in PBMC assay but were not inhibited by 2G12 in TZM-bl assay. All 6 envelopes carried a mutation in the core epitope of 2G12. Viruses from patients receiving passive immunization with 2G12 were sensitive to 2G12 both in vivo and in PBMC assay. Upon emergence of 2G12 resistant viruses in vivo, the viruses were shown resistant to neutralization by 2G12 in PBMC assay. The study suggests that TZM-bl assay can fail to detect neutralizing activity of in vivo relevance but may be more prone to detect epitope mismatches. Causes of the observed differences between the PBMC and TZM-bl assays were due to virus producer cells and target cells, that could influence virus entry inhibition.
Mann2009
(assay or method development, neutralization)
-
2G12: NAb specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. The integrity and specificity of gp120 beads in adsorption assay were validated by their ability to adsorb binding activity of 2G12. gp120 point mutation D368R was used to screen the sera for CD4bs- Abs, and it was shown that this mutant could adsorb binding activity of 2G12. To test for presence of coreceptor binding region MAbs in sera, gp120 I420 mutant was used. This mutant was recognized by 2G12 at equal levels as the wild type, and it could adsorb binding activity of 2G12 in adsorption assay. In some of the broadly neutralizing sera, the gp120-directed neutralization was mapped to CD4bs. Some sera were positive for NAbs against coreceptor binding region. A subset of sera also contained NAbs directed against MPER.
Li2009c
(assay or method development)
-
2G12: 2G12 domain swapping mode of epitope recognition is reviewed in detail. The review also summarizes on how different modes of Ab binding and recognition are used to overcome viral evasion tactics and how this knowledge may be used to re-elicit responses in vivo.
Kwong2009a
(antibody binding site, review)
-
2G12: The review discusses the implications of HIV-1 diversity on vaccine design and induction of neutralizing Abs, and possible novel approaches for rational vaccine design that can enhance coverage of HIV diversity. Patterns of within-clade and between-clade diversity in core epitopes of known potent neutralizing Abs, including 2G12, is displayed.
Korber2009
(review)
-
2G12: 2G12 alone was not able to trigger complement-mediated lysis (CML) of 93BR020 and 92UG037 strains, however, it did so in combination with 4E10. Lysis experiments of viruses from three donors showed that 2G12 in combination with allotype-specific Abs Cw4 or Cw7 significantly increased CML. 2G12 in combination with Abs against HLA A1 resulted in significant reduction in CML.
Hildgartner2009
(complement)
-
2G12: The effect of continuous 2G12 infusion on protection from infection and on viral load is reviewed.
Haigwood2009
(immunoprophylaxis, review)
-
2G12: FcγR-mediated inhibition and neutralization of HIV by 2G12 and other MAbs is reviewed. The review also summarizes the role of ADCC and ADCVI Abs on HIV infection inhibition and neutralization.
Forthal2009
(review)
-
2G12: A set of Env variants with deletions in V1/V2 were constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Most variants were found more sensitive to neutralization by 2G12 than the wild type, indicating that deletion of V1/V2 increases 2G12 epitope accessibility.
Bontjer2009
(antibody binding site, neutralization)
-
2G12: This review summarizes novel approaches to mapping broad neutralizing activities in sera and novel technologies for targeted MAb retrieval.
Binley2009
(assay or method development, review)
-
2G12: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 retained strong reactivity with 2G12. Memory B cells were selected that bound to RSC3 and full IgG mAbs were expressed. Binding profiles of the three newly detected mAbs (VRC1, VRC2 and VRC3) were compared to binding profile of 2G12.
Wu2010
(binding affinity)
-
2G12: Glycosylation patterns of HIV-1 were altered using different glycosidase inhibitors or a mutant cell line. Recombinant production of gp120 in the presence of kifunensine resulted in increased neutralization by 2G12, while swainsonine and NB-DNJ treatment resulted in neutralization similar to the wild type.
Doores2010
(glycosylation, neutralization)
-
2G12: In 25% of cases, the broad and potent neutralizing activity of sera from elite neutralizers displayed critical correlation to the N-linked glycosylation at position 332 of HIV-1. Although this N-linked glycan is important for formation of the 2G12 epitope, none of the donor sera inhibited 2G12 binding to gp120, indicating presence of NAbs distinct of 2G12. Unlike PG9 and PG16, 2G12 neutralized kifunensine-treated pseudoviruses with similar potency as wild type pseudoviruses.
Walker2010
(glycosylation, neutralization, binding affinity)
-
2G12: Ab gene divergence analyses found that 2G12 Ab was significantly more divergent from the closest germline Abs than were hmAbs against other viruses. Germline-like 2G12 was constructed in a scFv format. It was shown that germline-like 2G12 did not bind to recombinant gp140 although the corresponding mature 2G12 showed binding.
Xiao2009
(binding affinity, antibody sequence)
-
2G12: Patient sera from 13 HIV controllers and 75 chronic viremic patients were tested for the ability to block binding of 2G12 to Env JRFL gp140 oligomers. There was no difference observed between the controllers and chronic viremic patients. The NAb response was significantly lower in controllers, while ADCC was detected in all controllers but in only 40% of viremic patients.
Lambotte2009
(elite controllers and/or long-term non-progressors, neutralization)
-
2G12: One functional Env clone from each of 10 HIV-1 infected seroconverting individuals from India were analyzed for their sensitivity to MAbs and plasma pools of subtypes B, C and D. All 10 Envs were resistant to 2G12, and the resistance was associated with the absence of a PNLG at position 295. HIVIG neutralized all 10 Envs, and the Envs were most sensitive to neutralization by subtype C pool, followed by subtype D and B pools, respectively. Amino acid signature patterns that associated with neutralization clusters were found. Signature patterns included PNLG at positions 295, 392 and 448, which participate in the 2G12 epitope.
Kulkarni2009
(glycosylation, neutralization, acute/early infection)
-
2G12: Combinations of loop alternations, filling hydrophobic pockets (F-mutations) and introduction of inter-domain cysteine pairs (D-mutations) were used to construct four immunogens with stabilized gp120 core. Modified truncations of the V1V2 and the V3 loop had no impact on 2G12 binding. However, introduction of stabilizing F and D mutations in one case slightly reduced 2G12 affinity and in other two cases slightly increased it.
Dey2009
(binding affinity)
-
2G12: A review about the in vivo efficacy of 2G12 and other MAbs against HIV-1, and about inhibition of HIV-1 infection by Ab fragments Fab, scFv and engineered human Ab variable domains or "domain antibodies" (dAbs).
Chen2009b
(neutralization, immunotherapy, review)
-
2G12: Env derivatives from R3A TA1 virus with eliminated V1 and V2 regions, truncated V3, and deleted cleavage, fusion, and interhelical domains were able to bind 2G12. A membrane anchored variant of this outer domain glycoprotein was also shown to bind to 2G12. Truncations of the β20-β21 hairpin increased reactivity with 2G12. Replacement of the central 20 amino acids of the V3 loop with a basic hexapeptide further significantly increased binding to 2G12.
Wu2009a
(binding affinity)
-
2G12: During purification of 2G12 from mammalian cells, two forms of 2G12 were discovered, a monomeric and a dimeric form. The 2G12 dimer had an average increased potency of 82-fold compared to the monomer and was able to neutralize three out of 20 strains not neutralized by the monomer. Clade C strains were resistant to neutralization by both 2G12 dimer and monomer. A dimeric form of 2G12 was constructed that was more potent in neutralization of 2G12-sensitive strains than the monomeric form. There was no significant difference observed in binding of 2G12 dimers and monomers to gp120.
West2009
(neutralization, kinetics, binding affinity)
-
2G12: 2G12 neutralization breadth and potency was compared to that of two broadly neutralizing Abs PG9 and PG16 in a panel of 162 multi-clade viruses. 2G12 exhibited lower neutralization potency than PG9 and PG16. 2G12 bound with high affinity to both monomeric gp120 and trimeric Env. Binding of 2G12 to Endo H and mock treated gp120 was determined.
Walker2009a
(neutralization, variant cross-reactivity, binding affinity)
-
2G12: NL4.3 virus was cultured with cyclotriazadisulfonamide (CADA) and CADA-resistant virus was selected. 2G12 MAb showed a slightly higher neutralizing potency against the CADA-resistant virus compared to wildtype. The mutations in CADA-resistant virus are suggested to stabilize the conformation of gp120 and reduce glycosylation.
Vermeire2009
(neutralization)
-
2G12: Glyco-engineered tobacco plants were used for efficient expression of recombinant 2G12 with quantitative β1,4-galactosylation (AA structure). Antigen binding capacity of 2G12 glycoforms compared to CHO-derived 2G12 was 115-140%. Neutralization activity of fully galactosylated 2G12 was more than 3 times higher than that of other plant-derived glycoforms and CHO-derived 2G12.
Strasser2009
(neutralization, binding affinity)
-
2G12: An analytical selection algorithm and a reduced virus screening panel were created for assessment of serum neutralizing activity. It is suggested that selection of pseudoviruses for neutralization assays should focus on the overall resistance profile of the pseudovirus and against MAbs b12, 4E10, 2F5 and 2G12. Neutralization profiles of all viruses used for screenings were determined for 2G12.
Simek2009
(neutralization)
-
2G12: Substantial increase in neutralization potency (58-fold) of 2G12 was observed in cells expressing FcγRI against HIV 6535.3 virus strain while there was no effect on the neutralization potency of this Ab against QH0692 strain. With virus SC422661.8, FcγRIIa and FcγRIIb impaired the neutralizing activity of 2G12, suggesting possible infection enhancement.
Perez2009
(enhancing activity, neutralization)
-
2G12: Aqueous two-phase partition system (ATPS) was used to successfully separate 2G12 from unclarified tobacco extract with a yield of 85%. ATPS was successfully combined with affinity chromatography and yielded Ab was stable without any major contaminating proteins or degraded Ab variants.
Platis2009a
(assay or method development)
-
2G12: Δ49-12a, a mutant virus derived from an in-vitro passaged virus with four residues removed from the V3 stem, was shown to be completely resistant to CCR5 inhibitors but was 3-fold more sensitive to neutralization by 2G12 compared to the parental R3A virus. TA1, a mutant with a 15 amino acid deletion of the distal half of V3, was resistant to neutralization by 2G12.
Nolan2009
(neutralization)
-
2G12: Swarm analysis of viruses from one patient resulted in isolation of several different clones with different neutralization sensitivities against four HIV-1 positive sera. None of the clones were sensitive to neutralization by 2G12.
ORourke2009
(neutralization, acute/early infection)
-
2G12: Binding of 2G12 to gp120 was not inhibited by YZ23, an Ab derived from mice immunized with eletcrophilic analogs of gp120 (E-gp120), indicating no overlap of these MAb epitopes.
Nishiyama2009
-
2G12: Binding of 2G12 to various lipid antigens was studied. 2G12 did not bind to any lipids.
Matyas2009
-
2G12: There was no association between 2G12 Abs and anticardiolipin in serum samples from slow progressors.
Martinez2009
(autoantibody or autoimmunity)
-
2G12: By manipulation of the glycosylation machinery of S. cerevisiae a heavily glycosylated yeast protein, Pst1, was identified, that presents closely arrayed N-glycans. Pst1 produced in TM yeast bound 2G12 with high affinity and was able to inhibit 2G12 binding to gp120 more efficiently than a heterologous gp120 from the same subtype. Pst1 was also able to inhibit 2G12 neutralization of HxB and SF162 Env.
Luallen2009
(antibody binding site, glycosylation, neutralization, kinetics, binding affinity)
-
2G12: Subtype A gp140 SOSIP trimers bound to 2G12. Sera from rabbits immunized with SOSIP gp140 and gp120 were unable to capture pseudovirions of the homologous virus by 2G12. 2G12 was unable to bind to the 295 N/A mutant of the virus.
Kang2009
-
2G12: Five rhesus macaques were intravenously treated with 40mg/kg 2G12, which resulted in a high 2G12 serum concentration, and challenged with SHIV SF162P3. Three animals were protected against infection. One animal showed delayed and lower peak viremia compared to controls. Sequence analysis of one of the infected animals showed presence of T388A mutation disrupting the N-glycosylation consistent with escape. Thus, 2G12 can offer protection at relatively low titers, where a titer of 1:1 was sufficient to protect 60% of animals against infection. Vaginal concentrations of 2G12 and b12 were similar when compared in 3 animals, and thus unlikely to contribute to protection differences between the two MAbs.
Hessell2009
(glycosylation, neutralization, escape, immunotherapy, rate of progression)
-
2G12: Ten new non-neutralizing, cross-reactive mAbs were found in immunized mice. 2G12 only reacted with a subset of different Env subtypes tested. 2G12 also reacted with cells expressing A1.con, B.con, B_17779 and B_MN Envs. None of the new mAbs could bind free virus particles while 2G12 did. Binding of 2G12 to B_JRFL oligomer was not blocked by any of the newly detected mAbs.
Gao2009
(variant cross-reactivity)
-
2G12: The heavy and light chains of 2G12 were expressed in transgenic tobacco plants. The accumulation of the Ab chains was increased 2-3-fold by elastin-like peptide (ELP) fusion in both leaves and seeds of the plant. The quality of leaf-derived Abs was comparable to 2G12 generated in CHO cells, and the presence of ELP did not affect N-glycan processing nor intracellular trafficking. Plant-derived 2G12 lacking ELP was more efficient in neutralizing HIV-1 than CHO-2G12, but the fusion of ELP to either of the Ab chains significantly reduced the neutralization efficacy.
Floss2009
(neutralization, kinetics, binding affinity)
-
2G12: An international collaboration (NeutNet) was organized to compare the performance of a wide variety of HIV-1 neutralization assays performed in different laboratories. Four neutralizing agents were evaluated: 4E10, 447-52D, sCD4 and TriMab (equal mixture of 2F5, 2G12 and b12). For TriMab, the mean IC50 values were always lower in the pseudovirus assays than in virus infectivity assays. In general, there were clear differences in assay sensitivities that were dependent on both the neutralizing agent and the virus. No single assay was capable of detecting the entire spectrum of neutralizing activities.
Fenyo2009
(assay or method development, neutralization)
-
2G12: Gene encoding gp140 was fused with three trimerization motifs, T4F, GCN and ATC. gp140, gp140(-)(with mutations in the furin-cleavage site), gp140(-)T4F and gp140(-)GCN bound 2G12 as well, or better than, gp120. gp140(-)ATC bound 2G12 less strongly than gp120.
Du2009
(binding affinity)
-
2G12: Four groups of Abs were detected in a CRF02_AG infected patient directed against mimotopes of MPER, V3, C1 and LLP2. Out of four pseudoviruses from 4 different time points of infection, only one showed moderate susceptibility to 2G12.
Dieltjens2009
(neutralization)
-
2G12: A phylogenetic analysis of gp120 evolution was performed in patients with different patterns of disease progression. In the LNTP patient group, and in 2 NPs, many N-linked glycosylation sites were shown to be under positive selection and exposed on the surface, indicating that Abs binding close to or to 2G12 binding site exert selective pressure on the viral surface in some patients.
Canducci2009
(glycosylation, rate of progression)
-
2G12: Neutralization profiles of cloned Envs derived from recent heterosexual infections by subtypes A, C, D, and A/D from Kenya were determined. The transmitted env variants were generally resistant to neutralization by 2G12, as only 4/31 variants were neutralized by this Ab. These were also the only variants that maintained all five PNGS within the 2G12 epitope.
Blish2009
(neutralization, acute/early infection)
-
2G12: This report investigated whether mannose removal alters gp120 immunogenicity in mice. Approximately 55 mannose residues were removed from gp120 by mannosidase digestion creating D-gp120 for immunization. 2G12 was unable to bind to D-gp120, indicating that 2G12 epitope was eliminated and that the mannosidase digestion was functional.
Banerjee2009
(glycosylation, binding affinity)
-
2G12: HIV-1 variants derived from 5 patients at different timepoints during chronic infection were analysed for their sensitivity to neutralization by b12, 2G12, 2F5 and 4E10. In four of the patients, almost all variants from all time points were resistant to neutralization by 2G12. In two of these patients, resistance to neutralization coincided with the absence of N-linked glycans at position 339 at all time points. In one patient, resistance to neutralization by 2G12 correlated with absence of N-linked glycans at positions 295, 332 and/or 339, and in the second patient, resistance correlated with absence of glycans at positions 295, 339, 386, and/or 339. In the fifth patient, early viruses were sensitive to neutralization by 2G12, but late variants were resistant, which coincided with the loss of N-linked glycans at either 386 or 392 positions.
Bunnik2009
(glycosylation, neutralization, escape)
-
2G12: 2G12 neutralized infection of PBLs with various HIV-1 strains with high potency. However, 2G12 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including 2G12, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs.
Chomont2008
(neutralization)
-
2G12: 5 loop structures surrounding the CD4 binding site in the gp120 liganded conformation were identified that may protect gp120 from Abs. Loops A, B, C and E were located in the C2, C3, C4 and C5 regions respectively, and loop D was situated in the V5 region. Binding of 2G12 to gp120 was unaffected by loop deletions, as this Ab bound equally to HIV-1 IIIB wild type and its loop B deletion mutant, and to HIV-1 89.6 wild type and its loop C deletion mutant.
Berkower2008
(binding affinity)
-
2G12: A reference panel of recently transmitted Tier 2 HIV-1 subtype B envelope viruses was developed representing a broad spectrum of genetic diversity and neutralization sensitivity. The panel includes viruses derived from male-to-male, female-to-male, and male-to-female sexual transmissions, and CCR5 as well as CXCR4 using viruses. The envelopes displayed varying degrees of neutralization sensitivity to 2G12, with 11 of 19 envelopes sensitive to neutralization by this Ab.
Schweighardt2007
(assay or method development, neutralization)
-
2G12: Pre-treatment of gp120 with 2G12 strongly inhibited induction of IL-10, indicating that interaction between gp120 and a mannose C-type lectin receptor is a critical trigger for IL-10 induction.
Shan2007
-
2G12: Modeling of protein-protein interaction based on the gp120 crystal structure, X-ray crystal structure of 2G12 and its complexes with glycans, suggested that the glycans attached to N295 and N302 from the V3 loop are the two most likely involved in the conformational epitope of 2G12.
Sirois2007
(review, structure)
-
2G12: A chimeric protein entry inhibitor, L5, was designed consisting of an allosteric peptide inhibitor 12p1 and a carbohydrate-binding protein cyanovirin (CNV) connected via a flexible linker. The L5 chimera inhibited 2G12-gp120 interaction, as did CNV alone, indicating that the chimera has the high affinity binding property of the CNV molecule.
McFadden2007
-
2G12: This review summarizes data on possible vaccine targets for elicitation of neutralizing Abs and discusses whether it is more practical to design a clade-specific than a clade-generic HIV-1 vaccine. Development of a neutralizing Ab response in HIV-1 infected individuals is reviewed, including data that show no apparent division of different HIV-1 subtypes into clade-related neutralization groups. Also, a summary of the neutralizing activity of MAb 2G12 in different HIV-1 clades is provided.
McKnight2007
(variant cross-reactivity, review)
-
2G12: HIV-1 passaged in the presence of chloroquine was observed to have lost two glycosylation sites important for 2G12 binding, at positions 332 and 397 in the gp120 region, indicating that the drug can alter the immunogenic properties of gp120.
Naarding2007
-
2G12: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 2G12 structure and binding to HIV-1 envelope and current strategies to develop versions of the Env spike with functional trimer properties for elicitation of broadly neutralizing Abs, such as 2G12, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed.
Phogat2007
(review)
-
2G12: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including 2G12 MAb, in vivo and in vitro activity of neutralizing Abs, the importance and downfalls of non-neutralizing Abs and antibodies that mediate antibody-dependent cellular cytotoxicity and the complement system, and summarizes data on areas that need future investigation on Ab-mediated immune control.
Huber2007
(review)
-
2G12: A new high throughput method was developed for neutralization analyses of HIV-1 env genes by adding cytomegalovirus (CMV) immediate enhancer/promoter to the 5' end of the HIV-1 rev/env gene PCR products. The PCR method eliminates cloning, transformation, and plasmid DNA preparation steps in the generation of HIV-1 pseudovirions and allows for sufficient amounts of pseudovirions to be obtained for a large number of neutralization assays. Pseudovirions generated with the PCR method showed similar sensitivity to 2G12 Ab, indicating that the neutralization properties are not altered by the new method.
Kirchherr2007
(assay or method development, neutralization)
-
2G12: 2G12 structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit 2G12-like Abs, are reviewed in detail.
Lin2007
(vaccine antigen design, review, structure)
-
2G12: This review summarizes 2G12Ab epitope, properties and neutralization activity. 2G12 use in passive immunization studies in primates and possible mechanisms explaining protection against infection are discussed.
Kramer2007
(immunotherapy, review)
-
2G12: gp120 proteins were developed with double mutation T257S+S375W, which alters the cavity at the epicenter of the CD4 binding region, and used to immunize rabbits. The ability of rabbit sera to affect binding of CD4 to unmodified gp120 proteins was tested. CD4 binding to gp120 was unaffected by 2G12.
Dey2007a
(antibody binding site)
-
2G12: The various effects that neutralizing and non-neutralizing anti-envelope Abs have on HIV infection are reviewed, such as Ab-mediated complement activation and Fc-receptor mediated activities, that both can, through various mechanisms, increase and decrease the infectivity of the virus. The importance of these mechanisms in vaccine design is discussed. The unusual features of the 2G12 MAb, and its neutralization capacities, are described.
Willey2008
(neutralization, review)
-
2G12: Current insights into CTLs and NAbs, and their possible protective mechanisms against establishment of persistent HIV/SIV infection are discussed. Pre- and post-infection sterile and non-sterile protection of NAbs against viral challenge, and potential role of NAbs in antibody-mediated antigen presentation in modification of cellular immunity, are reviewed. Use of 2G12 in immunization experiments and its in vivo anti-viral activity in suppression of viral rebound in HIV-1 infected humans undergoing structured treatment interruptions are described.
Yamamoto2008
(immunotherapy, supervised treatment interruptions (STI), review)
-
2G12: A yeast strain was produced (TM) with a deletion of genes encoding two key carbohydrate processing enzymes, Och1 and Mnn1, that resulted in efficient recognition of the TM yeast by 2G12 MAb. Four heavily glycosylated yeast proteins were isolated that supported 2G12 binding. Removal of high-mannose-type N-linked carbohydrates from the proteins resulted in loss of 2G12 recognition. Sera from rabbits immunized with TM yeast cells contained Abs that could cross-react with HIV-1 gp120 and that recognized a variety of clade B, C and SIV gp120 proteins. Like 2G12, binding of these Abs to Env proteins was abrogated by removal of N-linked high mannose glycans. The elicited Abs had 50-100-fold lower gp120 binding activity than 2G12, and the antiserum recognized a larger variety of mannose-dependent epitopes. There was no observed neutralizing activity of the sera. The results indicate that immunizations with TM yeast can elicit 2G12-like Abs.
Luallen2008
(vaccine antigen design)
-
2G12: A mathematical model was developed and used to derive transmitted or founder Env sequences from individuals with acute HIV-1 subtype B infection. All of the transmitted or early founder Envs were sensitive to neutralization by 2G12.
Keele2008
(neutralization, acute/early infection)
-
2G12: This review summarizes the obstacles that stand in the way of making a successful preventive HIV-1 vaccine, such as masked or transiently expressed Ab epitopes, polyclonal B-cell class switching, and inefficient, late, and not sufficiently robust mucosal IgA and IgG responses. Possible reasons why HIV-1 envelope constructs expressing 2G12 epitope fail to induce broadly neutralizing Abs are discussed.
Haynes2008
(vaccine antigen design, review)
-
2G12: Transmission of HIV-1 by immature and mature DCs to CD4+ T lymphocytes was significantly higher for CXCR4- than for CCR5-tropic strains. In addition, preneutralization of X4 virus with 2G12 prior to capture efficiently blocked transmission to 36%, while transmission of R5 was blocked to 63%, indicating that 2G12 treatment results in more efficient transfer of X4 than of R5 HIV-1.
vanMontfort2008
(co-receptor, neutralization, dendritic cells)
-
2G12: 2G12 did not neutralize a clade C SHIV strain in the TZM-bl based assay.
Zhang2008
(neutralization)
-
2G12: Sera from both gp120 DNA prime-protein boost immunized rabbits and from protein-only immunized rabbits did not compete for binding to 2G12, indicating no elicitation of 2G12-like Abs by either of the immunization regimens.
Vaine2008
(vaccine antigen design)
-
2G12: An R5 HIV variant, in contrast to its parental virus, was shown to infect T-cell lines expressing low levels of cell surface CCR5 and to infect cells in the absence of CD4. The variant was neutralized less efficiently by 2G12 than the parental virus, indicating conformational changes in gp120. These properties of the mutant virus were determined by alternations in gp41.
Taylor2008
(co-receptor, neutralization)
-
2G12: In order to assess whether small molecule CCR5 inhibitor resistant viruses were more sensitive to neutralization by NAbs, two escape mutant viruses, CC101.19 and D1/85.16, were tested for their sensitivity to neutralization by 2G12, compared to the sensitivity of CC1/85 parental isolate and the CCcon.19 control isolate. The CC101.19 escape mutant has 4 sequence changes in V3 while the D1/85.16 has no sequence changes in V3 and relies on other sequence changes for its resistance. D1/85.16, but not CC101.19 escape variant, was markedly more sensitive to neutralization by 2G12 (approx. 50-fold). As 2G12 had no significantly higher affinity for gp120 from D1/85.16, the increased sensitivity of this virus is most likely due to alternation in the conformation or accessibility of the 2G12 epitope on its Env trimer. Overall, the study suggests that CCR5 inhibitor-resistant viruses are likely to be somewhat more sensitive to neutralization than their parental viruses.
Pugach2008
(co-receptor, neutralization, escape, binding affinity)
-
2G12: The sensitivity of R5 envelopes derived from several patients and several tissue sites, including brain tissue, lymph nodes, blood, and semen, was tested against a range of inhibitors and Abs targeting CD4, CCR5, and various sites on the HIV envelope. All but one envelopes from brain tissue were macrophage-tropic while none of the envelopes from the lymph nodes were macrophage-tropic. Macrophage-tropic envelopes were also less frequent in blood and semen. There was a clear variation in sensitivity to 2G12, where most envelopes were sensitive, while some were resistant to neutralization by this Ab. There was a significant correlation between increased envelope macrophage-tropism and decreased 2G12 sensitivity. It is suggested that the macrophage-tropic brain variants are less protected by glycosylation due to absence of Abs in the brain, thus lacking N-glycosylation sites critical for 2G12 neutralization. Three of nine brain envelopes were resistant to 2G12, while only one of nine lymph node envelopes were resistant to 2G12.
Peters2008a
(antibody binding site, neutralization)
-
2G12: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 2G12 was used as control in neutralization assays, and was able to neutralize JR-FL and SF162 isolates, as well as a chimeric SF162 variant with a JR-FL-like V3 sequence.
Patel2008
(neutralization)
-
2G12: Contemporaneous biological clones of HIV-1 were isolated from plasma of chronically infected patients and tested for their functional properties. The clones showed striking functional diversity both within and among patients, including differences in infectivity and sensitivity to inhibition by 2G12. There was no correlation between clonal virus infectivity and sensitivity to 2G12 inhibition, indicating that these properties are dissociable. The sensitivity to 2G12 inhibition was, however, a property shared by viruses from a given patient, suggesting that the genetic determinants that define this sensitivity may lie in regions that are not necessarily subject to extensive diversity.
Nora2008
(neutralization)
-
2G12: A peptide 2G12.1, that binds to 2G12, was derived by screening of phage-displayed peptide libraries with 2G12. Comparison of the crystal structure of the Fab 2G12 bound to 2G12.1 peptide, and 2G12 bound to carbohydrate, revealed that 2G12 binding to peptide and carbohydrate occurs through different Ab interactions. The 2G12.1 peptide occupied a site different from, but adjacent to, the primary carbohydrate binding site on 2G12. Thus, this does not support structural mimicry of the peptide to the native carbohydrate epitope on gp120. In addition, the 2G12.1 peptide was not an immunogenic mimic of the 2G12 epitope either, since the sera from mice immunized with the peptide did not bind gp120.
Menendez2008
(mimics, structure)
-
2G12: Maize was evaluated as a potential inexpensive large-scale production system for therapeutic antibodies against HIV. 2G12 was expressed in maize endosperm. In vitro cell assays demonstrated that the HIV-neutralizing properties of the maize-produced 2G12 MAb were equivalent to those of Chinese hamster ovary cell-derived MAb 2G12.
Rademacher2008
-
2G12: Neutralization susceptibility of CRF01_AE Env-recombinant viruses, derived from blood samples of Thai HIV-1 infected patients in 2006, was tested to 2G12. Most of the 35 viruses tested replicated efficiently in the presence of 2G12, in spite of highly conserved PNLG sites recognized by this Ab, indicating that CRF01_AE is not susceptible to neutralization by 2G12. These results suggest that the protein structure , including conformation of the CD4 binding domain, may somehow be different between CRF01_AE and subtype B Env gp120.
Utachee2009
(neutralization)
-
2G12: Concentrations of neutralizing Abs in long-term non-progressors (LNTPs) were significantly higher than the concentrations in asymptomatic subjects and subjects with AIDS, with no statistically significant difference between the two latter groups. Amino acid substitutions in the 2G12 epitope were found in both asymptomatic subjects and subjects with AIDS, while no such mutations were found among LNTPs. Eight different mutations were found at five N-glycosylation linked sites: 295V/T/D/K, 297I, 332E. 334N, and 386D. The mutation rates of the conserved 2G12 neutralization epitopes were significantly different among LNTPs, asymptomatic patients, and patients with AIDS.
Wang2008
(escape, rate of progression)
-
2G12: Synergy of 2F5 with MAbs 2G12, D5, and peptide C34 was examined. 2G12 exhibited synergy in inhibition of HIV-1 89.6 with MAb 2F5. 2G12 was not as synergistic when combined with D5 as 2F5 was.
Hrin2008
(antibody interactions)
-
2G12: A series of peptide conjugates were constructed via click reaction of both aryl and alkyl acetylenes with an internally incorporated azidoproline 6 derived from parent peptide RINNIPWSEAMM. Many of these conjugates exhibited increase in both affinity for gp120 and inhibition potencies at both the CD4 and coreceptor binding sites. None of the high affinity peptides inhibited the interactions of YU2 gp120 with 2G12 Ab. The aromatic, hydrophobic, and steric features in the residue 6 side-chain were found important for the increased affinity and inhibition of the high-affinity peptides.
Gopi2008
-
2G12: Three constructs of the outer domain (OD) of gp120 of subtype C, fused with Fc, were generated for immunization of mice: OD(DL3)-Fc (has 29 residues from the center of the V3 loop removed), OD(2F5)-Fc (has the same deletion reconstructed to contain the sequence of 2F5 epitope), and the parental OD-Fc molecule. All OD variants contained substitutions at residues 295 and 394 that reintroduced the 2G12 epitope into the used sequence. All three OD-variants reacted with 2G12, indicating that the isolated outer domain is conformationally immobile. Despite the presence of the 2G12 epitope, none of the sera from mice immunized with the three OD-constructs showed 2G12-like reactivity.
Chen2008a
(vaccine antigen design)
-
2G12: The goal of the study was to measure NAb responses in patients infected with HIV-1 prevalent subtypes in China. g160 genes from plasma samples were used to establish a pseudovirus-based neutralization assay. 2G12 neutralized 33% of subtype B clones but not subtype BC and AE clones.
Chong2008
(neutralization, subtype comparisons)
-
2G12: To investigate B-cell responses immediately following HIV-1 transmission, Env-specific Ab responses to autologous and consensus Envs in plasma donors were determined. Broadly neutralizing Abs with specificity similar to 2G12 did not appear during the first 40 days after plasma virus detection.
Tomaras2008
(acute/early infection)
-
2G12: The neutralization profile of early R5, intermediate R5X4, and late X4 viruses from a rhesus macaque infected with SHIV-SF162P3N was assessed. 2G12 neutralized all three viruses with similar low potency.
Tasca2008
(co-receptor, neutralization)
-
C2G12: Neutralization of HIV-1 IIIB LAV isolate by 2G12 was within the same range as the neutralization of the virus by natural antibodies from human sera against the gal(α1,3)gal disaccaride linked to CD4 gp120-binding peptides, indicating that the activity of natural antibodies can be re-directed to neutralize HIV-1.
Perdomo2008
(neutralization)
-
2G12: A new purification method was developed using a high affinity peptide mimicking CD4 as a ligand in affinity chromatography. This allowed the separation in one step of HIV envelope monomer from cell supernatant and capture of pre-purified trimer. Binding of 2G12 to gp120SF162 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the miniCD4 allows the separation of HIV-1 envelope with intact 2G12 epitope. gp140DF162ΔV2 was purified by the miniCD4 method to assess its ability to capture gp140 trimers. Binding of 2G12 to gp140DF162ΔV2 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the SF162 trimer antigenicity was preserved.
Martin2008
(assay or method development, binding affinity)
-
2G12: A divalent Man9ClcNAc2 glycopeptide, that binds to 2G12, was covalently coupled to the OMPC carrier and used as immunogen to test its efficacy to induce 2G12-like neutralizing Ab response. High levels of carbohydrate-specific Ab were induced in both guinea pigs and rhesus macaques, but these Ab showed poor recognition of recombinant gp160 and failed to neutralize a panel of subtype B isolates. Sera from HIV-1 positive individuals was tested for binding to the synthetic antigen but failed to recognize the mimetics, although two of the patients showed presence of 2G12-like Abs. These results suggest that presentation of Man9ClcNAc2 on the constrained cyclic scaffold is insufficient to induce a polyclonal response that recognizes native 2G12 epitope.
Joyce2008
(mimotopes, neutralization, vaccine antigen design)
-
2G12: MAb 2G12 binds to gp120 and is essentially inactive after CD4 engagement, with a neutralization half-life of less than 1 minute. Thus, the binding site for 2G12 on gp120 is unavailable once the CD4-induced conformational changes in gp120 have occurred.
Gustchina2008
(antibody binding site, neutralization, kinetics)
-
2G12: Variable domains of three heavy chain Abs, the VHH, were characterized. The Abs were isolated from llamas, who produce immunoglobulins devoid of light chains, immunized with HIV-1 CRF07_BC, to gp120. It was hypothesized that the small size of the VHH, in combination with their protruding CDR3 loops, and their preference for cleft recognition and binding into active sites, may allow for recognition of conserved motifs on gp120 that are occluded from conventional Abs. 2G12 provided some inhibition of binding of the three neutralizing VHH Abs to gp120, suggesting that 2G12 imposes steric hinderance to binding of the VHH Abs to gp120.
Forsman2008
(antibody interactions)
-
2G12: 24 broadly neutralizing plasmas from HIV-1 subtype B and C infected individuals were investigated using a series of mapping methods to identify viral epitopes targeted by NAbs. In competitive virus capture assays on 2G12 coated plates, some of the subtype B plasmas, and two of the subtype C plasmas, inhibited virus capture. Mutant versions of JR-FL trimers were designed to selectively eliminate neutralization epitopes, but the plasma titers against the 2G12-eliminated mutant were similar to those against the wildtype. This indicated that very few, if any, 2G12-like Abs were present in the plasmas, and that a fraction of patients developed Abs that overlap the 2G12 epitope but do not neutralize the virus.
Binley2008
(neutralization, binding affinity)
-
2G12: 32 human HIV-1 positive sera neutralized most viruses from clades A, B, and C. Two of the sera stood out as particularly potent and broadly reactive. Two CD4-binding site defective mutant Env proteins were generated to evaluate whether Abs to the CD4-binding site are involved in the neutralizing activity of the two sera. The integrity of the wildtype and mutant proteins was tested for their reactivity to 2G12.
Li2007a
(binding affinity)
-
2G12: A recombinant gp120-Fc bound to 2G12, indicating it was conformationally intact. 2G12 binding to gp120 was inhibited by the soluble recombinant extracellular domain (ECD) of DC-SIGN in a dose-dependent fashion, but 2G12 did not inhibit binding of gp120 to DC-SIGN. Many single, double, and triple N-glycan mutations in the 2G12 epitope did not affect binding of gp120 to DC-SIGN, however, some of the N-glycan sites within the 2G12 epitope were shown to be optimally positioned to significantly contribute to DC-SIGN binding. Thus, it is suggested that DC-SIGN can bind to a flexible combination of N-glycans on gp120, both within and outside of the 2G12 epitope, but that its optimal binding site overlaps with specific N-glycans within the 2G12 epitope.
Hong2007
(binding affinity)
-
2G12: HIV-1 env clones resistant to cyanovirin (CV-N), a carbohydrate binding agent, showed amino acid changes that resulted in deglycosylation of high-mannose type residues in the C2-C4 region of gp120. Compared to their parental virus HIV-1 IIIB, these CV-N resistant viruses were also completely resistant to 2G12, as they lost one or more 2G12 binding glycans on gp120.
Hu2007
(neutralization, escape)
-
2G12: Chemical inhibition of mammalian glycoprotein synthesis with the plant alkaloid kifunensine resulted in an abundance of oligomannose-type glycans on the cell surface, and binding of 2G12 to previously non-antigenic self proteins and cells. Expression of gp120 in the presence of kifunensine also increased both binding and valency of gp120 to 2G12.
Scanlan2007
(antibody binding site, binding affinity)
-
2G12: The ability of 2G12 to neutralize recently transmitted viruses was examined in four homosexual and two parenteral transmission couples. The vast majority of recently transmitted viruses from homosexual recipients were resistant to neutralization by 2G12, although viruses isolated later in the course of infection showed increased sensitivity to 2G12 in one of the patients. In the parenteral transmission, one of the recipients had early viruses resistant to 2G12 neutralization, and one had viruses somewhat sensitive to 2G12 neutralization. The neutralization sensitivity patterns of recipient viruses to 2G12 did not correlate to the neutralization sensitivity patterns of their donors in the homosexual couples, while the HIV-1 variants from the one of the two parenteral pairs were similarly resistant to neutralization by 2G12. 12% of 2G12 resistant viruses had all five PNGS of the 2G12 epitope. 88.5% of the 2G12 resistant viruses lacked at least one of the five PNGS, and viruses isolated later in infection that had become sensitive to 2G12 neutralization had restored the 2G12 epitope.
Quakkelaar2007a
(neutralization, acute/early infection, mother-to-infant transmission)
-
2G12: Three MAbs, 2G12, 4E10 and 2F5, were administered to ten HIV-1 infected individuals treated with ART during acute and early infection, in order to prevent viral rebound after interruption of ART. MAb infusions were well tolerated with essentially no toxicity. Viral rebound was not prevented, but was significantly delayed in 8/10 patients. 2G12 activity was dominant among the MAbs used. Baseline susceptibility to 2G12 was inversely correlated with the time to viral rebound. Escape from 2G12 was associated with viral rebound. Long-term suppression of viremia was achieved in 3/10 patients.
Mehandru2007
(escape, immunotherapy, supervised treatment interruptions (STI))
-
2G12: MBL, a lectin present in human serum that recognizes mannose-rich N-glycans, was shown to mediate increased HIV-1 infectivity, and to reduce 2G12-mediated neutralization of HIV-1.
Marzi2007
(neutralization)
-
2G12: The study compared Ab neutralization against the JR-FL primary isolate and trimer binding affinities judged by native PAGE. There was direct quantitative relationship between monovalent Fab-trimer binding and neutralization, implying that neutralization begins as each trimer is occupied by one Ab. In BN-PAGE, neutralizing Fabs, 2G12 in particular, and sCD4 were able to shift JR-FL trimers. In contrast, most non-neutralizing Fabs bound to monomer, but their epitopes were conformationally occluded on trimers, confirming the exclusive relationship of trimer binding and neutralization. For 2G12, there was a ladder of partially and fully liganded trimers
Crooks2008
(neutralization, binding affinity)
-
2G12: Five amino acids in the gp41 N-terminal region that promote gp140 trimerization (I535, Q543, S553, K567 and R588) were considered. Their influence on the function and antigenic properties of JR-FL Env expressed on the surfaces of pseudoviruses and Env-transfected cells was studied. Various non-neutralizing antibodies bind less strongly to the Env mutant, but neutralizing antibody binding is unaffected. There was no difference in 2G12 binding to wild type and mutant JR-FL, and 2G12 inhibited infection of the two pseudoviruses with comparable potencies.
Dey2008
(binding affinity)
-
2G12: The study explores how the V1 loop of Env influences the neutralization susceptibilities of heterologous viruses to antibodies elicited by the SF162gp140 immunogen. All viruses expressing the WT Envs were susceptible to neutralization by 2G12. Replacement of the V1 loops by that of SF162 did not alter the neutralization susceptibilities of the viruses.
Ching2008
(neutralization)
-
2G12: Molecular mechanism of neutralization by MPER antibodies, 2F5 and 4E10, was studied using preparations of trimeric HIV-1 Env protein in the prefusion, the prehairpin intermediate and postfusion conformations. MAb 2G12 was used to analyze antigenic properties of construct 92UG-gp140-Fd, derived from isolate 92UG037.8 and stabilized by a C-terminal foldon tag. 92UG-gp140-Fd binds 2G12 with high affinity.
Frey2008
(binding affinity)
-
2G12: The study explores the development of a carbohydrate immunogen that could elicit 2G12-like neutralizing ABs to contribute to an AIDS vaccine. Specifically, the study describes the development of neoglycoconjugates displaying variable copy numbers of synthetic tetramannoside (Man(4) on bovine serum albumin (BSA) molecules by conjugation to Lys residues. Immunization of rabbits with BSA-(Man(4))(14) elicits significant serum Ab titers to Man(4). However, these Abs are unable to bind gp120.
Astronomo2008
(vaccine antigen design)
-
2G12: Addition of a glycosylation site at position V295N in three different subtype C envelope clones (COT9.6, COT6.15 and Du151.2) resulted in increase in binding of 2G12. However, only one of the viral clones (COT9.6) became sensitive to neutralization by 2G12 at high Ab concentrations. Introduction of glycosylation site at position 448 in COT6.15 further increased its binding to 2G12 and resulted in viruses more sensitive to neutralization. Furthermore, addition of glycosylation at position 442 increased binding and neutralization sensitivity of the corresponding viruses to 2G12, and deletion of glycosylation at position 386 resulted in reduction in binding and resistance to neutralization by 2G12.
Gray2007a
(antibody binding site, neutralization, binding affinity, subtype comparisons)
-
2G12: A D386N change in the V4 region, which results in restoration of N-glycosylation at this site, did not have any impact on the neutralization of a mutant virus by 2G12 compared to wildtype. Also, there was no association between increased sensitivity to 2G12 neutralization and enhanced macrophage tropism.
Dunfee2007
(antibody binding site)
-
2G12: This review summarizes data on the development of HIV-1 centralized genes (consensus and ancestral) for induction of neutralizing antibody responses. Functionality and conformation of native epitopes in proteins based on the centralized genes was tested and confirmed by binding to 2G12 and other MAbs. Antibodies induced by immunization with these centralized proteins did not, however, have the breadth and potency compared to that of 2G12 and other broadly neutralizing MAbs.
Gao2007
(antibody binding site, neutralization, vaccine antigen design, review)
-
2G12: Macaques were immunized with either CD4, gp120, cross-linked gp120-human CD4 complex (gp120-CD4 XL), and with single chain complex containing gp120 rhesus macaque CD4 domains 1 and 2 (rhFLSC). Sera from the rhFLSC immunized animals showed slightly higher competition titers, being able to block gp120-CD4 complex interactions with 2G12 slightly more efficiently than sera from animals immunized with the three other proteins.
DeVico2007
(neutralization)
-
2G12: 2G12-blocking activity was very low in all of the sera from guinea pigs immunized with gp120 protein, or with three types of VLPs: disulfide-shackled functional trimers (SOS-VLP), uncleaved nonfunctional Env (UNC-VLP), naked VLP bearing no Env.
Crooks2007
(neutralization, vaccine antigen design)
-
2G12: Interactions of this Ab with gp120 monomer and two cleavage-defective gp140 trimers were studied. It was shown that 2G12 interactions with the soluble monomers and trimers were minimally affected by GA cross-linking of the proteins, indicating that the 2G12 epitope was maintained after cross-linking. This Ab was associated with a small entropy change upon gp120 binding. This Ab was shown to have a kinetic advantage as it bound to gp120 faster than other less neutralizing Abs.
Yuan2006
(antibody binding site, antibody interactions, kinetics, binding affinity)
-
2G12: No significant levels of 2G12 were shown to bind to HA/gp41 expressed on cell surfaces and this Ab did not stain cells expressing HA/gp41 in a fluorescence assay. However, it did bind to HIV 89.6 Env expressing cells.
Ye2006
(antibody binding site, binding affinity)
-
2G12: Viruses with wild-type HIV-1JR-FL Envs were neutralized by this Ab at much lower concentrations than HIV-1 YU2 Env viruses.
Yang2006
(neutralization, binding affinity)
-
2G12: SHIV SF162p4 virus used as challenge in ISCOM vaccinated macaques was shown to be highly sensitive to neutralization by this Ab.
Pahar2006
(neutralization)
-
2G12: All subtype C env-pseudotyped clones derived from individuals in acute/early stage of HIV-1 infection were highly resistant to neutralization by this Ab, since each of the clones lacked a PNLG at one or more critical epitope positions. The sensitivity of clones to a mix of Abs IgG1b12, 2G12 and 2F5 was tracked to IgG1b12.
Li2006a
(neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
-
2G12: This Ab was used as a control since its epitope is independent of either V1/V2 or V3 domains confirmed in its equal neutralization of SF162 and variants SF162(JR-FL V3), SF162(JR-FL V1/V2) and SF162(JR-FL V1/V2/V3). This Ab was also shown to neutralize viruses with V3 sequences from several different subtypes (B, F, A1, H, C, CRF02_AG and CRF01_AE).
Krachmarov2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: Binding of 2G12 to wt gp120 and two constructs with 5 and 9 residues deleted in the middle of the beta3-beta5 loop in the C2 region of gp120 was examined. The deletions of the loop residues did not affect the conformation of 2G12 epitope as 2G12 Ab binding and kinetics were identical for the wt gp120 and both constructs.
Rits-Volloch2006
(antibody binding site, kinetics, binding affinity)
-
2G12: This Ab was used as a positive control in the neutralization assay. At the highest Ab concentrations, 2G12 was able to neutralize several primary isolates but not all, with a neutralization pattern similar to that of rabbit sera immunized with monovalent and polyvalent DNA-prime/protein-boost Env from different HIV-1 subtypes. At a reduced concentrations, 2G12 showed much weaker neutralizing activities.
Wang2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: Novel approaches based on sequential (SAP) and competitive (CAP) antigen panning methodologies, and use of antigens with increased exposure of conserved epitopes, for enhanced identification of broadly cross-reactive neutralizing Abs are reviewed. Previously known broadly neutralizing human mAbs are compared to Abs identified by these methods.
Zhang2007
(review)
-
2G12: This Ab was used in the analysis of clade C gp140 (97CN54) antigenicity and was shown not to bind to this molecule, as the glycan epitope is absent.
Sheppard2007a
(binding affinity)
-
2G12: 2 glycosylation site additions to asparagines 295 and 392 on the clade C gp120 backbone (gp120CN54+) were used to reconstruct the 2G12 epitope, as the gp120CN54+ construct showed excellent reactivity with 2G12. gp120CN54+ and an Fc tagged outer domain of gp120 (ODCN54+-Fc) bound equally well to 2G12, while Fc fusion to gp120CN54+ reduced 2G12 binding, indicating partial occlusion of the 2G12 epitope.
Chen2007a
(antibody binding site, binding affinity)
-
2G12: Pseudoviruses derived from gp120 Env variants that evolved in multiple macaques infected with SHIV 89.6P displayed a range of degrees of virion-associated Env cleavage. Pseudoviruses with higher amount of cleaved Env were more sensitive to neutralization by 2G12, as they contained peripheral glycan N386, not present in the wildtype 89.6P.
Blay2007
(neutralization)
-
2G12: Carbohydrate-binding agents, including 2G12, are reviewed regarding to their antiviral activity, resistance development, and their potential use as therapeutic agents.
Balzarini2007
(review)
-
2G12: Increased neutralization sensitivity was observed for (R5)X4 viruses from timepoints both early and late after emergence of X4 compared to their coexisting R5 variants in one patient, and only for the early (R5)X4 viruses in another patient. In a third patient, in contrast, late (R5)X4 viruses were found to be significantly more resistant to 2G12 neutralization than their coexisting R5 variants.
Bunnik2007
(co-receptor, neutralization)
-
2G12: Neutralization sensitivity of maternal and infant viruses to 2G12 close to transmission timepoint was shown to be poor. Even the viruses from one mother, that were shown to be sensitive to maternal Abs and pooled plasma, were not neutralized by 2G12, indicating that Abs in plasma are not directed to this Ab epitope.
Rainwater2007
(neutralization, mother-to-infant transmission)
-
2G12: 2G12-neutralized HIV-1 captured on Raji-DC-SIGN cells or immature monocyte-derived DCs (iMDDCs) was successfully transferred to CD4+ T lymphocytes, indicating that the 2G12-HIV-1 complex was disassembled upon capture by DC-SIGN-cells.
vanMontfort2007
(neutralization, dendritic cells)
-
2G12: Synthetic monomeric D1 arm oligosaccharide, corresponding to the D1 arm of Man9 which has a high affinity to 2G12, and its fluorinated derivative interacted with 2G12 only weakly. However, when four units of synthetic D1 arm tetrasaccharide were introduced to a cyclic decapeptide template, it showed high affinity to 2G12. Introduction of two T-helper epitopes onto the template did not affect 2G12 binding, indicating that the construct could be used as a new type of immunogen for raising carbohydrate-specific neutralizing Abs against HIV.
Wang2007b
(mimotopes, vaccine antigen design, kinetics, binding affinity)
-
2G12: Infusion of a MAb cocktail (4E10, 2G12 and 2F5) into HIV-1 infected subjects was shown to be associated with increased levels of serum anti-cardiolipin and anti-phosphatidylserine Ab titers, and increased coagulation times. In the absence or in the presence of adult and neonate plasma, 2G12 did not bind to either phosphatidylserine nor to cardiolipin, and did not induce significant prolongations of clotting times in human plasma, indicating that infusion of 2G12 was not responsible for autoreactivity and prolonged clotting times.
Vcelar2007
(antibody interactions, autoantibody or autoimmunity, binding affinity, immunotherapy)
-
2G12: The major infectivity and neutralization differences between a PBMC-derived HIV-1 W61D strain and its T-cell line adapted counterpart were conferred by the interactions of three Env amino acid substitutions, E440G, D457G and H564N. Chimeric Env-pseudotyped virus Ch5, containing all three of the mutations, was equally neutralization sensitive to 2G12 as Ch2, which did not contain any of these mutations.
Beddows2005a
(neutralization)
-
2G12: Four primary isolates (PIs), Bx08, Bx17, 11105C and Kon, were tested for binding and neutralization by 2G12. 2G12 was only able to neutralize Bx08, but bound well to both Bx08 and Bx17 and less well to 11105C and Kon. There was no direct correlation between binding and neutralization of the four PIs by 2G12. CD4-induced gp120 shedding resulted in a decrease of 2G12 binding to Bx08. Presence of gp160 depleted of the principal immunodominant domain (PID) significantly decreased capture of Bx17 and Kon by 2G12. Presence of both gp160ΔPID and PID slightly improved the inhibition of virus capture compared to PID peptide alone, revealing an additive effect.
Burrer2005
(neutralization, binding affinity)
-
2G12: A panel of 60 HIV-1 isolates, with complete genome sequences available, was formed for neutralization assay standardization. It comprises of 10 isolates from each of the subtypes A, B, C, D, CRF01_AE and CRF02AG, with majority of the viruses being of R5 phenotype and few of X4 phenotype. Neutralization profile of each isolate was assessed by measuring neutralization by sCD4, a cocktail of MAbs including 2G12, 2F5 and IgG1b12, and a large pool of sera collected from HIV-1 positive patients. The MAb cocktail neutralized with >50% a large portion of the isolates (51/60) including: 10 subtype A isolates, 8 subtype B isolates, 8 subtype C isolates, 9 subtype D isolates, 7 CRF-01_AE isolates, and 9 CRF_02AG isolates.
Brown2005a
(assay or method development, neutralization, subtype comparisons)
-
2G12: The unique structure of the 2G12 MAb, and the reasons for its unique ability to recognize oligomannose chains on the silent face of the gp120, are reviewed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed.
Burton2005
(antibody binding site, review, structure)
-
2G12: SFV-gp140(-GCN4) was constructed for analysis of its immunogenic properties in animal models. Both gp120 and gp140(-GCN4) secreted from rSFV-infected cells were recognized by 2G12, suggesting that the proteins retained their native folding.
Forsell2005
(antibody binding site)
-
2G12: Monomeric gp120 and trimeric gp140CF proteins synthesized from an artificial group M consensus Env gene (CON6) bound efficiently to 2G12, indicating correct exposure of the 2G12 epitope. A mix of 2G12, 2F5 and b12 MAbs (TriMab2) was used for neutralization assessment of some subtype B isolates, but showed no significant neutralization.
Gao2005a
(antibody binding site, neutralization)
-
2G12: 2G12 neutralized viral isolates HXBc2, SF162, 89.6 and BaL. ADA isolate was poorly neutralized and the YU2 isolate was not neutralized. Neutralization was concentration dependent, as higher MAb concentration resulted in higher % of neutralization. The exception was the YU2 isolate, where higher concentration of 2G12 resulted in enhancement of viral infection.
Grundner2005
(enhancing activity, neutralization)
-
2G12: 2G12 bound with a higher maximal mean fluorescence intensity (MFI) to Env protein on the surface of cells producing gp140Δct-pseudotyped neutralization resistant 3.2P strain, than to the Env of pseudotyped neutralization sensitive HXBc2. Neutralization assays with the pseudotyped viruses showed that 2G12 neutralized both viruses with same potency. Furin co-transfection did not have an effect on the reactivity of pseudoviruses with 2G12 or on their neutralization sensitivity. Presence or absence of sialic acid residues did not affect Env reactivity with 2G12.
Herrera2005
(antibody binding site, neutralization, binding affinity)
-
2G12: Why broadly neutralizing Abs, such as 2G12, 2F5 and 4E10, are extremely rare, and their protective abilities and potential role in immunotherapy are discussed.
Julg2005
(neutralization, immunotherapy, review)
-
2G12: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alternations of both gp41 and gp120. The alternations did not affect virus CD4 binding, coreceptor binding site exposure, or infectivity of the virus, but did result in increased relative neutralization resistance of the LLP-2 mutant virus to 2G12, compared with wildtype virus. The increased neutralization resistance of LLP-2 virus was associated with decreased 2G12 binding to its epitope.
Kalia2005
(antibody binding site, neutralization, binding affinity)
-
2G12: A series of genetically modified Env proteins were generated and expressed in both insect and animal cells to be monitored for their antigenic characteristics. For 2G12, two of the modified proteins expressed in insect cells, dV1V2 mutant (V1V2 deletions) followed by the dV2 mutant, showed higher binding to the Ab than the wildtype Env did, indicating that V1V2 deletion exposes epitopes against 2G12 better than other proteins. Unlike for most of the other MAbs, 3G mutant (mutations in 3 glycosylation sites) did not show a higher binding affinity to 2G12. When expressed in animal cells, only dV2 mutant resulted in higher binding to 2G12, while all other modified proteins showed lower binding compared to the wildtype.
Kang2005
(antibody binding site, binding affinity)
-
2G12: Full-length gp160 clones were derived from acute and early human HIV-1 infections and used as env-pseudotyped viruses in neutralization assays for their characterization as neutralization reference agents. 12 out of 19 pseudoviruses were neutralized by 2G12, as were SF162.LS and IIIB strains but not the MN strain. Resistance to 2G12 was generally associated with lack of N-glycosylation sites, except in one case, where the clone was resistant to neutralization in spite of presence N-glycosylation sites. Two clones lacked N-glycosylation at residues 339 and 386, but remained sensitive to 2G12. A mixture of IgG1b12, 2F5 and 2G12 (TriMab) exhibited potent neutralizing activity against all Env-pseudotyped viruses except one. 7 out of 12 Env-pseudotyped viruses were more sensitive to neutralization by 2G12 than their uncloned parental PBMC-grown viruses.
Li2005a
(assay or method development, neutralization)
-
2G12: Pseudoviruses expressing HIV-1 envelope glycoproteins from BL01, BR07 and 89.6 strains were compared in neutralization assays to replication competent clone derived from transfection of 293T cells (IMC-293T) and to the IMC-293T derived from a single passage through PBMC (IMC-PBMC). The neutralization responses of pseudoviruses and corresponding IMC-293T to 2G12 were similar, while a significant decrease in viral neutralization sensitivity to 2G12 was observed for all three IMC-PBMC viruses. The decrease was associated with an increase in average virion envelope glycoprotein content on the PBMC-derived virus.
Louder2005
(assay or method development, neutralization)
-
2G12: 2G12 was used as isolating template for screening of a phage library in order to develop mimotopes that target carbohydrate antigens of gp120. Specific binding of 2G12 to three phages expressing peptides was observed, however, 2G12 did not bind to the peptides themselves.
Pashov2005a
(assay or method development)
-
2G12: 2G12 neutralized JR-FL, but not YU2 HIV-1 strain. 2G12 and other neutralizing mAbs recognized JR-FL cleavage-competent and cleavage-defective env glycoproteins, while non-neutralizing Abs only recognized JR-FL cleavage-defective glycoproteins. It is suggested that an inefficient env glycoprotein precursor cleavage exposes non-neutralizing determinants, while only neutralizing regions remain accessible on efficiently cleaved spikes. For YU2, both cleavage-competent and -defective glycoproteins were recognized by both neutralizing and non-neutralizing Abs.
Pancera2005
(antibody binding site, neutralization, binding affinity)
-
2G12: A short review of 2F5 and 4E10 interaction with autoantigens, epitope accessibility, structure, neutralizing capability, and the reasons for their infrequent appearance in nature. Immunotherapy and escape to 2G12 is also discussed.
Nabel2005
(escape, immunotherapy, review)
-
2G12: Viruses containing substitutions at either L568 or K574 of the gp41 hydrophobic pocket were resistant to D5-IgG1 but were as sensitive to 2G12 as the wildtype virus.
Miller2005
-
2G12: This short review summarizes recent findings of the role of neutralizing Abs in controlling HIV-1 infection. Certain neutralizing MAbs and their potential role in immunotherapy and vaccination, as well as the reasons for their poor immunogenicity, are discussed.
Montefiori2005
(antibody binding site, therapeutic vaccine, escape, immunotherapy)
-
2G12: Virions containing a single point mutation Y706C in gp41 had a 10-fold increase in binding to 2G12 compared to wildtype. This, together with the same p24 supernatant levels after transfection with wildtype and mutant virus, indicated that the mutant virions contained more envelope on a per-particle basis.
Poon2005
(antibody binding site, binding affinity)
-
2G12: Escape mutations in HR1 of gp41 that confer resistance to Enfuvirtide reduced infection and fusion efficiency and also delayed fusion kinetics of HIV-1. They also conferred increased neutralization sensitivity to a subset of neutralizing MAbs that target fusion intermediates or with epitopes exposed following receptor interactions. Enhanced neutralization correlated with reduced fusion kinetics. None of the mutations had a significant effect on 2G12 neutralization of virus.
Reeves2005
(antibody binding site, drug resistance, neutralization, escape, HAART, ART)
-
2G12: There was no difference found in the neutralization sensitivity of viruses isolated from acutely and from chronically infected HIV-1 patients to this Ab, suggesting that the glycosylation sites manifesting the epitope of 2G12 are well conserved throughout the course of infection.
Rusert2005
(antibody binding site, neutralization, acute/early infection)
-
2G12: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed.
Srivastava2005
(antibody binding site, neutralization, vaccine antigen design, binding affinity, immunotherapy, review, structure)
-
2G12: Six acutely and eight chronically infected patients were passively immunized with a mix of 2G12, 2F5 and 4E10 neutralizing Abs during treatment interruption. Two chronically and four acutely infected individuals showed evidence of a delay in viral rebound during Ab treatment suggesting that NAbs can contain viremia in HIV-1 infected individuals. All subjects with virus sensitive to 2G12 developed Ab escape mutants resulting in loss of viremia and failure to treatment. In several cases resistance to 2G12 emerged rapidly. Plasma levels of 2G12 were substantially higher than those of 2F5 and 4E10, and the 2G12 levels exceeded the in vitro required 90% inhibitory doses by two orders of magnitude in subjects that responded to Ab treatment. This suggested that high levels of NAbs are required for inhibition in vivo.
Trkola2005
(neutralization, acute/early infection, escape, immunotherapy, early treatment, HAART, ART, supervised treatment interruptions (STI))
-
2G12: Ab neutralization of viruses with mixtures of neutralization-sensitive and neutralization-resistant envelope glycoproteins was measured. It was concluded that binding of a single Ab molecule is sufficient to inactivate function of an HIV-1 glycoprotein trimer. The inhibitory effect of the Ab was similar for neutralization-resistant and -sensitive viruses indicating that the major determinant of neutralization potency of an Ab is the efficiency with which it binds to the trimer. It was also indicated that each functional trimer on the virus surface supports HIV-1 entry independently, meaning that every trimer on the viral surface must be bound by an Ab for neutralization of the virus to be achieved.
Yang2005b
(neutralization)
-
2G12: A substantial fraction of soluble envelope glycoprotein trimers contained inter-subunit disulfide bonds. Reduction of these disulfide bonds had little effect on binding of the 2G12 to the glycoprotein, indicating that the inter-S-S bonds had no impact on the exposure of 2G12 epitope.
Yuan2005
(antibody binding site)
-
2G12: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1.
McCann2005
(antibody binding site, antibody interactions, neutralization, vaccine antigen design, variant cross-reactivity, immunotherapy, review, structure)
-
2G12: 2G12 was investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. The activity of 2G12 was induced in the post-CD4 format and was less pronounced in the standard format. 2G12 did not neutralize after CD4/CCR5 engagement. HIV-1+ human plasma mediated high-levels of post-CD4 neutralization indicating presence of b12 and 2G12 -like Abs.
Crooks2005
(antibody binding site, assay or method development, neutralization)
-
2G12: This review summarizes data on the polyspecific reactivities to host antigens by the broadly neutralizing MAbs IgG1b12, 2G12, 2F5 and 4E10. It also hypothesizes that some broadly reactive Abs might not be routinely made because they are derived from B cell populations that frequently make polyspecific Abs and are thus subjected to B cell negative selection.
Haynes2005a
(antibody interactions, review)
-
2G12: This review summarizes data that indicate that the V3 region of HIV-1 may be an epitope to target for the induction of protective Abs. Data shows that the V3 region can induce broadly-reactive, cross-neutralizing Abs, that it is partially exposed during various stages of the infectious process, and that it is immunogenic. 2G12 is the only highly neutralizing MAb targeting the carbohydrate region of gp120, suggesting that this region does not induce protective Abs. The carbohydrate epitope is poorly immunogenic and 2G12 has an aberrant structure probably extremely rare in the human Ab repertoire.
Zolla-Pazner2005
(antibody binding site, variant cross-reactivity, review)
-
2G12: In addition to gp120-gp41 trimers, HIV-1 particles were shown to bear nonfunctional gp120-gp41 monomers and gp120-depleted gp41 stumps on their surface. 2G12 effectively neutralized wildype virus particles. 2G12 was found to bind to both nonfunctional monomers and to gp120-gp41 trimers. Binding of 2G12 to trimers correlated with its neutralization of wildtype virus particles. Monomer binding did not correlate with neutralization, but it did correlate with virus capture. It is hypothesized that the nonfunctional monomers on the HIV-1 surface serve to divert the Ab response, helping the virus to avoid neutralization.
Moore2006
(antibody binding site, neutralization, binding affinity)
-
2G12: A carbohydrate mimetic peptide with central motif versions RYRY and YPYRY was shown to precipitate human IgG Ab that bind to gp120 and to immunoprecipitate gp120 from transfected cells. 2G12 showed significant binding only to the PYPY motif version of the peptide.
Pashov2006
(mimotopes)
-
Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). 2G12 recognized all four gp140 proteins equally. Low titers of Abs capable of blocking the binding of 2G12 were present in the sera from the SHIV-infected macaque, but were absent in the sera from the gp140-immunized animals.
Derby2006
(antibody binding site)
-
2G12: Development of neutralizing Abs and changes to Env gp120 were analyzed in SHIV infected macaques during a period of 1 year. 4 macaques showed little viral divergence while the remaining 7 showed significant env divergence from the inoculum, associated with higher titers of homologous NAbs. In five of the 7 divergent animals, the glycosylation site N386, which is a part of the 2G12 epitope, was significantly added. Glycosylation sites N392, on the inner domain of gp120, and N295, on the silent face, also forma a part of the 2G12 epitope, and were found to be highly conserved.
Blay2006
(antibody binding site)
-
2G12: 2G12 did not inhibit binding of Fc-gp120 to CD4, however, it inhibited binding of Fc-gp120, and of the virus itself, to the CCR5 coreceptor and to the DC-SIGN. Thus 2G12 probably inhibits HIV-1 by two mechanisms: blocking of gp120-CCR5 and of gp120-DC-SIGN interactions. Pre-incubation of virus with sCD4 did not affect its neutralization by 2G12. This Ab was also shown to effectively inhibit trans-infection of virus from primary monocyte-derived dendritic cells (MDDCs) to CD4+ T-cells. Attachment of Fc-gp120 to MDDCs and PBLs was partially inhibited by 2G12, while b12 and sCD4 did not inhibit binding to MDDCs but did inhibit binding to PBLs. The results indicate that Env attachment is mediated through DC-SIGN and other receptors on MDDCs while it is predominantly mediated by CD4 and CCR5 on PBLs.
Binley2006
(antibody binding site, co-receptor, neutralization, binding affinity, dendritic cells)
-
2G12: A fusion protein (FLSC R/T-IgG1) that targets CCR5 was expressed from a synthetic gene linking a single chain gp120-CD4 complex containing an R5 gp120 sequence with the hinge-Ch2-Ch3 portion of human IgG1. The fusion protein did not activate the co-receptor by binding. In cell-line based assays, the FLSC R/T-IgG1 was less potent in neutralizing R5 HIV-1 primary isolates than 2G12, while in PBMC assays they were comparable.
Vu2006
(neutralization)
-
2G12: Env-pseudotyped viruses were constructed from the gp160 envelope genes from seven children infected with subtype C HIV-1. 2G12 failed to neutralize any of the seven viruses, correlating with the absence of crucial N-linked glycans that define 2G12 epitope on these viruses. When this Ab was mixed with IgG1b12 and 2F5, the neutralization was similar as to IgGb12 alone, indicating that the majority of the pool activity was due to IgG1b12. When 4E10 was added to this mix, all isolates were neutralized.
Gray2006
(neutralization, variant cross-reactivity, responses in children, mother-to-infant transmission)
-
2G12: Pharmacokinetic properties of this Ab were studied in HIV infected patients infused with high doses of 2G12. The Ab did not elicit an endogenous immune response and had distribution and systemic clearance values similar to other Abs. The elimination half-life was measured to 21.8 days, which is significantly longer than the elimination half-life of 4E10 and 2F5.
Joos2006
(kinetics, immunotherapy)
-
2G12: Inhibition of 2G12 binding to gp120 by 2G12-like Abs in sera from long-term non-progressors (LTNP) was determined. 2G12-like Abs were present in almost all sera from LTNPs but at a lower levels than b12. Higher 2G12-like Ab levels were significantly associated with the broadest neutralizing activity in sera from LNTPs.
Braibant2006
(enhancing activity, neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: Neutralization rates and rate constants for the neutralization of clade B primary isolates SF33, SF162 and 89.6 by this Ab were determined. Statistically significant neutralization was not observed for isolate SF162. It was shown that neutralization sensitivity is not associated with neutralization of cell-associated or free virus.
Davis2006
(neutralization, variant cross-reactivity, kinetics)
-
2G12: Cloned Envs (clades A, B, C, D, F1, CRF01_AE, CRF02_AG, CRF06_cpx and CRF11_cpx) derived from donors either with or without broadly cross-reactive neutralizing antibodies were shown to be of comparable susceptibility to neutralization by 2G12.
Cham2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
2G12: The ability of this Ab to inhibit viral growth was increased when macrophages and immature dendritic cells (iDCs) were used as target cells instead of PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication by this Ab for macrophages and iDCs can occur by two distinct mechanisms, neutralization of infectivity involving only the Fab part of the IgG, and, an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles.
Holl2006
(neutralization, dendritic cells)
-
2G12: Viruses with cleavage-competent 2G12-knockout Env and cleavage-defective Env able to bind 2G12 were constructed. The amount of Env precipitated by 2G12 was same when the two pseudotyped virus variants were mixed as with the wildtype alone, suggesting formation of heterotrimers consisting of both cleavage-competent and defective Envs. The presence of nonfunctional Envs on the surface of infectious virions did not affect the neutralization by 2G12. The neutralization by the CD4-binding agents was also unaffected by 2G12 binding to uncleaved Env indicating that the function of a trimer is unaffected sterically by the binding of an antibody to adjacent trimer.
Herrera2006
(neutralization, binding affinity)
-
2G12: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The neutralizing activity of 2G12 was higher in iMDDCs than in PHA-stimulated PBMCs. A 90% reduction of HIV infection was observed without induction of MDDC maturation by this MAb. Blockade of FcgammaRII on iMDDCs decreased the anti-HIV activity of 2G12 while increased expression of FcgammaRI increased inhibition of HIV by 2G12, suggesting the involvement of these receptors in the HIV-inhibitory activity of this Ab.
Holl2006a
(neutralization, dendritic cells)
-
2G12: G1 and G2 recombinant gp120 proteins, consisting of 2F5 and 4E10, and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120, were tested as an immunogen to see if they could elicit MPER antibody responses. Deletion of V1/V2 from gp120 or its replacement with G1 and G2 grafts, did not greatly affect binding of 2G12 to gp120. Shortening of the N and C termini of the V3 loop nearly abolished binding of 2G12.
Law2007
(vaccine antigen design)
-
2G12: This review describes the effectiveness of the current HIV-1 immunogens in eliciting neutralizing antibody responses to different clades of HIV-1. It also summarizes different evasion and antibody escape mechanisms, as well as the most potent neutralizing MAbs and their properties. MAbs reviewed in this article are: 2G12, IgG1b12, 2F5, 4E10, A32, 447-52D and, briefly, D50. Novel immunogen design strategies are also discussed.
Haynes2006a
(antibody binding site, neutralization, variant cross-reactivity, escape)
-
2G12: 2G12 was used as a negative control to investigate the relationship of MAb 412d epitope to the CCR5 binding site of gp120. These two MAbs were incubated with soluble CD4 and ADA gp120 in the presence of a peptide shown to block the association of gp120-CD4 with CCR5. As expected, the presence of the peptide did not inhibit precipitation of gp120 by 2G12, since it binds an epitope distinct from the CCR5 binding domain, while it did inhibit the 412d.
Choe2003
(antibody binding site)
-
2G12: The gp140δCFI protein of CON-S M group consensus protein and gp140CFI and gp140CF proteins of CON6 and WT viruses from HIV-1 subtypes A, B and C were expressed in recombinant vaccinia viruses and tested as immunogens in guinea pigs. 2G12 was shown to bind specifically to all recombinant proteins except for the subtype B gp140δCF and subtype A gp140δCFI. The specific binding of this Ab to CON-S indicated that its conformational epitope was intact. This Ab also bound specifically to the two tested subtype B gp120 proteins.
Liao2006
(antibody binding site, vaccine antigen design, subtype comparisons)
-
2G12: Cross-neutralization was limited in this study. 2G12 neutralized subtype A strain UG273 and subtype B strains US2, NL4-3, and IIIB. It did not neutralize subtype C strain ETH2220, subtype D UG270, CRF01 A/E ID12; subtype F BZ163; nor subtype G BCF06. 3 HIV-2 strains and SIVmac 251 were also not neutralized. 2G12 bound to MN and NDK, but did not neutralize them. Neutralization resistance was selected in culture using strains NL43 and IIIB. NL43 escaped via loss of the glycosylation sequon at positions 295-297, IIIB escaped via sequon losses at positions 392-394 and 295-297, or 406-408, as expected from earlier studies defining critical mannose residues for 2G12 binding. The loss of the mannose actually enhanced mannose-specific lectin inhibition of the virus.
Huskens2007
(antibody binding site, neutralization, variant cross-reactivity, escape, subtype comparisons)
-
2G12: Binding of 2G12 to gp120 was not significantly affected by the small molecule HIV-1 entry inhibitor IC9564. IC9564 induces conformational change of gp120 to allow CD4i antibody 17b to bind, but inhibits CD4-induced gp41 conformational changes.
Huang2007
(antibody binding site)
-
2G12: The neutralizing activity of this antibody for the JR-FL Env variant with the N160K/E160K mutations was measured in comparison with the neutralizing activity of 2909, which was found to be higher.
Honnen2007
(neutralization, variant cross-reactivity)
-
2G12: Controlled attachment of Ab-bound HIV to cells was not affected by the presence of this Ab. However, the virus was still efficiently neutralized indicating that binding of 2G12 to the cell-free virus interferes with a step of infection subsequent to cell attachment.
Haim2007
(antibody binding site, neutralization, kinetics)
-
2G12: This Ab was used to help define the antigenic profile of envelopes used in serum depletion experiments to attempt to define the neutralizing specificities of broadly cross-reactive neutralizing serum. It bound to JR-FL and JR-CSF gp120 monomers and to a lesser extent to core JR-CSF gp120 monomer.
Dhillon2007
(antibody binding site, neutralization)
-
2G12: SOSIP Env proteins are modified by the introduction of a disulfide bond between gp120 and gp41 (SOS), and an I559P (IP) substitution in gp41, and form trimers. The KNH1144 subtype A virus formed more stable trimers than did the prototype subtype B SOSIP Env, JRFL. The stability of gp140 trimers was increased for JR-FL and Ba-L SOSIP proteins by substituting the five amino acid residues in the N-terminal region of gp41 with corresponding residues from KNH1144 virus. b12, 2G12, 2F5, 4E10 and CD4-IgG2 all bound similarly to the WT and to the stabilized JRFL SOSIP timers, suggesting that the trimer-stabilizing substitutions do not impair the overall antigenic structure of gp140 trimers.
Dey2007
-
2G12: 15 subtype A HIV-1 envelopes from early in infection were not neutralized by 2G12, likely because of a deletion or shift in one or more of the 5 glycosylation sites associated with 2G12 recognition. SF162 was neutralized as expected.
Blish2007
(neutralization, acute/early infection, subtype comparisons)
-
2G12: This Ab was found to be able to bind to a highly stable trimeric rgp140 derived from a HIV-1 subtype D isolate containing intermonomer V3-derived disulfide bonds and lacking gp120/gp41 cleavage.
Billington2007
-
2G12: Yeast display was compared to phage display and shown to select all the scFv identified by phage display and additional novel antibodies. Biotinylated C11 and 2G12 were used to minimize selection of non-gp120 specific clones from the yeast displayed antibody library; these MAbs were used as they have unique epitopes with limited overlap with most known epitopes.
Bowley2007
(assay or method development)
-
2G12: Four consensus B Env constructs: full length gp160, uncleaved gp160, truncated gp145, and N-linked glycosylation-site deleted (gp160-201N/S) were compared. All were packaged into virions, and all but the fusion defective uncleaved version mediated infection using the CCR5 co-receptor. Primary isolate Envs were completely resistant or just somewhat sensitive to neutralization by 2G12 while the consensus B constructs were sensitive. Thus the 2G12 epitope is present on the consensus B Env glycoprotein and was not influenced by the Env modifications in this study.
Kothe2007
(vaccine antigen design, variant cross-reactivity)
-
2G12: Newborn macaques were challenged orally with the highly pathogenic SHIV89.6P and then treated intravenously with a combination of IgG1b12, 2G12, 2F5 and 4E10 one and 12 hours post-virus exposure. All control animals became highly viremic and developed AIDS. In the group treated with mAbs 1 hour post-virus exposure, 3/4 animals were protected from persistent systemic infection and one was protected from disease. In the group treated with mAbs 12 hour post-virus exposure, one animal was protected from persistent systemic infection and disease was prevented or delayed in two animals. IgG1b12, 2G12, and 4E10 were also given 24 hours after exposure in a separate study; 4/4 treated animals become viremic, but with delayed and lower peak viremia relative to controls. 3/4 treated animals did not get AIDS during the follow up period, and 1 showed a delayed progression to AIDS , while the 4 untreated animals died of AIDS. Thus the success of passive immunization with NAbs depends on the time window between virus exposure and the start of immunoprophylaxis.
Ferrantelli2007
(immunoprophylaxis)
-
2G12: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. 2G12 had diminished binding to both antigen constructs.
Selvarajah2005
(vaccine antigen design, vaccine-induced immune responses)
-
2G12: Concanavalin A (ConA) binds to mannose and blocks 2G12 binding, but 2G12 does not block ConA binding. ConA binding is less sensitive to mutations in glycosylation sites than 2G12. Furthermore, ConA neutralizes HIV-1 at a post-CD4 binding step. Thus, this report indicates that designing antigens based on the HIV-1 mannose residues that bind ConA may be an effective vaccine strategy, as antibodies elicited might be broadly cross-reactive.
Pashov2005
(vaccine antigen design)
-
2G12: Passive immunization of 8 HIV-1 infected patients with 4E10, 2F5 and 2G12 (day 0, 4E10; days 7, 14 and 21 4E10+2G12+2F5; virus isolated on days 0 and 77) resulted in 0/8 patients with virus that escaped all three NAbs. Three patients had viruses that escaped 2G12, and two of these were sequenced. Each had lost two of the glycosylation sites required for 2G12 binding (one had 295 N->D and 332 N->T changes, the other had 295 N->T and 392 N->T changes). In a companion in vitro study, resistance to a single MAb emerged in 3-22 weeks, but triple combination resistance was slower and characterized by decreased viral fitness. In contrast to the in vivo escape study, only one N was lost in the in vitro experiments, a 386 N->K change in a triple resistant mutant. The lack of resistance to the combination of MAbs in vivo and the reduced fitness of the escape mutants selected in vitro suggests passive immunotherapy may be of value in HIV infection.
Nakowitsch2005
(escape, immunotherapy)
-
2G12: Nine anti-gp41 bivalent Fabs that interacted with either or both of the six-helix bundle and the internal coiled-coil of N-helices of gp41 were selected from a non-immune human phage display library. The IC50 the range for the inhibition of LAV ENV-mediated cell-fusion was 6-61 ug/ml -- for context, 2F5 and 2G12 (IC50s of 0.5-1.5 ug/ml) were about an order of magnitude more potent in this assay than the best Fabs generated here.
Louis2005
(neutralization)
-
2G12: Retrovirus inactivation for vaccine antigen delivery was explored through lipid modification by hydrophobic photoinduced alkylating probe 1.5 iodonaphthylazide (INA). The viral proteins were shown to be structurally intact in the treated non-infectious virus, through the preservation of antibody binding sites for polyclonal anti-gp120 serum, and for broadly neutralizing MAbs 2G12, b12 and 4E10, although the modifications of the lipid disabled viral infection.
Raviv2005
(vaccine antigen design)
-
2G12: This study is about the V2 MAb C108g, that is type-specific and neutralizes BaL and HXB2. JR-FL is a neutralization resistant strain; modification of JRFL at V2 positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The modification in V2 also increased neutralization sensitivity to V3 MABs 4117c, 2219, 2191, and 447-52D, but only had minor effects on neutralization by CD4BS MAb 5145A, and broadly neutralizing MAbs IgG1b12, 2G12, and 2F5.
Pinter2005
(antibody binding site)
-
2G12: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication in microglial cells. Bori-15 had increased replication in microglial cells and a robust syncytium-forming phenotype, ability to use low levels of CD4 for infection, and increased sensitivity to neutralization by sCD4 and 17b. Four amino acid changes in gp120 V1-V2 were responsible for this change. Protein functionality and integrity of soluble, monomeric gp120-molecules derived from parental HIV-1 Bori and microglia-adapted HIV-1 Bori-15 was assessed in ELISA binding assays using CD4BS MAbs F105 and IgG1b12, glycan-specific 2G12, and V3-specific 447-52D, and were unchanged. Association rates of sCD4 and 17b were not changed, but dissociation rates were 3-fold slower for sCD4 and 14-fold slower for 17b.
Martin-Garcia2005
(antibody binding site)
-
2G12: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B V3s. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. Neutralization by Cameroonian sera MAbs was blocked by Clade A and B V3 loop fusion proteins, while NAbs to non-V3 epitopes, 2F5, 2G12, and b12, were not blocked.
Krachmarov2005
(antibody binding site, variant cross-reactivity, subtype comparisons)
-
2G12: Of 35 Env-specific MAbs tested, only 2F5, 4E10, IgG1b12, and two CD4BS adjacent MAbs (A32 and 1.4G) and gp41 MAbs (2.2B and KU32) had binding patterns suggesting polyspecific autoreactivity, and similar reactivities may be difficult to induce with vaccines because of elimination of such autoreactivity. Unlike the other three broadly neutralizing human anti-HIV-1 MAbs, 2G12 has no indication of polyspecific autoreactivity.
Haynes2005
(antibody binding site)
-
2G12: 2909 is a human anti-Env NAb that was selected by a neutralization assay and binds to the quaternary structure on the intact virion. ELISA-based competition assays and subsequent mutational analysis determined that the CD4BS and V2 and V3 loops contribute to the 2909 epitope: 2909 binding was inhibited by MAbs 447-52d (anti-V3), 830A (anti-V2), and IgG1b12 (anti-CD4BS) and sCD4. 2909 was not inhibited by MAbs 670, 1418, nor 2G12; in fact, 2G12 enhanced 2909 binding.
Gorny2005
-
2G12: Precise characterization of 2G12 binding to carbohydrate was undertaken; the 2G12 Fab was co-crystallized with four oligomannose derivatives, Man4, Man5, Man7 and Man8. 2G12 recognizes the terminal Manα1-2Man both in the context of the D1 arm (Manα1-2Manα1-2Man) and D3 arm (Manα1-2Manα1-6Man) of the Man9GlcNAc2 moiety, but not the D2 arm. This gives the 2G12 more binding flexibility than previously thought, as only the D1 arm binding had been shown previously.
Calarese2005
(antibody binding site, structure)
-
2G12: The lack of glycosylation sites at residues Asn 295 and Thy 394 within C-clade gp120s generally causes the loss of 2G12 recognition. Introduction of glycans in the subtype C strain HIV-1CN54 at these positions restored 2G12 binding, and addition of just a single glycan partially restored binding (V295N + A394T >> V295N > A395T). 2G12 epitope recovery decreased b12 binding.
Chen2005
(antibody binding site)
-
2G12: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it binds to the neutralizing MAb 2G12. It masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120.
Pantophlet2004
(vaccine antigen design)
-
2G12: Infusions of 2F5 and 2G12 intravenously administered 24h prior to vaginal SHIV-89.P challenge are able to protect macaques from infections. Animals that receive a IL-2 adjuvanted DNA immunization SIV Gag and HIV Env have T-cell responses and lower viral loads, but were not protected. Suboptimal levels of 2F5 and 2G12 were not able to confer sterile protection in combination with the T-cell responses stimulated by DNA immunizations.
Mascola2003
-
2G12: Nabs against HIV-1 M group isolates were tested for their ability to neutralize 6 randomly selected HIV-1 O group strains. 2G12 did not neutralize O group strains, although it was included in a quadruple combination of b12, 2F5, 2G12, and 4E10, that neutralized the six Group O viruses between 62-97%.
Ferrantelli2004a
(variant cross-reactivity)
-
2G12: Neonatal rhesus macaques were exposed orally to a pathogenic SHIV, 89.6P. 4/8 were given an intramuscular, passive immunization consisting of NAbs 2G12, 2F5 and 4E10, each given at a different body sites at 40 mg/kg per Ab, at one hour and again at 8 days after exposure to 89.6P. The four animals that were untreated all died with a mean survival time of 5.5 weeks, the four animals that got the NAb combination were protected from infection. This model suggests Abs may be protective against mother-to-infant transmission of HIV.
Ferrantelli2004
(mother-to-infant transmission)
-
2G12: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. 2G12 primarily neutralized B clade viruses with sporadic neutralization of A, D, and two AC recombinants, and no C or CRF01 (E) isolates. Envelopes from subtypes C and E have generally lost critical glycans for 2G12 binding.
Binley2004
(variant cross-reactivity, subtype comparisons)
-
2G12: Env sequences were derived from 4 men at primary infection and four years later; the antigenicity in terms of the ability to bind to 2G12, 2F5 and IgG1b12 was determined. 2G12 bound primarily to late clones in 3 of the 4 patients, and to both early and late in the other patient. Neither 2F5 nor IgG1b12 showed a difference in binding affinity to early or late envelopes. The number of glycosylation sites increased in the three patients. The ability to bind to 2G12 correlated perfectly with having all three sites known to be important for binding: N295 in C2, N332 in C3, and N392 in the V4 loop.
Dacheux2004
(antibody binding site, acute/early infection, kinetics)
-
2G12: Crystal structure analysis of Fab 2G12 alone or complexed with Manα1-2Man or Man9GlcNac2 demonstrates that the exchange of VH domains forms stable dimers for gp120 binding. Two Fabs assemble in an interlocked VH domain swapped dimer, providing an extended surface for multivalent interaction with the cluster of oligomannose on gp120, allowing high-affinity recognition of repeated epitopes in the carbohydrate structure. Ala substitutions of the 2G12 VH/VH' interface residues Ile H19, Arg H57, Phe H77, Tyr H80, Val H84 and Pro H113 result in the loss of 2G12-gp120 JR-FL binding.
Calarese2003
(antibody binding site, antibody sequence, structure)
-
2G12: Synthetic mannose Man9 clusters arranged on a scaffold were used to mimic the epitope of 2G12. Bi-, tri, and tetra-valent clusters had a 7-, 22-, and 73-fold higher affinities for 2G12 than the monomers, suggesting that 2G12 binds best to multiple carbohydrate moieties. 2G12 bound larger mannose oligosaccharides with higher affinity: Ma9GlcNAc bound 210- and 74-fold more effectively that Man6GlcNac and Man5GlcNAc, respectively.
Wang2004
(antibody binding site)
-
2G12: This review discusses research presented at the Ghent Workshop of prevention of breast milk transmission and immunoprophylaxis for HIV-1 in pediatrics (Seattle, Oct. 2002), and makes the case for developing passive or active immunoprophylaxis in neonates to prevent mother-to-infant transmission. Macaque studies have shown that passive transfer of NAb combinations (for example, IgG1b12, 2G12, 2F5, and 4E10; or 2G12 and 2F5) can confer partial or complete protection to infant macaques from subsequent oral SHIV challenge.
Safrit2004
(immunoprophylaxis, mother-to-infant transmission)
-
2G12: A primary isolate, CC1/85, was passaged 19 times in PBMC and gradually acquired increased sensitivity to FAb b12 and sCD4 that was attributed to changes in the V1V2 loop region, in particular the loss of a potential glycosylation site. The affinity for sCD4 was unchanged in the monomer, suggesting that the structural impact of the change was manifested at the level of the trimer. The passaged virus, CCcon19, retained an R5 phenotype and its neutralization susceptibility to other Abs was essentially the same as CC1/85. The IC50 for 2G12 was 1.8 for CC1/85, and was 4.2 for CCcon19, so both the primary and passaged viruses were neutralized.
Pugach2004
(variant cross-reactivity, viral fitness and/or reversion)
-
2G12: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neutralization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype. 2G12 was the only MAb that neutralized JRFL more efficiently than SF162, with a 6-fold lower ND50 for JRFL. 2G12 also had a higher affinity for JRFL.
Pinter2004
(variant cross-reactivity)
-
2G12: An antigen panel representing different regions of gp41 was generated, and sera from 23 individuals were screened. 2G12 was a control, binding to gp120 but to none of the gp41 peptides in the experiment.
Opalka2004
(assay or method development)
-
2G12: A set of HIV-1 chimeras that altered V3 net charge and glycosylation patterns in V1V2 and V3, involving inserting V1V2 loops from a late stage primary isolate taken after the R5 to X4 switch, were studied with regard to phenotype, co-receptor usage, and MAb neutralization. The loops were cloned into a HXB2 envelope with a LAI viral backbone. It was observed that the addition of the late-stage isolate V1V2 region and the loss of V3-linked glycosylation site in the context of high positive charge gave an X4 phenotype. R5X4 viruses were more sCD4 and 2G12 neutralization resistant than either R5 or X4, but the opposite pattern was observed for b12. Addition of the late stage V1V2 altered neutralization for both MAbs, but this alteration was reversed with the loss of the V3 glycan.
Nabatov2004
(antibody binding site, co-receptor)
-
2G12: Mice susceptible to MV infection were intraperitoneally immunized with native HIV-1 89.6 env gp160 and gp140 and δV3 HIV-1 89.6 mutants expressed in live attenuated Schwarz measles vector (MV). The gp160ΔV3 construct raised more cross-reactive NAbs to primary isolates. A HIVIG/2F5/2G12 combination was used as a positive control and could neutralize all isolates.
Lorin2004
(vaccine antigen design)
-
2G12: 2G12 was used as a positive control in a study that showed that A32-rgp120 complexes open up the CCR5 co-receptor binding site, but did not induce neutralizing antibodies with greater breadth among B subtype isolates than did uncomplexed rgp120 in vaccinated guinea pigs.
Liao2004
(vaccine antigen design)
-
2G12: A set of oligomeric envelope proteins were made from six primary isolates for potential use as vaccine antigens: 92/UG/037 (clade A), HAN2/2 (clade B), 92/BR25/025 (clade C), 92/UG/021 (clade D), 93/BR/029 (clade F) and MVP5180 (clade O). This was one of a panel of MAbs used to explore folding and exposure of well characterized epitopes. The clade C isolate BR25 is apparently misfolded, as conformation-dependent antibodies did not bind to it. 2G12 bound to clade A, B, D and F HIV-1 primary isolates. Polyclonal sera raised in rabbits against these antigens cross-bound the other antigens, but none of the sera had neutralizing activity.
Jeffs2004
(vaccine antigen design, subtype comparisons)
-
2G12: The peptide 12p1 (RINNIPWSEAMM) inhibits direct binding of YU2 gp120 or Env trimer to CD4, CCR5 and MAb 17b in a concentration-dependent allosteric manner. 12p1 is thought to bind to unbound gp120 near the CD4 binding site, with a 1:1 stoichiometry. 12p1 also inhibited MAb F105 binding; presumably because F105 favors an unactivated conformation, but not MAbs 2G12 or b12. The 1:1 stoichiometry, the fact that the peptide binding site is accessible on the trimer, the non-CD4 like aspect of the binding, and an ability to inhibit viral infection in cell cultures make it a promising lead for therapeutic design.
Biorn2004
-
2G12: This paper is a review of anti-HIV-1 Envelope antibodies. This unique epitope is formed from carbohydrates. The mechanism of MAb neutralization is thought to be steric inhibition of CCR5 binding. 2G12 neutralizes many TCLA strains and about 40% of primary isolates tested.
Gorny2003
(review)
-
2G12: A gp120 molecule was designed to focus the immune response onto the IgG1b12 epitope. Ala substitutions that enhance the binding of IgG1b12 and reduce the binding of non-neutralizing MAbs were combined with additional N-linked glycosylation site sequons inhibiting binding of non-neutralizing MAbs; b12 bound to the mutated gp120. C1 and C5 were also removed, but this compromised b12 binding.
Pantophlet2003b
(vaccine antigen design)
-
2G12: scFv 4KG5 reacts with a conformational epitope. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120. MAbs to the V2 loop, V3 loop, V3-C4 region, and CD4BS diminished binding, while MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected. 2G12 had no impact on 4KG5 binding.
Zwick2003a
(antibody interactions)
-
2G12: The broadly neutralizing antibodies 2F5 and 2G12 were class-switched from IgG to IgA and IgM isotypes. Neutralizing potency was increased with valence for 2G12 so the IgM form was most potent, but for 2F5 the IgG form was most potent. Eight primary isolates were tested including two subtype A isolates. The polymeric IgM and IgA Abs, but not the corresponding IgGs, could interfere with HIV-1 entry across a mucosal epithelial layer, although they were limited in a standard neutralization assay. All isotypes could interact with activated human sera, presumably through complement, to inhibit HIV replication.
Wolbank2003
(complement, genital and mucosal immunity, isotype switch, variant cross-reactivity, subtype comparisons)
-
2G12: The antiviral response to intravenously administered MAbs 2F5 and 2G12 was evaluated in 7 HAART-naïve asymptomatic HIV-1 infected patients during a treatment period of 28 days. MAb therapy reduced plasma HIV RNA in 3/7 patients during the treatment period, and transiently reduced viral load in two more. CD4 counts were up in 3/7 through day 28, and transiently increased in three more. Vigorous complement activation was observed after 48/56 Ab infusions. Virus derived from 2/7 patients could be neutralized by 2G12, and escape from 2G12 was observed in both cases after infusion; one year after the infusion, isolates were again sensitive to 2G12.
Stiegler2002
(complement, variant cross-reactivity, escape, immunotherapy)
-
2G12: Env genes derived from uncultured brain biopsy samples from four HIV-1 infected patients with late-stage AIDS were compared to env genes from PBMC samples. Brain isolates did not differ in the total number or positions of N-glycosylation sites, patterns of coreceptor usage, or ability to be recognized by gp160 and gp41 MAbs. 2G12 was the only MAb tested to recognize all blood and brain isolates from all four patients by gp120 immunoprecipitation.
Ohagen2003
(variant cross-reactivity)
-
2G12: AC10 is a subject who was given treatment early after infection, and had a viral rebound after cessation of therapy, which then declined to a low level. The polyclonal sera from AC10 could potently neutralize the rebound virus, and NAb escape followed with a neutralizing response against the escape variant and subsequent escape from that response. Viral loads remained low in this subject despite escape. The rebound isolate that was potently neutralized by autologous sera was not particularly neutralization sensitive, as it resisted neutralization by sCD4 and MAbs IgG1b12, 2G12 and 2F5, and was only moderately sensitive to sera from other HIV+ individuals that had high titers of NAbs to TCLA strains.
Montefiori2003
(acute/early infection, escape)
-
2G12: Polyclonal Abs raised against soluble trivalently linked N35CCG-N13 and N34CCG, the internal trimeric core of the coiled-coil ectodomain, inhibit HIV-1 Env-mediated cell fusion at levels comparable to 2G12.
Louis2003
(vaccine antigen design)
-
2G12: Thermodynamics of binding to gp120 was measured using isothermal titration calorimetry for sCD4, 17b, b12, 48d, F105, 2G12 and C11 to intact YU2 and the HXBc2 core. The free energy of binding was similar, except for 2G12, which might not have bound well to the carbohydrate additions on the Drosophila expressed core. Enthalpy and entropy changes were divergent, but compensated. Not only CD4 but MAb ligands induced thermodynamic changes in gp120 that were independent of whether the core or the full gp120 protein was used. Non-neutralizing CD4BS and CD4i MAbs (17b, 48d, 1.5e, b6, F105 and F91) had large entropy contributions to free energy (mean: 26.1 kcal/mol) of binding to the gp120 monomer, but the potent CD4BS neutralizing MAb b6 had a much smaller value of 5.7 kcal/mol. The high values suggest surface burial or protein folding an ordering of amino acids. 2G12 had an entropy value of -1.6. These results suggest that while the trimeric Env complex has four surfaces, a non-neutralizing face (occluded on the oligomer), a variable face, a neutralizing face and a silent face (protected by carbohydrate masking), gp120 monomers further protect receptor binding sites by conformational or entropic masking, requiring a large energy handicap for Ab binding not faced by other anti-gp120 Abs.
Kwong2002
(antibody binding site)
-
2G12: MAbs IgG1b12, 2G12, 2F5 and 4E10 were tested for their ability to neutralize two primary HIV-1 clade A isolates (UG/92/031 and UG/92/037) and two primary HIV-1 clade D isolates (UG/92/001 and UG/92/005). 4E10 demonstrated the most potent cross-neutralization activity. Quadruple administration of MAbs IgG1b12, 2G12, 2F5, and 4E10 induced strong synergistic neutralization of 4 clade A isolates (UG/92/031, UG/92/037, RW/92/020 and RW/92/025) as well as 5 clade D isolates (UG/92/001,UG/9/005, /93/086/RUG/94/108, UG/94/114). The authors note this combination of 4 MAbs neutralizes primary HIV A, B, C, and D isolates.
Kitabwalla2003
(antibody interactions, immunoprophylaxis, variant cross-reactivity, mother-to-infant transmission, subtype comparisons)
-
2G12: This paper shows that binding of CD4BS MAbs to Env blocks the conformational shift that allows co-receptor CCR5 binding and CD4-independent mediated cell fusion. CD4BS MAbs IgG1b12, F91 and F105 and their Fab counterparts (except for C11, used as a negative control) inhibited CD4-independent JR-FL and YU-2 gp120-CCR5 binding to CCR5-expressing Cf2Th cells and syncytium formation. The carbohydrated binding MAb 2G12 also inhibited CD4-independent syncytium formation.
Raja2003
(co-receptor)
-
2G12: To begin to design vaccine antigens that can mimic the carbohydrate structure, the gp120 peptide 336-342 was synthesized with Man(9), Man(6), and Man(5) moieties attached.
Singh2003
(vaccine antigen design)
-
2G12: Review of current neutralizing antibody-based HIV vaccine candidates and strategies of vaccine design. Strategies for targeting of the epitopes for NAbs 2F5, 2G12, 4E10, b12, and Z13 are described. They have shown that both N-glycans, at 295N and 332N are required for 2G12 binding, emphasizing the oligosaccharide cluster nature of the epitope, and suggest the uniqueness of the target structure may not result in autoimmune reactions.
Wang2003
(vaccine antigen design, review)
-
2G12: Most plasma samples of patients from early infection had NAb responses to early autologous viruses, and NAbs against heterologous strains tended to be delayed. Serial plasma samples were tested against serial isolates, and neutralization escape was shown to be rapid and continuous throughout infection. Autologous neutralization-susceptible and resistant viruses from four patients were tested for susceptibility to neutralizing Ab responses using MAbs 2G12, IgG1b12 and 2F5. No correlation was established, all viruses tested were susceptible to at least one of the neutralizing MAbs. Two patients that did not have an autologous NAb response also did not evolve changes in susceptibility to these MAbs, while one patient with a pattern of autologous neutralization and escape acquired a 2G12 sensitive virus at month 6, and lost IgG1b12 sensitivity at month 21.
Richman2003
(autologous responses, acute/early infection, escape)
-
2G12: This review discusses the importance and function of protective antibody responses in animal model studies in the context of effective vaccine development. SHIV models have shown protection using high levels of MAbs can prevent infection, and partial protection that can influence disease course can be obtained from modest levels of NAbs. SHIV challenges studies conducted with infusions of combinations of MAbs b12, 2G12, and 2F5 are reviewed.
Mascola2003a
(immunoprophylaxis, review)
-
2G12: This study investigates the effects of glycosylation inhibitors on the binding between HIV-1 gp120 and mannose-binding lectin (MBL). Mannosidase I inhibitor deoxymannojirimycin (dMM) inhibits formation of complex and hybrid N-linked saccharides and yields virus with more mannose residues. dMM added during viral production significantly enhanced the binding 2F5 and 2G12, but not IgG1b12 in a viral capture assay.
Hart2003
(antibody binding site)
-
2G12: UK1-br and MACS2-br are R5 isolates derived from brain tissue samples from AIDS patients with dementia and HIV-1 encephalitis; both are neurotropic, but only UK1-br induced neuronal apoptosis and high levels of syncytium formation in macrophages. UK1-br Env had a greater affinity for CCR5 than MACS-br, and required low levels of CCR5 and CD4 for cell-to-cell fusion and single round infection. PBMC infected with UK1-br and MACS2-br virus isolates were resistant to neutralization by MAb 2G12. UK1-br was more sensitive than MACS2-br to IgG1b12, 2F5 and CD4-IgG2 neutralization.
Gorry2002
(brain/CSF, co-receptor)
-
2G12: Four newborn macaques were challenged with pathogenic SHIV 89.6 and given post exposure prophylaxis using a combination of NAbs 2F5, 2G12, 4E10 and IgG1b12. 2/4 treated animals did not show signs of infection, and 2/4 macaques maintained normal CD4+ T cell counts and had a lower delayed peak viremia compared to the controls.
Ferrantelli2003
(immunoprophylaxis, mother-to-infant transmission)
-
2G12: A sCD4-17b single chain chimera was made that can bind to the CD4 binding site, then bind and block co-receptor interaction. This chimeric protein is a very potent neutralizing agent, more potent than IgG1b12, 2G12 or 2F5 against Ba-L infection of CCR5-MAGI cells. It has potential for prophylaxis or therapy.
Dey2003
(co-receptor)
-
2G12:The MAb B4e8 binds to the base of the V3 loop, neutralizes multiple primary isolates and was studied for interaction with other MAbs. B4e8 and 2G12 enhanced each other's binding, and gave synergistic neutralization. B4e8 could neutralize R5X4 virus 92HT593 better than 2G12, while 2G12 was better at neutralizing R5 virus 92US660.
Cavacini2003
(antibody interactions)
-
2G12: This study examined Ab interactions, binding and neutralization with a B clade R5 isolate (92US660) and R5X4 isolate (92HT593). Abs generally bound and neutralized the R5X4 isolate better than the R5 isolate. Anti-gp41 MAb F240 did not affect binding of 2G12 to either R5X4 and R5 isolates, and anti-V3 MAb B4a1 increased 2G12 binding to R5X4 virions but not R5. Neutralization with B4al and 2G12 was additive for the R5X4 virus, and was enhanced for the R5 virus.
Cavacini2002
(antibody interactions, co-receptor, variant cross-reactivity)
-
2G12: Neutralization assays with rsCD4, MAbs, and serum samples from SHIV-infected macaques and HIV-1 infected individuals were used to characterize the antigenic properties of the env glycoprotein of six primary isolate-like or TCLA SHIV variants. 2G12 neutralized the five SHIV strains tested, HXBc2, KU2, 89.6, 89.6P and KB9, in MT-2 cells.
Crawford1999
(variant cross-reactivity)
-
2G12: The SOS mutant envelope protein introduces a covalent disulfide bond between gp120 surface and gp41 transmembrane proteins into the R5 isolate JR-FL by adding cysteines at residues 501 and 605. Pseudovirions bearing this protein bind to CD4 and co-receptor bearing cells, but do not fuse until treatment with a reducing agent, and are arrested prior to fusion after CD4 and co-receptor engagement. 2G12 is able to neutralize both the wildtype and SOS protein comparably, but 2G12 could not neutralize SOS when added post-attachment.
Binley2003
(vaccine antigen design)
-
2G12: IgG1b12 neutralized many South African (5/8) and Malawian (4/8) clade C primary HIV-1 isolates, being more effective than 2F5 which neutralized only two Malawian and no South African isolates. 2G12 did not neutralize any of the 16 isolates.
Bures2002
(subtype comparisons)
-
2G12: SOS-Env is a mutant protein engineered to have a disulfide bond between gp120 and gp41. Cells expressing SOS-Env due not fuse with target cells expressing CD4 and CCR5, although the fusion process proceeds to an intermediate state associated with CD4 and co-receptors, prior to the formation of the six helix bundle that allows fusion.2G12 was used to monitor surface expression of SOS-Env compared to wildtype.
Abrahamyan2003b
(co-receptor, vaccine antigen design)
-
2G12: 2G12 was used as a positive control to test for a NAb activity in mice intranasally immunized with gp120 or gp140 with IL-12 and Cholera Toxin B.
Albu2003
-
2G12: NIH AIDS Research and Reference Reagent Program: 1476.
-
2G12: UK Medical Research council AIDS reagent: ARP3030.
-
2G12: CD4BS MAbs b12 (neutralizing) and 205-42-15, 204-43-1, 205-46-9 (non-neutralizing) all cross-competed for binding to monomeric gp120, indicating the topological proximity of their epitopes, however, the non-neutralizing CD4BS MAbs did not interfere with the neutralization activity of MAb b12 -- 2G12 was used to normalize and as a control in these experiments.
Herrera2003
(antibody interactions)
-
2G12: Alanine scanning mutagenesis was used to compare substitutions that affected anti-CD4BS NAb b12 -- rec gp120s were engineered to contain combinations of Alanine substitutions that enhanced b12 binding, and while binding of b12 to these gp120 monomers was generally maintained or increased, binding by five non-neutralizing anti-CD4bs MAbs (b3, b6, F105, 15e, and F91) was reduced or completely abolished -- 2G12 binding was largely unperturbed, indicating these proteins were not grossly misfolded.
Pantophlet2003
(antibody binding site)
-
2G12: Review of NAbs that discusses mechanisms of neutralization, passive transfer of NAbs and protection in animal studies, and vaccine strategies.
Liu2002
(review)
-
2G12: Review of NAbs that notes 2G12 alone or in combination with other MAbs can protect some macaques against SHIV infection, that it has strong ADCC activity, and that it is safe and well tolerated in humans.
Ferrantelli2002
(immunoprophylaxis)
-
2G12: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain.
Zhang2002
(antibody binding site)
-
2G12: Rhesus macaques were better protected from vaginal challenge with SHIV89.6D (MAb 2G12, 2/4; MAbs 2F5/2G12, 2/5; and HIVIG/2F5/2G12, 4/5 infected) than from intravenous challenge (MAb 2G12, 0/3; MAbs 2F5/2G12, 1/3; and HIVIG/2F5/2G12, 3/6 infected)-- the animals that were infected by vaginal challenge after Ab infusion had low or undetectable viral RNA levels and modest CD4 T-cell decline.
Mascola2002
(genital and mucosal immunity, immunoprophylaxis)
-
2G12: HIV-1 gp160deltaCT (cytoplasmic tail-deleted) proteoliposomes (PLs) containing native, trimeric envelope glycoproteins from R5 strains YU2 and JRFL, and X4 strain HXBc2, were made in a physiologic membrane setting as candidate immunogens for HIV vaccines -- 2F5 bound to gp160deltaCT with a reconstituted membrane ten-fold better than the same protein on beads, while such an affinity difference was not seen with F105 and 2G12 -- anti-CD4BS MAbs IgG1b12 and F105, A32 (C1-C4), C11 (C1-C5), and 39F (V3) MAbs bound gp160deltaCT PLs indistinguishably from gp160deltaCT expressed on the cell surface.
Grundner2002
(antibody binding site, vaccine antigen design)
-
2G12: Truncation of the gp41 cytoplasmic domain of X4, R5, and X4R5 viruses forces a conformation that more closely resembles the CD4 bound state of the external Envelope, enhancing binding of CD4i MAbs 17b and 48d and of CD4BS MAbs F105, b12, and in most cases of glycosylation site dependent MAb 2G12 and the anti-gp41 MAb 246D -- in contrast, binding of the anti-V2 MAb 697D and the anti-V3 MAb 694/98D were not affected -- viruses bearing the truncation were more sensitive to neutralization by MAbs 48d, b12, and 2G12 -- the anti-C5 MAb 1331A was used to track levels of cell surface expression of the mutated proteins.
EdwardsBH2002
(antibody binding site)
-
2G12: A modified gp140 (gp140deltaCFI), with C-term mutations intended to mimic a fusion intermediate and stabilize trimer formation, retained antigenic conformational determinants as defined by binding to CD4 and to MAbs 2F5, 2G12, F105, and b12, and enhanced humoral immunity without diminishing the CTL response in mice injected with a DNA vaccine.
Chakrabarti2002
(vaccine antigen design)
-
2G12: Passive immunization of neonate macaques with a combination of F105+2G12+2F5 conferred complete protection against oral challenge with SHIV-vpu+ or -- the combination b12+2G12+2F5 conferred partial protection against SHIV89.6 -- such combinations may be useful for prophylaxis at birth and against milk born transmission -- the synergistic combination of IgG1b12, 2G12, 2F5, and 4E10 neutralized a collection of HIV clade C primary isolates.
Xu2002
(antibody interactions, immunoprophylaxis, mother-to-infant transmission)
-
2G12: Uncleaved soluble gp140 (YU2 strain, R5 primary isolate) can be stabilized in an oligomer by fusion with a C-term trimeric GCN4 motif or using a T4 trimeric motif derived from T4 bacteriophage fibritin -- stabilized oligomer gp140 delta683(-FT) showed strong preferential recognition by NAbs IgG1b12 and 2G12 relative to the gp120 monomer, in contrast to poorly neutralizing MAbs F105, F91, 17b, 48d, and 39F which showed reduced levels of binding, and MAbs C11, A32, and 30D which did not bind the stabilized oligomer.
Yang2002
(antibody binding site)
-
2G12: Ab binding characteristics of SOS gp140 were tested using SPR and RIPA -- SOS gp140 is gp120-gp41 bound by a disulfide bond -- NAbs 2G12, 2F5, IgG1b12, CD4 inducible 17b, and 19b bound to SOS gp140 better than uncleaved gp140 (gp140unc) and gp120 -- non-neutralizing MAbs 2.2B (binds to gp41 in gp140unc) and 23A (binds gp120) did not bind SOS gp140 -- 2G12 complexes with SOS gp140 or with gp120 had a very unusual linear structure.
Schulke2002
(antibody binding site, vaccine antigen design)
-
2G12: Alanine scanning mutagenesis used in conjunction with competition and replacement studies of N-linked carbohydrates and sugars suggest that the 2G12 epitope is formed from mannose residues contributed by the glycans attached to N295 and N332, with the other N-linked carbohydrates in positions N339, N386, and N392 playing a role in maintaining conformation relevant to 2G12 binding -- N295A and N332A mutants showed essentially unchanged anti-CD4BS NAb b12 binding affinities, while N339A, N386A and N392A mutants displayed significantly lowered b12 affinity, presumably due to conformational changes.
Scanlan2002
(antibody binding site)
-
2G12: The 2G12 epitope is composed of carbohydrates involving high-mannose and hybrid glycans of residues 295, 332, and 392, with peripheral glycans from 386 and 448 contributing on either flank, and with little direct gp120 protein surface involvement -- these mannose residues are proximal to each other near the chemokine receptor binding surface.
Sanders2002
(antibody binding site)
-
2G12: The fusion process was slowed by using a suboptimal temperature (31.5 C) to re-evaluate the potential of Abs targeting fusion intermediates to block HIV entry -- preincubation of E/T cells at 31.5 C enabled polyclonal anti-N-HR Ab and anti-six-helix bundle Abs to inhibit fusion, indicating six-helix bundles form prior to fusion -- the preincubation 31.5 C step did not alter the inhibitory activity of neutralizing Abs anti-gp41 2F5, or anti-gp120 2G12, IG1b12, 48d, and 17b.
GoldingH2002
(antibody binding site)
-
2G12: A phase I trial in seven HIV+ individuals was conducted with MAbs 2F5 and 2G12 -- no clinical or laboratory abnormalities were observed throughout the study -- eight infusions were administered over a 4-week period (total dose 14 g) -- the elimination half-life (t1/2) was calculated to be 7.94 (range, 3.46--8.31) days for 2F5 and 16.48 (range, 12.84--24.85) days for 2G12.
Armbruster2002
(kinetics, immunotherapy)
-
2G12: Chloroquine reduces the HIV-1-infectivity of H9 IIIB cells, apparently through altering the conformation of envelope -- there is a reduction of reactivity of 2G12 to its epitope in chloroquine treated cultures.
Savarino2001
(antibody binding site)
-
2G12: Twenty HIV clade C isolates from five different countries were susceptible to neutralization by anti-clade B MAbs in a synergistic quadruple combination of mAbs IgG1b12, 2G12, 2F5, and 4E10.
Xu2001
(antibody interactions, variant cross-reactivity, subtype comparisons)
-
2G12: A combination of MAbs IgG1b12, 2F5, and 2G12 was given postnatally to four neonates macaques that were then challenged with highly pathogenic SHIV89.6P -- one of the four infants remained uninfected after oral challenge, two infants had no or a delayed CD4(+) T-cell decline.
HofmannLehmann2001
(immunoprophylaxis, mother-to-infant transmission)
-
2G12: A panel of 12 MAbs was used to identify those that could neutralize the dual-tropic primary isolate HIV-1 89.6 -- six gave significant neutralization at 2 to 10 ug/ml: 2F5, 50-69, IgG1b12, 447-52D, 2G12, and 670-D six did not have neutralizing activity: 654-D, 4.8D, 450-D, 246-D, 98-6, and 1281 -- no synergy, only additive effects were seen for pairwise combinations of MAbs, and antagonism was noted between gp41 MAbs 50-69 and 98-6, as well as 98-6 and 2F5.
Verrier2001
(antibody interactions)
-
2G12: A luciferase-reporter gene-expressing T-cell line was developed to facilitate neutralization and drug-sensitivity assays -- luciferase and p24 antigen neutralization titer end points were found comparable using NAb from sera from HIV+ donors, and MAbs 2F5, 2G12 and IgG1b12.
Spenlehauer2001
(assay or method development)
-
2G12: Neutralizing synergy between MAbs 1b12, 2G12 and 2F5 was studied using surface plasmon resonance to determine the binding kinetics for these three MAbs with respect to monomeric and oligomeric Env protein gp160 IIIB -- the 2G12 epitope is highly accessible on both monomeric and oligomeric Envs, 1b12 is highly accessible on monomers but not oligomers, and 2F5 on neither form -- binding of 2G12 exposes the 2F5 epitope on gp160 oligomers -- 2G12-gp160 oligomer interactions were best fitted to a two state model, with the first complex having a high association constant and fast dissociation, stabilized by conformational changes induced by the binding of a second MAb.
ZederLutz2001
(antibody binding site, antibody interactions, kinetics)
-
2G12: Structural aspects of the interaction of neutralizing Abs with HIV-1 Env are reviewed -- Env essentially has three faces, one is largely inaccessible on the native trimer, and two that exposed but have low immunogenicity on primary viruses -- neutralization is suggested to occur by inhibition of the interaction between gp120 and the target cell membrane receptors as a result of steric hindrance and it is noted that the attachment of approximately 70 IgG molecules per virion is required for neutralization, which is equivalent to about one IgG molecule per spike -- the 2G12, 17b and b12 epitopes are discussed in detail -- although it is potently neutralizing, 2G12 does not interfere with CD4 and coreceptor binding, and this Ab specificity is uncommon in sera from HIV-1-infected individuals.
Poignard2001
(antibody binding site, review)
-
2G12: Moore and colleagues review structural aspects of gp120 and how they relate to antigenic domains, and review the data concerning the lack of a clear relationship between genetic subtype and serotype -- an exception exists for human MAb 2G12, which does not recognize CRF01 envelopes because of an unusual additional disulfide bond in the V4 loop region that appears to be unique to the subtype E, CRF01 gp120 protein.
Moore2001
(antibody binding site, review)
-
2G12: SF162DeltaV2 is a virus that has a 30 amino acids deletion in the V2 loop that does not abrogate its infectivity but renders it highly susceptible to neutralization -- when incorporated into a codon-optimized DNA vaccine with a CMV promoter and delivered by gene gun, SF162DeltaV2 gave higher neutralizing Ab titers against SF162 than did SF162 itself, and Abs that cross-neutralized non-homologous primary isolates were obtained only when SF162DeltaV2, but not intact SF162, was used as the immunogen -- Control MAbs 2F5 and 2G12 could neutralize all of the following primary isolates: 91US056(R5), 92US714(R5), 92US660(R5), 92HT593(R5X4), and BZ167(R5X4), while after the first protein boost, the sera from two SF162DeltaV2 immunized macaques could neutralize 91US056(R5), 92US714(R5), 92US660(R5) and ADA(R5), but not 92HT593(R5X4) or 92US657(R5) -- the pattern of cross-recognition shifted after the second boost.
Barnett2001a
(vaccine antigen design)
-
2G12: Review of studies in macaques that have shown immune control of pathogenic SHIV viremia, improved clinical outcome, and protection, and the implications of the observations for HIV vaccines.
Mascola2001
(review)
-
2G12: Neutralization synergy between anti-HIV NAbs b12, 2G12, 2F5, and 4E10 was studied -- a classic fixed-ratio method was used, as well as a method where one Ab was fixed at a low neutralization titer and the other was varied -- using primary isolates, a two-four fold enhancement of neutralization was observed with MAb pairs, and a ten-fold enhancement with a quadruple Ab combination -- no synergy was observed with any MAb pair in the neutralization of TCLA strain HXB2 -- there was no evidence for cooperativity of binding between b12 and 2G12 to envelope spikes expressed on the cell surface of TCLA or primary isolates.
Zwick2001c
(antibody interactions)
-
2G12: SHIV-HXBc2 is a neutralization sensitive non-pathogenic virus, and several in vivo passages through monkey's yielded highly pathogenic SHIV KU-1 -- HXBc2 and the KU-1 clone HXBc2P3.2 differ in 12 amino acids in gp160 -- substitutions in both gp120 and gp41 reduced the ability of sCD4, IgG1b12, F105 and AG1121 to Env achieve saturation and full occupancy, and neutralize KU-1 -- 17b and 2F5 also bound less efficiently to HXBc2P3.2, although 2G12 was able to bind both comparably.
Si2001
-
2G12: Six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- 2G12 was an exception and could not neutralize MN in either form.
Park2000
-
2G12: To determine the antigenicity of virus killed by thermal and chemical inactivation, retention of conformation-dependent neutralization epitopes was examined, and exposure of CD4BS epitopes was found to be enhanced (MAbs IgG1b12, 205-46-9, and 205-43-1) -- binding to 2G12 and 447-52D epitopes was essentially unaltered -- the 17b CD4i epitope was also exposed.
Grovit-Ferbas2000
(vaccine antigen design)
-
2G12: A triple combination of 2F5, F105 and 2G12 effectively neutralized perinatal infection of macaque infants when challenged with SHIV-vpu+ -- the mean plasma half-life was 14.0 +/- 7.9 days, the longest of the three Abs.
Baba2000
(immunoprophylaxis, mother-to-infant transmission)
-
2G12: A mini-review of observations of passive administration of IgG NAbs conferring protection against intervenous or vaginal SHIV challenge, that considers why IgG MAbs might protect against mucosal challenge. Database note: First author "RobertGuroff" is also found as "Robert-Guroff" on annotated papers in this database.
RobertGuroff2000
(genital and mucosal immunity, immunoprophylaxis, review)
-
2G12: The MAbs with the broadest neutralizing activity, IgG1b12, 2G12 and 2F5, all have high affinity for the native trimer, indicating that they were raised in an immune response to the oligomer on the virion surface rather than dissociated subunits -- a disulfide linked gp120-gp41 (SOS gp140) was created by introducing A501C and T605C mutations to mimic the native conformation of Env and explore its potential as an immunogen -- SOS gp140 is recognized by NAbs IgG1b12, 2G12, and CD4-IgG2, and also by anti-V3 MAbs 19b and 83.1 -- SOSgp140 is not recognized by C4 region MAbs that neutralize only TCLA strains, G3-42 and G3-519 -- nor did it bind C11, 23A, and M90, MAbs that bind to gp120 C1 and C5, where it interacts with gp41 -- MAbs that bind CD4 inducible epitopes, 17b and A32 were very strongly induced by CD4 in SOS gp140 -- anti-gp41 MAbs that bind in the region that interacts with gp120, 7B2, 2.2B, T4, T15G1 and 4D4, did not bind to SOSgp140, in contrast to 2F5, which binds to the only gp41 epitope that is well exposed in native gp120-gp41 complexes.
Binley2000
(antibody binding site, vaccine antigen design)
-
2G12: Because HIV-1 is most often transmitted across mucosal surfaces, the ability of passive transfer of infused HIVIG/2F5/2G12 to protect against mucosal exposure of macaques to pathogenic SHIV 89.6PD was studied -- HIVIG/2F5/2G12 protected 4/5 animals against vaginal challenge, 2F5/2G12 combined protected 2/5 animals, and 2G12 alone protected 2/4 animals -- in contrast, Mascola and co-workers had previously shown single MAbs could not protect against intervenous challenge -- Ab treated animals that got infected through vaginal inoculation had low viral loads and only modest declines in CD4 counts -- the infused Abs were detected in the nasal, vaginal, and oral mucosa.
Mascola2000a
(genital and mucosal immunity, immunoprophylaxis)
-
2G12: Combinations of HIVIG, 2F5, 2G12 were administered in passive-transfer experiments 24 hours prior to challenge with pathogenic SHIV 89.6PD -- 3/6 animals given HIVIG/2F5/2G12 were completely protected, the others had reduced viremia and normal CD4 counts -- 1/3 monkeys given 2F5/2G12 showed transient infection, the other two had reduced viral load -- all monkeys that received HIVIG, 2F5, or 2G12 alone became infected and developed high-level plasma viremia, although animals that got HIVIG or 2G12 had a less profound CD4 T cell decline.
Mascola1999
(antibody interactions)
-
2G12: Review of the neutralizing Ab response to HIV-1.
Parren1999
(review)
-
2G12: Hu-PBL-SCID mice were infected with HIV-1s JRCSF and SF162 to study the effect of NAbs on an established infection -- no significant differences in the initial rate of decrease in viral load or the plateau levels of viral RNA between the b12 treated and control mice were seen -- in most of the Ab treated mice b12 escape mutants were observed with varying patterns of mutations -- a combination of b12, 2G12 and 2F5 protected 1/3 mice, and an isolate from one of the other two was resistant to neutralization by all three MAbs.
Poignard1999
(antibody interactions, escape)
-
2G12: A Semliki Forest virus (SFV) expression system carrying BX08 Env was used to study the conformation of gp120 Env -- intracytoplasmic gp120 was recognized by the anti-V3 MAbs K24 and F5.5, while gp120 at the plasma membrane was detected only by conformation dependent MAbs 2G12, 670-D and 694/98D and not V3 MAbs -- expression in rat brain also showed that surface expressed Env was recognized only by the conformation-dependent Abs and not by anti-V3 Abs.
Altmeyer1999
-
2G12: rgp120 derived from a R5X4 subtype B virus was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- 2G12 was able to bind with low affinity to the rgp120 monomer HIV-1 W61D.
Beddows1999
-
2G12: A meeting summary presented results regarding neutralization --MAbs 2G12 and 2F5 tested for their ability to neutralize primary isolate infection of genetically engineered cell lines (cMAGI and others, presented by T. Matthews, A. Trkola, J. Bradac) -- an advantage of such cells lines over PBMCs is that markers (X-Gal) can be added for staining to simplify the assay -- the consensus of the meeting was that these engineered cell lines did not improve the sensitivity of detection of primary isolate neutralization -- D. Burton and J. Mascola presented results concerning passive immunization and protection of hu-PBL-SCID mice and macaques, respectively, and both found combinations of MAbs that were able to achieve 99% neutralization in vitro corresponded to efficacy in vivo.
Montefiori1999
(review)
-
2G12: Infection of dendritic cells cultured from CD14+ blood cells or from cadaveric human skin was blocked by neutralizing MAbs IgG1b12, or 2F5 and 2G12 delivered together, but not by control non-neutralizing anti-gp120 MAb 4.8D, indicating that NAbs could interrupt early mucosal transmission events.
Frankel1998
(genital and mucosal immunity)
-
2G12: In a study of the influence of the glycan at position 306 of the V3 loop on MAb recognition, 2G12 was found to neutralize an HIV-BRU mutant virus that lacks the V3 loop glycan and has a mutation at the tip of the loop more efficiently than it neutralizes HIV-BRU.
Schonning1998
(antibody binding site)
-
2G12: The complete V, J and D(H) domain was sequenced -- unlike non-neutralizing anti-gp41 MAb 3D6, five neutralizing MAbs (2F5, 2G12, 1B1, 1F7, and 3D5) showed extensive somatic mutations giving evidence of persistent antigenic pressure over long periods -- 2G12 D(H) has the best homology to a D(H) segment between D3-22 and D4-23, a region not usually considered for heavy-chain rearrangement because it lacks associated recombination signals in the flanking regions, Kunert et al. suggest this may be why Abs that compete with 2G12 are rare.
Kunert1998
(antibody sequence)
-
2G12: Review of the antigenic and receptor binding-domains of gp120 in relation to the structure of the molecule -- MAbs are discussed by category (anti-V2, anti-V3, CD4i, CD4BS...), however as 2G12 binds to a rarely immunogenic region, and it is dependent on glycosylation, it was discussed individually.
Wyatt1998a
(review)
-
2G12: Neutralization synergy was observed when the MAbs 694/98-D (V3), 2F5 (gp41), and 2G12 (gp120 discontinuous) were used in combination, and even greater neutralizing potential was seen with the addition of a fourth MAb, F105 (CD4 BS).
Li1998
(antibody interactions)
-
2G12: MAbs 2G12, 2F5 and b12 are broadly neutralizing, as are some human polyconal sera, but this paper describes a set of primary isolates that are resistant to all three MAbs and 2 broadly neutralizing sera -- results indicate that resistance levels of pediatric isolates might be higher than adult isolates -- resistance in general did not seem to be conferred by a loss of binding affinity for gp120 or gp41, rather by a more global perturbation of oligomeric Envelope.
Parren1998a
(variant cross-reactivity)
-
2G12: Induces complement-mediated lysis in MN but not primary isolates -- primary isolates are refractive to CML.
Takefman1998
(complement, variant cross-reactivity)
-
2G12: Notes that 2G12 and 2F5, potent neutralizing antibodies, were identified by screening for cell surface (oligomeric Envelope) reactivity.
Fouts1998
(antibody binding site)
-
2G12: A wide range of neutralizing titers was observed that was independent of co-receptor usage.
Trkola1998
(co-receptor, variant cross-reactivity)
-
2G12: A panel of MAbs were shown to bind with similar or greater affinity and similar competition profiles to a deglycosylated or variable loop deleted core gp120 protein (Delta V1, V2, and V3), thus such a core protein produces a structure closely approximating full length folded monomer -- MAb 2G12 was the only exception to this, showing reduced binding efficiency.
Binley1998
(antibody binding site)
-
2G12: Does not compete with binding of MAb generated in response to gp120-CD4 complex, CG10.
Sullivan1998
(antibody interactions)
-
2G12: Ab from gp120 vaccinated individuals prior to infection, who subsequently became HIV infected, could not achieve 90% neutralization of the primary virus by which the individuals were ultimately infected -- these viruses were not particularly refractive to neutralization, as determined by their susceptibility to neutralization by MAbs 2G12, IgG1b12, 2F5 and 447-52D.
Connor1998
-
2G12: Enhances Hx10 binding to CD4 positive or negative HeLa cells, but inhibited binding to CD4+ T-cell line A3.01 -- neutralizes Hx10 infection of the HeLa cells.
Mondor1998
-
2G12: Summary of the implications of the crystal structure of gp120 combined with what is known about mutations that reduce NAb binding -- probable mechanism of neutralization by 2G12 is unknown, but dependent on proper glycosylation and 2G12 is predicted to be oriented toward the target cell when bound, so neutralization may be due to steric hindrance -- mutations in positions N 295, T 297, S 334, N 386, N 392 and N 397 HXBc2 (IIIB) decrease 2G12 binding, and the binding region is 25 angstroms from the CD4 binding site -- probably the Ab binds in part to carbohydrates, which may account for both its broad reactivity and the scarcity of Abs in the same competition group.
Wyatt1998
(antibody binding site)
-
2G12: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope.
Parren1998
(antibody binding site)
-
2G12: Post-exposure prophylaxis was effective when MAb 694/98-D was delivered 15 min post-exposure to HIV-1 LAI in hu-PBL-SCID mice, but declined to 50% if delivered 60 min post-exposure, and similar time constraints have been observed for HIVIG, 2F5 and 2G12, in contrast to MAb BAT123 that could protect when delivered 4 hours post infection.
Andrus1998
(immunoprophylaxis)
-
2G12: Neutralizes TCLA strains and primary isolates.
Parren1997
(variant cross-reactivity)
-
2G12: Review that discusses this MAb -- reacts with residues at the base of the V3 loop and V4, and most of the changes that reduce binding are glycosylation sites -- it is not clear whether the binding site is peptidic or direct carbohydrate.
Burton1997
(antibody binding site, review)
-
2G12: Viral binding inhibition by 2G12 was strongly correlated with neutralization (all other neutralizing MAbs tested showed some correlation except 2F5).
Ugolini1997
(antibody binding site)
-
2G12: Using concentrations of Abs achievable in vivo, the triple combination of 2F5, 2G12 and HIVIG was found to be synergistic to have the greatest breadth and magnitude of response against 15 clade B primary isolates.
Mascola1997
(antibody interactions, variant cross-reactivity)
-
2G12: Review: MAbs 2F5, 2G12 and IgG1b12 have potential for use in combination with CD4-IgG2 as an immunotherapeutic or immunoprophylactic -- homologous MAbs to these are rare in humans and vaccine strategies should consider including constructs that may enhance exposure of these MAbs' epitopes.
Moore1997
(immunoprophylaxis, immunotherapy, review)
-
2G12: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB Env -- 2G12 was a strong neutralizer of SHIV-vpu+ -- all Ab combinations tested showed synergistic neutralization -- 2G12 has synergistic response with MAbs 694/98-D (anti-V3), 2F5, F105, and b12.
Li1997
(antibody interactions)
-
2G12: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 2G12 bound monomer, and weakly bound oligomer and neutralized JRFL.
Fouts1997
(antibody binding site)
-
2G12: A JRCSF variant that was selected for IgG1b12 resistance remained sensitive to MAbs 2G12 and 2F5, for combination therapy.
Mo1997
(escape)
-
2G12: In a multilab evaluation of monoclonal antibodies, only IgG1b12, 2G12, and 2F5 could neutralize at least half of the 9 primary test isolates at a concentration of < 25 mug per ml for 90% viral inhibition -- neutralized 6 of 9 primary isolates.
DSouza1997
(variant cross-reactivity)
-
2G12: Review: Only four epitopes have been described which can stimulate a useful neutralizing response to a broad spectrum of primary isolates, represented by the binding sites of MAbs: 447-52-D, 2G12, Fab b12, and 2F5.
Sattentau1996
(review)
-
2G12: Neutralizes primary isolates, HXB2, and chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
(variant cross-reactivity)
-
2G12: Neutralizes JR-FL -- inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study.
Trkola1996b
(co-receptor)
-
2G12: Review: exceptional capacity to neutralize primary isolates in terms of both breadth and potency -- one of three MAbs (IgG1b12, 2G12, and 2F5) generally accepted as having significant potency against primary isolates.
Poignard1996
(variant cross-reactivity, review)
-
2G12: Review: binding site is distinct from CD4BS MAbs epitope and is unique among known gp120 MAbs, human or rodent.
Moore1995c
(review)
-
2G12: Binding weakly enhanced by some anti-C1, -C4, -V3, and CD4 binding site MAbs -- unusual in that 2G12 binding neither enhanced or inhibited the binding of other MAbs included in the study.
Moore1996
(antibody interactions)
-
2G12: Conformationally sensitive epitope destroyed by mutations altering the N-linked glycosylation sites near the base of the V3 loop and the amino-terminal flank of the V4 loop.
Trkola1996
(antibody binding site, effector function)
-
2G12: Highly potent Cross-clade neutralizing activity.
Trkola1995a
(subtype comparisons)
-
2G12: Human MAb generated by electrofusion of PBL from HIV-1+ volunteers with CB-F7 cells.
Buchacher1994
(antibody generation)
References
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565 references.
Isolation Paper
Buchacher1994
A. Buchacher, R. Predl, K. Strutzenberger, W. Steinfellner, A. Trkola, M. Purtscher, G. Gruber, C. Tauer, F. Steindl, A. Jungbauer, and H. Katinger. Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization. AIDS Res. Hum. Retroviruses, 10:359-369, 1994. A panel of 33 human monoclonal antibodies were produced. Linear epitopes for some of this set of MAbs were mapped using peptide ELISA. Linear epitopes were mapped in gp41, and a single epitope was mapped in p24. While multiple gp120 specific MAbs were generated, all seemed to be conformational or carbohydrate dependent, or both. PubMed ID: 7520721.
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Abrahamyan2003b
L. G. Abrahamyan, R. M. Markosyan, J. P. Moore, F. S. Cohen, and G. B. Melikyan. Human Immunodeficiency Virus Type 1 Env with an Intersubunit Disulfide Bond Engages Coreceptors but Requires Bond Reduction after Engagement To Induce Fusion. J. Virol., 77(10):5829-5836, May 2003. PubMed ID: 12719576.
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Alam2017
S. Munir Alam, Baptiste Aussedat, Yusuf Vohra, R. Ryan Meyerhoff, Evan M. Cale, William E. Walkowicz, Nathan A. Radakovich, Kara Anasti, Lawrence Armand, Robert Parks, Laura Sutherland, Richard Scearce, M. Gordon Joyce, Marie Pancera, Aliaksandr Druz, Ivelin S. Georgiev, Tarra Von Holle, Amanda Eaton, Christopher Fox, Steven G. Reed, Mark Louder, Robert T. Bailer, Lynn Morris, Salim S. Abdool-Karim, Myron Cohen, Hua-Xin Liao, David C. Montefiori, Peter K. Park, Alberto Fernández-Tejada, Kevin Wiehe, Sampa Santra, Thomas B. Kepler, Kevin O. Saunders, Joseph Sodroski, Peter D. Kwong, John R. Mascola, Mattia Bonsignori, M. Anthony Moody, Samuel Danishefsky, and Barton F. Haynes. Mimicry of an HIV Broadly Neutralizing Antibody Epitope with a Synthetic Glycopeptide. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298421.
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Albu2003
Diana I. Albu, Agnes Jones-Trower, Amy M. Woron, Kathleen Stellrecht, Christopher C. Broder, and Dennis W. Metzger. Intranasal Vaccination Using Interleukin-12 and Cholera Toxin Subunit B as Adjuvants To Enhance Mucosal and Systemic Immunity to Human Immunodeficiency Virus Type 1 Glycoproteins. J. Virol., 77(10):5589-5597, May 2003. PubMed ID: 12719551.
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Alexandre2010
Kabamba B. Alexandre, Elin S. Gray, Bronwen E. Lambson, Penny L. Moore, Isaac A. Choge, Koleka Mlisana, Salim S. Abdool Karim, James McMahon, Barry O'Keefe, Rachel Chikwamba, and Lynn Morris. Mannose-Rich Glycosylation Patterns on HIV-1 Subtype C gp120 and Sensitivity to the Lectins, Griffithsin, Cyanovirin-N and Scytovirin. Virology, 402(1):187-196, 20 Jun 2010. PubMed ID: 20392471.
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Altmeyer1999
R. Altmeyer, E. Mordelet, M. Girard, and C. Vidal. Expression and detection of macrophage tropic HIV-1 gp120 in the brain using conformation-dependent antibodies. Virology, 259:314-21, 1999. PubMed ID: 10388656.
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Andrus1998
L. Andrus, A. M. Prince, I. Bernal, P. McCormack, D. H. Lee, M. K. Gorny, and S. Zolla-Pazner. Passive immunization with a human immunodeficiency virus type 1- neutralizing monoclonal antibody in Hu-PBL-SCID mice: isolation of a neutralization escape variant. J. Infect. Dis., 177:889-97, 1998. PubMed ID: 9534960.
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Armbruster2002
Christine Armbruster, Gabriela M. Stiegler, Brigitta A. Vcelar, Walter Jager, Nelson L. Michael, Norbert Vetter, and Hermann W. D. Katinger. A phase I trial with two human monoclonal antibodies (hMAb 2F5, 2G12) against HIV-1. AIDS, 16(2):227-233, 25 Jan 2002. PubMed ID: 11807307.
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Astronomo2008
Rena D. Astronomo, Hing-Ken Lee, Christopher N. Scanlan, Ralph Pantophlet, Cheng-Yuan Huang, Ian A. Wilson, Ola Blixt, Raymond A. Dwek, Chi-Huey Wong, and Dennis R. Burton. A Glycoconjugate Antigen Based on the Recognition Motif of a Broadly Neutralizing Human Immunodeficiency Virus Antibody, 2G12, Is Immunogenic but Elicits Antibodies Unable To Bind to the Self Glycans of gp120. J. Virol., 82(13):6359-6368, Jul 2008. PubMed ID: 18434393.
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Baan2013
Elly Baan, Anthony de Ronde, Martijn Stax, Rogier W. Sanders, Stanley Luchters, Joseph Vyankandondera, Joep M. Lange, Georgios Pollakis, and William A. Paxton. HIV-1 Autologous Antibody Neutralization Associates with Mother to Child Transmission. PLoS One, 8(7):e69274, 2013. PubMed ID: 23874931.
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Baba2000
T. W. Baba, V. Liska, R. Hofmann-Lehmann, J. Vlasak, W. Xu, S. Ayehunie, L. A. Cavacini, M. R. Posner, H. Katinger, G. Stiegler, B. J. Bernacky, T. A. Rizvi, R. Schmidt, L. R. Hill, M. E. Keeling, Y. Lu, J. E. Wright, T. C. Chou, and R. M. Ruprecht. Human neutralizing monoclonal antibodies of the IgG1 subtype protect. Nat. Med., 6:200-6, 2000. PubMed ID: 10655110.
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Balzarini2007
Jan Balzarini. Carbohydrate-Binding Agents: A Potential Future Cornerstone for the Chemotherapy of Enveloped Viruses? Antivir. Chem. Chemother., 18(1):1-11, 2007. PubMed ID: 17354647.
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Banerjee2009
Kaustuv Banerjee, Sofija Andjelic, Per Johan Klasse, Yun Kang, Rogier W. Sanders, Elizabeth Michael, Robert J. Durso, Thomas J. Ketas, William C. Olson, and John P. Moore. Enzymatic Removal of Mannose Moieties Can Increase the Immune Response to HIV-1 gp120 In Vivo. Virology, 389(1-2):108-121, 20 Jun 2009. PubMed ID: 19410272.
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Barbian2015
Hannah J. Barbian, Julie M. Decker, Frederic Bibollet-Ruche, Rachel P. Galimidi, Anthony P. West, Jr., Gerald H. Learn, Nicholas F. Parrish, Shilpa S. Iyer, Yingying Li, Craig S. Pace, Ruijiang Song, Yaoxing Huang, Thomas N. Denny, Hugo Mouquet, Loic Martin, Priyamvada Acharya, Baoshan Zhang, Peter D. Kwong, John R. Mascola, C. Theo Verrips, Nika M. Strokappe, Lucy Rutten, Laura E. McCoy, Robin A. Weiss, Corrine S. Brown, Raven Jackson, Guido Silvestri, Mark Connors, Dennis R. Burton, George M. Shaw, Michel C. Nussenzweig, Pamela J. Bjorkman, David D. Ho, Michael Farzan, and Beatrice H. Hahn. Neutralization Properties of Simian Immunodeficiency Viruses Infecting Chimpanzees and Gorillas. mBio, 6(2), 21 Apr 2015. PubMed ID: 25900654.
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Barnett2001a
S. W. Barnett, S. Lu, I. Srivastava, S. Cherpelis, A. Gettie, J. Blanchard, S. Wang, I. Mboudjeka, L. Leung, Y. Lian, A. Fong, C. Buckner, A. Ly, S. Hilt, J. Ulmer, C. T. Wild, J. R. Mascola, and L. Stamatatos. The ability of an oligomeric human immunodeficiency virus type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region. J. Virol., 75(12):5526--40, Jun 2001. URL: http://jvi.asm.org/cgi/content/full/75/12/5526. PubMed ID: 11356960.
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Baum2010
Linda L. Baum. Role of Humoral Immunity in Host Defense Against HIV. Curr HIV/AIDS Rep, 7(1):11-18, Feb 2010. PubMed ID: 20425053.
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Beddows1999
S. Beddows, S. Lister, R. Cheingsong, C. Bruck, and J. Weber. Comparison of the Antibody Repertoire Generated in Healthy Volunteers following Immunization with a Monomeric Recombinant gp120 Construct Derived from a CCR5/CXCR4-Using Human Immunodeficiency Virus Type 1 Isolate with Sera from Naturally Infected Individuals. J. Virol., 73:1740-1745, 1999. PubMed ID: 9882391.
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Beddows2005a
Simon Beddows, Natalie N. Zheng, Carolina Herrera, Elizabeth Michael, Kelly Barnes, John P. Moore, Rod S. Daniels, and Jonathan N. Weber. Neutralization Sensitivity of HIV-1 Env-Pseudotyped Virus Clones is Determined by Co-Operativity between Mutations Which Modulate the CD4-Binding Site and Those That Affect gp120-gp41 Stability. Virology, 337(1):136-148, 20 Jun 2005. PubMed ID: 15914227.
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Belanger2010
Julie M. Belanger, Yossef Raviv, Mathias Viard, Michael Jason de la Cruz, Kunio Nagashima, and Robert Blumenthal. Characterization of the Effects of Aryl-Azido Compounds and UVA Irradiation on the Viral Proteins and Infectivity of Human Immunodeficiency Virus Type 1. Photochem. Photobiol., 86(5):1099-1108, Sep-Oct 2010. PubMed ID: 20630026.
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Berkower2008
Ira Berkower, Chiraag Patel, Yisheng Ni, Konstantin Virnik, Zhexin Xiang, and Angelo Spadaccini. Targeted Deletion in the beta20--beta21 Loop of HIV Envelope Glycoprotein gp120 Exposes the CD4 Binding Site for Antibody Binding. Virology, 377(2):330-338, 1 Aug 2008. PubMed ID: 18519142.
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Billington2007
J. Billington, T. P. Hickling, G. H. Munro, C. Halai, R. Chung, G. G. Dodson, and R. S. Daniels. Stability of a Receptor-Binding Active Human Immunodeficiency Virus Type 1 Recombinant gp140 Trimer Conferred by Intermonomer Disulfide Bonding of the V3 Loop: Differential Effects of Protein Disulfide Isomerase on CD4 and Coreceptor Binding. J. Virol., 81(9):4604-4614, May 2007. PubMed ID: 17301129.
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Binley1997
J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287.
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Binley1998
J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908.
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Binley2000
J. Binley, R. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D. Anselma, P. Maddon, W. Olson, and J. Moore. A Recombinant Human Immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intramolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion associated structure. J. Virol., 74:627-43, 1999. PubMed ID: 10623724.
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Binley2003
James M. Binley, Charmagne S. Cayanan, Cheryl Wiley, Norbert Schülke, William C. Olson, and Dennis R. Burton. Redox-Triggered Infection by Disulfide-Shackled Human Immunodeficiency Virus Type 1 Pseudovirions. J. Virol., 77(10):5678-5684, May 2003. PubMed ID: 12719560.
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Binley2004
James M. Binley, Terri Wrin, Bette Korber, Michael B. Zwick, Meng Wang, Colombe Chappey, Gabriela Stiegler, Renate Kunert, Susan Zolla-Pazner, Hermann Katinger, Christos J. Petropoulos, and Dennis R. Burton. Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies. J. Virol., 78(23):13232-13252, Dec 2004. PubMed ID: 15542675.
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Binley2006
James M. Binley, Stacie Ngo-Abdalla, Penny Moore, Michael Bobardt, Udayan Chatterji, Philippe Gallay, Dennis R. Burton, Ian A. Wilson, John H. Elder, and Aymeric de Parseval. Inhibition of HIV Env Binding to Cellular Receptors by Monoclonal Antibody 2G12 as Probed by Fc-Tagged gp120. Retrovirology, 3:39, 2006. PubMed ID: 16817962.
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Binley2008
James M. Binley, Elizabeth A. Lybarger, Emma T. Crooks, Michael S. Seaman, Elin Gray, Katie L. Davis, Julie M. Decker, Diane Wycuff, Linda Harris, Natalie Hawkins, Blake Wood, Cory Nathe, Douglas Richman, Georgia D. Tomaras, Frederic Bibollet-Ruche, James E. Robinson, Lynn Morris, George M. Shaw, David C. Montefiori, and John R. Mascola. Profiling the Specificity of Neutralizing Antibodies in a Large Panel of Plasmas from Patients Chronically Infected with Human Immunodeficiency Virus Type 1 Subtypes B and C. J. Virol., 82(23):11651-11668, Dec 2008. PubMed ID: 18815292.
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Binley2009
James Binley. Specificities of Broadly Neutralizing Anti-HIV-1 Sera. Curr. Opin. HIV AIDS, 4(5):364-372, Sep 2009. PubMed ID: 20048699.
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Binley2010
James M Binley, Yih-En Andrew Ban, Emma T. Crooks, Dirk Eggink, Keiko Osawa, William R. Schief, and Rogier W. Sanders. Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization. J. Virol., 84(11):5637-5655, Jun 2010. PubMed ID: 20335257.
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Biorn2004
Alyssa C. Biorn, Simon Cocklin, Navid Madani, Zhihai Si, Tijana Ivanovic, James Samanen, Donald I. Van Ryk, Ralph Pantophlet, Dennis R. Burton, Ernesto Freire, Joseph Sodroski, and Irwin M. Chaiken. Mode of Action for Linear Peptide Inhibitors of HIV-1 gp120 Interactions. Biochemistry, 43(7):1928-1938, 24 Feb 2004. PubMed ID: 14967033.
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Blay2006
W. M. Blay, S. Gnanakaran, B. Foley, N. A. Doria-Rose, B. T. Korber, and N. L. Haigwood. Consistent Patterns of Change During the Divergence of Human Immunodeficiency Virus Type 1 Envelope from That of the Inoculated Virus in Simian/Human Immunodeficiency Virus-Infected Macaques. J. Virol., 80(2):999-1014, Jan 2006. PubMed ID: 16379001.
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Blay2007
Wendy M. Blay, Theresa Kasprzyk, Lynda Misher, Barbra A. Richardson, and Nancy L. Haigwood. Mutations in Envelope gp120 Can Impact Proteolytic Processing of the gp160 Precursor and Thereby Affect Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Pseudoviruses. J. Virol., 81(23):13037-13049, Dec 2007. PubMed ID: 17855534.
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Blish2007
Catherine A. Blish, Wendy M. Blay, Nancy L. Haigwood, and Julie Overbaugh. Transmission of HIV-1 in the Face of Neutralizing Antibodies. Curr. HIV Res., 5(6):578-587, Nov 2007. PubMed ID: 18045114.
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Blish2009
Catherine A. Blish, Zahra Jalalian-Lechak, Stephanie Rainwater, Minh-An Nguyen, Ozge C. Dogan, and Julie Overbaugh. Cross-Subtype Neutralization Sensitivity Despite Monoclonal Antibody Resistance among Early Subtype A, C, and D Envelope Variants of Human Immunodeficiency Virus Type 1. J. Virol., 83(15):7783-7788, Aug 2009. PubMed ID: 19474105.
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Bontjer2009
Ilja Bontjer, Aafke Land, Dirk Eggink, Erwin Verkade, Kiki Tuin, Chris Baldwin, Georgios Pollakis, William A. Paxton, Ineke Braakman, Ben Berkhout, and Rogier W. Sanders. Optimization of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins with V1/V2 Deleted, Using Virus Evolution. J. Virol., 83(1):368-383, Jan 2009. PubMed ID: 18922866.
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Bontjer2010
Ilja Bontjer, Mark Melchers, Dirk Eggink, Kathryn David, John P. Moore, Ben Berkhout, and Rogier W. Sanders. Stabilized HIV-1 Envelope Glycoprotein Trimers Lacking the V1V2 Domain, Obtained by Virus Evolution. J. Biol. Chem, 285(47):36456-36470, 19 Nov 2010. PubMed ID: 20826824.
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Borggren2011
Marie Borggren, Johanna Repits, Jasminka Sterjovski, Hannes Uchtenhagen, Melissa J. Churchill, Anders Karlsson, Jan Albert, Adnane Achour, Paul R. Gorry, Eva Maria Fenyö, and Marianne Jansson. Increased Sensitivity to Broadly Neutralizing Antibodies of End-Stage Disease R5 HIV-1 Correlates with Evolution in Env Glycosylation and Charge. PLoS One, 6(6):e20135, 2011. PubMed ID: 21698221.
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Bouvin-Pley2014
M. Bouvin-Pley, M. Morgand, L. Meyer, C. Goujard, A. Moreau, H. Mouquet, M. Nussenzweig, C. Pace, D. Ho, P. J. Bjorkman, D. Baty, P. Chames, M. Pancera, P. D. Kwong, P. Poignard, F. Barin, and M. Braibant. Drift of the HIV-1 Envelope Glycoprotein gp120 Toward Increased Neutralization Resistance over the Course of the Epidemic: A Comprehensive Study Using the Most Potent and Broadly Neutralizing Monoclonal Antibodies. J. Virol., 88(23):13910-13917, Dec 2014. PubMed ID: 25231299.
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Bowley2007
D. R. Bowley, A. F. Labrijn, M. B. Zwick, and D. R. Burton. Antigen Selection from an HIV-1 Immune Antibody Library Displayed on Yeast Yields Many Novel Antibodies Compared to Selection from the Same Library Displayed on Phage. Protein Eng. Des. Sel., 20(2):81-90, Feb 2007. PubMed ID: 17242026.
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Braibant2006
Martine Braibant, Sylvie Brunet, Dominique Costagliola, Christine Rouzioux, Henri Agut, Hermann Katinger, Brigitte Autran, and Francis Barin. Antibodies to Conserved Epitopes of the HIV-1 Envelope in Sera from Long-Term Non-Progressors: Prevalence and Association with Neutralizing Activity. AIDS, 20(15):1923-30, 3 Oct 2006. PubMed ID: 16988513.
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Braibant2013
Martine Braibant, Eun-Yeung Gong, Jean-Christophe Plantier, Thierry Moreau, Elodie Alessandri, François Simon, and Francis Barin. Cross-Group Neutralization of HIV-1 and Evidence for Conservation of the PG9/PG16 Epitopes within Divergent Groups. AIDS, 27(8):1239-1244, 15 May 2013. PubMed ID: 23343910.
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Bricault2019
Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920.
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Brown2005a
Bruce K. Brown, Janice M. Darden, Sodsai Tovanabutra, Tamara Oblander, Julie Frost, Eric Sanders-Buell, Mark S. de Souza, Deborah L. Birx, Francine E. McCutchan, and Victoria R. Polonis. Biologic and Genetic Characterization of a Panel of 60 Human Immunodeficiency Virus Type 1 Isolates, Representing Clades A, B, C, D, CRF01\_AE, and CRF02\_AG, for the Development and Assessment of Candidate Vaccines. J. Virol., 79(10):6089-6101, May 2005. PubMed ID: 15857994.
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Brown2012
Bruce K. Brown, Lindsay Wieczorek, Gustavo Kijak, Kara Lombardi, Jeffrey Currier, Maggie Wesberry, John C. Kappes, Viseth Ngauy, Mary Marovich, Nelson Michael, Christina Ochsenbauer, David C Montefiori, and Victoria R. Polonis. The Role of Natural Killer (NK) Cells and NK Cell Receptor Polymorphisms in the Assessment of HIV-1 Neutralization. PLoS One, 7(4):e29454, 2012. PubMed ID: 22509241.
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Bunnik2007
Evelien M Bunnik, Esther D Quakkelaar, Ad C. van Nuenen, Brigitte Boeser-Nunnink, and Hanneke Schuitemaker. Increased Neutralization Sensitivity of Recently Emerged CXCR4-Using Human Immunodeficiency Virus Type 1 Strains Compared to Coexisting CCR5-Using Variants from the Same Patient. J. Virol., 81(2):525-531, Jan 2007. PubMed ID: 17079299.
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Bunnik2009
Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Ad C. van Nuenen, and Hanneke Schuitemaker. Changing Sensitivity to Broadly Neutralizing Antibodies b12, 2G12, 2F5, and 4E10 of Primary Subtype B Human Immunodeficiency Virus Type 1 Variants in the Natural Course of Infection. Virology, 390(2):348-355, 1 Aug 2009. PubMed ID: 19539340.
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Bunnik2010
Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Nening M. Nanlohy, Debbie van Baarle, Ad C. van Nuenen, Ann J. Hessell, and Hanneke Schuitemaker. Emergence of Monoclonal Antibody b12-Resistant Human Immunodeficiency Virus Type 1 Variants during Natural Infection in the Absence of Humoral Or Cellular Immune Pressure. J. Gen. Virol., 91(5):1354-1364, May 2010. PubMed ID: 20053822.
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Bunnik2010a
Evelien M. Bunnik, Zelda Euler, Matthijs R. A. Welkers, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Adaptation of HIV-1 Envelope gp120 to Humoral Immunity at a Population Level. Nat. Med., 16(9):995-997, Sep 2010. PubMed ID: 20802498.
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Bures2002
Renata Bures, Lynn Morris, Carolyn Williamson, Gita Ramjee, Mark Deers, Susan A Fiscus, Salim Abdool-Karim, and David C. Montefiori. Regional Clustering of Shared Neutralization Determinants on Primary Isolates of Clade C Human Immunodeficiency Virus Type 1 from South Africa. J. Virol., 76(5):2233-2244, Mar 2002. PubMed ID: 11836401.
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Burrer2005
Renaud Burrer, Sandrine Haessig-Einius, Anne-Marie Aubertin, and Christiane Moog. Neutralizing as Well as Non-Neutralizing Polyclonal Immunoglobulin (Ig)G from Infected Patients Capture HIV-1 via Antibodies Directed against the Principal Immunodominant Domain of gp41. Virology, 333(1):102-113, 1 Mar 2005. PubMed ID: 15708596.
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Burton1997
D. R. Burton and D. C. Montefiori. The antibody response in HIV-1 infection. AIDS, 11 Suppl A:S87-S98, 1997. An excellent review of Ab epitopes and the implications for Envelope structure, neutralization of HIV, the distinction between primary and TCLA strains, ADCC and its role in clearance, and the Ab response during the course of infection. PubMed ID: 9451972.
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Burton2005
Dennis R. Burton, Robyn L. Stanfield, and Ian A. Wilson. Antibody vs. HIV in a Clash of Evolutionary Titans. Proc. Natl. Acad. Sci. U.S.A., 102(42):14943-14948, 18 Oct 2005. PubMed ID: 16219699.
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Burton2012
Dennis R. Burton, Pascal Poignard, Robyn L. Stanfield, and Ian A. Wilson. Broadly Neutralizing Antibodies Present New Prospects to Counter Highly Antigenically Diverse Viruses. Science, 337(6091):183-186, 13 Jul 2012. PubMed ID: 22798606.
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Burton2016
Dennis R. Burton and Lars Hangartner. Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. Annu. Rev. Immunol., 34:635-659, 20 May 2016. PubMed ID: 27168247.
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Cai2017
Yongfei Cai, Selen Karaca-Griffin, Jia Chen, Sai Tian, Nicholas Fredette, Christine E. Linton, Sophia Rits-Volloch, Jianming Lu, Kshitij Wagh, James Theiler, Bette Korber, Michael S. Seaman, Stephen C. Harrison, Andrea Carfi, and Bing Chen. Antigenicity-Defined Conformations of an Extremely Neutralization-Resistant HIV-1 Envelope Spike. Proc. Natl. Acad. Sci. U.S.A., 114(17):4477-4482, 25 Apr 2017. PubMed ID: 28396421.
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Calarese2003
Daniel A. Calarese, Christopher N. Scanlan, Michael B. Zwick, Songpon Deechongkit, Yusuke Mimura, Renate Kunert, Ping Zhu, Mark R. Wormald, Robyn L. Stanfield, Kenneth H. Roux, Jeffery W. Kelly, Pauline M. Rudd, Raymond A. Dwek, Hermann Katinger, Dennis R. Burton, and Ian A. Wilson. Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition. Science, 300(5628):2065-2071, 27 Jun 2003. PubMed ID: 12829775.
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Calarese2005
Daniel A. Calarese, Hing-Ken Lee, Cheng-Yuan Huang, Michael D. Best, Rena D. Astronomo, Robyn L. Stanfield, Hermann Katinger, Dennis R. Burton, Chi-Huey Wong, and Ian A. Wilson. Dissection of the Carbohydrate Specificity of the Broadly Neutralizing Anti-HIV-1 Antibody 2G12. Proc. Natl. Acad. Sci. U.S.A., 102(38):13372-13377, 20 Sep 2005. PubMed ID: 16174734.
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Canducci2009
Filippo Canducci, Maria Chiara Marinozzi, Michela Sampaolo, Stefano Berrè, Patrizia Bagnarelli, Massimo Degano, Giulia Gallotta, Benedetta Mazzi, Philippe Lemey, Roberto Burioni, and Massimo Clementi. Dynamic Features of the Selective Pressure on the Human Immunodeficiency Virus Type 1 (HIV-1) gp120 CD4-Binding Site in a Group of Long Term Non Progressor (LTNP) Subjects. Retrovirology, 6:4, 2009. PubMed ID: 19146663.
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Carbonetti2014
Sara Carbonetti, Brian G. Oliver, Jolene Glenn, Leonidas Stamatatos, and D. Noah Sather. Soluble HIV-1 Envelope Immunogens Derived from an Elite Neutralizer Elicit Cross-Reactive V1V2 Antibodies and Low Potency Neutralizing Antibodies. PLoS One, 9(1):e86905, 2014. PubMed ID: 24466285.
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Castillo-Menendez2019
Luis R. Castillo-Menendez, Hanh T. Nguyen, and Joseph Sodroski. Conformational Differences between Functional Human Immunodeficiency Virus Envelope Glycoprotein Trimers and Stabilized Soluble Trimers. J. Virol., 93(3), 1 Feb 2019. PubMed ID: 30429345.
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Cavacini2002
Lisa A. Cavacini, Mark Duval, James Robinson, and Marshall R. Posner. Interactions of Human Antibodies, Epitope Exposure, Antibody Binding and Neutralization of Primary Isolate HIV-1 Virions. AIDS, 16(18):2409-2417, 6 Dec 2002. Erratum in AIDS. 2003 Aug 15;17(12):1863. PubMed ID: 12461414.
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Cavacini2003
Lisa Cavacini, Mark Duval, Leslie Song, Rebecca Sangster, Shi-hua Xiang, Joseph Sodroski, and Marshall Posner. Conformational Changes in env Oligomer Induced by an Antibody Dependent on the V3 Loop Base. AIDS, 17(5):685-689, 28 Mar 2003. PubMed ID: 12646791.
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Chaillon2011
Antoine Chaillon, Martine Braibant, Thierry Moreau, Suzie Thenin, Alain Moreau, Brigitte Autran, and Francis Barin. The V1V2 Domain and an N-Linked Glycosylation Site in the V3 Loop of the HIV-1 Envelope Glycoprotein Modulate Neutralization Sensitivity to the Human Broadly Neutralizing Antibody 2G12. J. Virol., 85(7):3642-3648, Apr 2011. PubMed ID: 21248038.
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Chakrabarti2002
Bimal K. Chakrabarti, Wing-pui Kong, Bei-yue Wu, Zhi-Yong Yang, Jacques Friborg, Xu Ling, Steven R. King, David C. Montefiori, and Gary J. Nabel. Modifications of the Human Immunodeficiency Virus Envelope Glycoprotein Enhance Immunogenicity for Genetic Immunization. J. Virol., 76(11):5357-5368, Jun 2002. PubMed ID: 11991964.
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Cham2006
Fatim Cham, Peng Fei Zhang, Leo Heyndrickx, Peter Bouma, Ping Zhong, Herman Katinger, James Robinson, Guido van der Groen, and Gerald V. Quinnan, Jr. Neutralization and Infectivity Characteristics of Envelope Glycoproteins from Human Immunodeficiency Virus Type 1 Infected Donors Whose Sera Exhibit Broadly Cross-Reactive Neutralizing Activity. Virology, 347(1):36-51, 30 Mar 2006. PubMed ID: 16378633.
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Cheeseman2017
Hannah M. Cheeseman, Natalia J. Olejniczak, Paul M. Rogers, Abbey B. Evans, Deborah F. L. King, Paul Ziprin, Hua-Xin Liao, Barton F. Haynes, and Robin J. Shattock. Broadly Neutralizing Antibodies Display Potential for Prevention of HIV-1 Infection of Mucosal Tissue Superior to That of Nonneutralizing Antibodies. J. Virol., 91(1), 1 Jan 2017. PubMed ID: 27795431.
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Chen2005
Hongying Chen, Xiaodong Xu, Alexandra Bishop, and Ian M. Jones. Reintroduction of the 2G12 Epitope in an HIV-1 Clade C gp120. AIDS, 19(8):833-835, 20 May 2005. PubMed ID: 15867500.
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Chen2007a
Hongying Chen, Xiaodong Xu, and Ian M Jones. Immunogenicity of the Outer Domain of a HIV-1 Clade C gp120. Retrovirology, 4:33, 2007. PubMed ID: 17509143.
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Chen2008a
Hongying Chen, Xiaodong Xu, Hsin-Hui Lin, Ssu-Hsien Chen, Anna Forsman, Marlen Aasa-Chapman, and Ian M. Jones. Mapping the Immune Response to the Outer Domain of a Human Immunodeficiency Virus-1 Clade C gp120. J. Gen. Virol., 89(10):2597-2604, Oct 2008. PubMed ID: 18796729.
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Chen2009b
Weizao Chen and Dimiter S. Dimitrov. Human Monoclonal Antibodies and Engineered Antibody Domains as HIV-1 Entry Inhibitors. Curr. Opin. HIV AIDS, 4(2):112-117, Mar 2009. PubMed ID: 19339949.
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Chen2015
Jia Chen, James M. Kovacs, Hanqin Peng, Sophia Rits-Volloch, Jianming Lu, Donghyun Park, Elise Zablowsky, Michael S. Seaman, and Bing Chen. Effect of the Cytoplasmic Domain on Antigenic Characteristics of HIV-1 Envelope Glycoprotein. Science, 349(6244):191-195, 10 Jul 2015. PubMed ID: 26113642.
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Chen2016
Danying Chen, Xiaozhou He, Jingrong Ye, Pengxiang Zhao, Yi Zeng, and Xia Feng. Genetic and Phenotypic Analysis of CRF01\_AE HIV-1 env Clones from Patients Residing in Beijing, China. AIDS Res. Hum. Retroviruses, 32(10-11):1113-1124, Nov 2016. PubMed ID: 27066910.
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Chen2016b
Yajing Chen, Richard Wilson, Sijy O'Dell, Javier Guenaga, Yu Feng, Karen Tran, Chi-I Chiang, Heather E. Arendt, Joanne DeStefano, John R. Mascola, Richard T. Wyatt, and Yuxing Li. An HIV-1 Env-Antibody Complex Focuses Antibody Responses to Conserved Neutralizing Epitopes. J. Immunol., 197(10):3982-3998, 15 Nov 2016. PubMed ID: 27815444.
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Chenine2018
Agnes-Laurence Chenine, Melanie Merbah, Lindsay Wieczorek, Sebastian Molnar, Brendan Mann, Jenica Lee, Anne-Marie O'Sullivan, Meera Bose, Eric Sanders-Buell, Gustavo H. Kijak, Carolina Herrera, Robert McLinden, Robert J. O'Connell, Nelson L. Michael, Merlin L. Robb, Jerome H. Kim, Victoria R. Polonis, and Sodsai Tovanabutra. Neutralization Sensitivity of a Novel HIV-1 CRF01\_AE Panel of Infectious Molecular Clones. J. Acquir. Immune Defic. Syndr., 78(3):348-355, 1 Jul 2018. PubMed ID: 29528942.
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Ching2008
Lance K. Ching, Giorgos Vlachogiannis, Katherine A. Bosch, and Leonidas Stamatatos. The First Hypervariable Region of the gp120 Env Glycoprotein Defines the Neutralizing Susceptibility of Heterologous Human Immunodeficiency Virus Type 1 Isolates to Neutralizing Antibodies Elicited by the SF162gp140 Immunogen. J. Virol., 82(2):949-956, Jan 2008. PubMed ID: 18003732.
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Ching2010
Lance Ching and Leonidas Stamatatos. Alterations in the Immunogenic Properties of Soluble Trimeric Human Immunodeficiency Virus Type 1 Envelope Proteins Induced by Deletion or Heterologous Substitutions of the V1 Loop. J. Virol., 84(19):9932-9946, Oct 2010. PubMed ID: 20660181.
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Choe2003
Hyeryun Choe, Wenhui Li, Paulette L. Wright, Natalya Vasilieva, Miro Venturi, Chih-Chin Huang, Christoph Grundner, Tatyana Dorfman, Michael B. Zwick, Liping Wang, Eric S. Rosenberg, Peter D. Kwong, Dennis R. Burton, James E. Robinson, Joseph G. Sodroski, and Michael Farzan. Tyrosine Sulfation of Human Antibodies Contributes to Recognition of the CCR5 Binding Region of HIV-1 gp120. Cell, 114(2):161-170, 25 Jul 2003. PubMed ID: 12887918.
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Chomont2008
Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650.
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Chong2008
Huihui Chong, Kunxue Hong, Chuntao Zhang, Jianhui Nie, Aijing Song, Wei Kong, and Youchun Wang. Genetic and Neutralization Properties of HIV-1 env Clones from Subtype B/BC/AE Infections in China. J. Acquir. Immune Defic. Syndr., 47(5):535-543, 15 Apr 2008. PubMed ID: 18209676.
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Chuang2017
Gwo-Yu Chuang, Hui Geng, Marie Pancera, Kai Xu, Cheng Cheng, Priyamvada Acharya, Michael Chambers, Aliaksandr Druz, Yaroslav Tsybovsky, Timothy G. Wanninger, Yongping Yang, Nicole A. Doria-Rose, Ivelin S. Georgiev, Jason Gorman, M. Gordon Joyce, Sijy O'Dell, Tongqing Zhou, Adrian B. McDermott, John R. Mascola, and Peter D. Kwong. Structure-Based Design of a Soluble Prefusion-Closed HIV-1 Env Trimer with Reduced CD4 Affinity and Improved Immunogenicity. J. Virol., 91(10), 15 May 2017. PubMed ID: 28275193.
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Chuang2019
Gwo-Yu Chuang, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, Tongqing Zhou, Robert T. Bailer, Venkata P. Dandey, Nicole A. Doria-Rose, Mark K. Louder, Krisha McKee, John R. Mascola, Lawrence Shapiro, and Peter D. Kwong. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure, 27(1):196-206.e6, 2 Jan 2019. PubMed ID: 30471922.
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Chun2014
Tae-Wook Chun, Danielle Murray, Jesse S. Justement, Jana Blazkova, Claire W. Hallahan, Olivia Fankuchen, Kathleen Gittens, Erika Benko, Colin Kovacs, Susan Moir, and Anthony S. Fauci. Broadly Neutralizing Antibodies Suppress HIV in the Persistent Viral Reservoir. Proc. Natl. Acad. Sci. U.S.A., 111(36):13151-13156, 9 Sep 2014. PubMed ID: 25157148.
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Connor1998
R. I. Connor, B. T. Korber, B. S. Graham, B. H. Hahn, D. D. Ho, B. D. Walker, A. U. Neumann, S. H. Vermund, J. Mestecky, S. Jackson, E. Fenamore, Y. Cao, F. Gao, S. Kalams, K. J. Kunstman, D. McDonald, N. McWilliams, A. Trkola, J. P. Moore, and S. M. Wolinsky. Immunological and virological analyses of persons infected by human immunodeficiency virus type 1 while participating in trials of recombinant gp120 subunit vaccines. J. Virol., 72:1552-76, 1998. No gp120-vaccine induced antibodies in a human trial of gp120 MN and SF2 could neutralize the primary viruses that infected the vaccinees. The primary isolates from the infected vaccinees were shown not to be particularly refractive to neutralization by their susceptibility to a panel of neutralizing MAbs. PubMed ID: 9445059.
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Corti2010
Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712.
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Crawford1999
John M.. Crawford, Patricia L. Earl, Bernard Moss, Kieth A. Reimann, Michael S. Wyand, Kelledy H. Manson, Miroslawa Bilska, Jin Tao Zhou, C. David Pauza, Paul W. H. I. Parren, Dennis R. Burton, Joseph G. Sodroski, Norman L. Letvin, and David C. Montefiori. Characterization of Primary Isolate-Like Variants of Simian-Human Immunodeficiency Virus. J. Virol., 73(12):10199-10207, Dec 1999. PubMed ID: 10559336.
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Crooks2005
Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980.
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Crooks2007
Emma T. Crooks, Penny L. Moore, Michael Franti, Charmagne S. Cayanan, Ping Zhu, Pengfei Jiang, Robbert P. de Vries, Cheryl Wiley, Irina Zharkikh, Norbert Schülke, Kenneth H. Roux, David C. Montefiori, Dennis R. Burton, and James M. Binley. A Comparative Immunogenicity Study of HIV-1 Virus-Like Particles Bearing Various Forms of Envelope Proteins, Particles Bearing no Envelope and Soluble Monomeric gp120. Virology, 366(2):245-262, 30 Sep 2007. PubMed ID: 17580087.
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Crooks2008
Emma T. Crooks, Pengfei Jiang, Michael Franti, Sharon Wong, Michael B. Zwick, James A. Hoxie, James E. Robinson, Penny L. Moore, and James M. Binley. Relationship of HIV-1 and SIV Envelope Glycoprotein Trimer Occupation and Neutralization. Virology, 377(2):364-378, 1 Aug 2008. PubMed ID: 18539308.
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Crooks2011
Ema T. Crooks, Tommy Tong, Keiko Osawa, and James M. Binley. Enzyme Digests Eliminate Nonfunctional Env from HIV-1 Particle Surfaces, Leaving Native Env Trimers Intact and Viral Infectivity Unaffected. J. Virol., 85(12):5825-5839, Jun 2011. PubMed ID: 21471242.
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Crooks2015
Ema T. Crooks, Tommy Tong, Bimal Chakrabarti, Kristin Narayan, Ivelin S. Georgiev, Sergey Menis, Xiaoxing Huang, Daniel Kulp, Keiko Osawa, Janelle Muranaka, Guillaume Stewart-Jones, Joanne Destefano, Sijy O'Dell, Celia LaBranche, James E. Robinson, David C. Montefiori, Krisha McKee, Sean X. Du, Nicole Doria-Rose, Peter D. Kwong, John R. Mascola, Ping Zhu, William R. Schief, Richard T. Wyatt, Robert G. Whalen, and James M. Binley. Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site. PLoS Pathog, 11(5):e1004932, May 2015. PubMed ID: 26023780.
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Dacheux2004
Laurent Dacheux, Alain Moreau, Yasemin Ataman-Önal, François Biron, Bernard Verrier, and Francis Barin. Evolutionary Dynamics of the Glycan Shield of the Human Immunodeficiency Virus Envelope during Natural Infection and Implications for Exposure of the 2G12 Epitope. J. Virol., 78(22):12625-12637, Nov 2004. PubMed ID: 15507649.
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Danesh2020
Ali Danesh, Yanqin Ren, and R. Brad Jones. Roles of Fragment Crystallizable-Mediated Effector Functions in Broadly Neutralizing Antibody Activity against HIV. Curr. Opin. HIV AIDS, 15(5):316-323, Sep 2020. PubMed ID: 32732552.
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Davis2006
David Davis, Helen Donners, Betty Willems, Michel Ntemgwa, Tine Vermoesen, Guido van der Groen, and Wouter Janssens. Neutralization Kinetics of Sensitive and Resistant Subtype B Primary Human Immunodeficiency Virus Type 1 Isolates. J. Med. Virol., 78(7):864-786, Jul 2006. PubMed ID: 16721864.
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Decamp2014
Allan deCamp, Peter Hraber, Robert T. Bailer, Michael S. Seaman, Christina Ochsenbauer, John Kappes, Raphael Gottardo, Paul Edlefsen, Steve Self, Haili Tang, Kelli Greene, Hongmei Gao, Xiaoju Daniell, Marcella Sarzotti-Kelsoe, Miroslaw K. Gorny, Susan Zolla-Pazner, Celia C. LaBranche, John R. Mascola, Bette T. Korber, and David C. Montefiori. Global Panel of HIV-1 Env Reference Strains for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 88(5):2489-2507, Mar 2014. PubMed ID: 24352443.
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Dennison2014
S. Moses Dennison, Kara M. Anasti, Frederick H. Jaeger, Shelley M. Stewart, Justin Pollara, Pinghuang Liu, Erika L. Kunz, Ruijun Zhang, Nathan Vandergrift, Sallie Permar, Guido Ferrari, Georgia D. Tomaras, Mattia Bonsignori, Nelson L. Michael, Jerome H Kim, Jaranit Kaewkungwal, Sorachai Nitayaphan, Punnee Pitisuttithum, Supachai Rerks-Ngarm, Hua-Xin Liao, Barton F. Haynes, and S. Munir Alam. Vaccine-Induced HIV-1 Envelope gp120 Constant Region 1-Specific Antibodies Expose a CD4-Inducible Epitope and Block the Interaction of HIV-1 gp140 with Galactosylceramide. J. Virol., 88(16):9406-9417, Aug 2014. PubMed ID: 24920809.
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Depetris2012
Rafael S Depetris, Jean-Philippe Julien, Reza Khayat, Jeong Hyun Lee, Robert Pejchal, Umesh Katpally, Nicolette Cocco, Milind Kachare, Evan Massi, Kathryn B. David, Albert Cupo, Andre J. Marozsan, William C. Olson, Andrew B. Ward, Ian A. Wilson, Rogier W. Sanders, and John P Moore. Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers. J. Biol. Chem., 287(29):24239-24254, 13 Jul 2012. PubMed ID: 22645128.
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Derby2006
Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322.
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Derking2015
Ronald Derking, Gabriel Ozorowski, Kwinten Sliepen, Anila Yasmeen, Albert Cupo, Jonathan L. Torres, Jean-Philippe Julien, Jeong Hyun Lee, Thijs van Montfort, Steven W. de Taeye, Mark Connors, Dennis R. Burton, Ian A. Wilson, Per-Johan Klasse, Andrew B. Ward, John P. Moore, and Rogier W. Sanders. Comprehensive Antigenic Map of a Cleaved Soluble HIV-1 Envelope Trimer. PLoS Pathog, 11(3):e1004767, Mar 2015. PubMed ID: 25807248.
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deTaeye2015
Steven W. de Taeye, Gabriel Ozorowski, Alba Torrents de la Peña, Miklos Guttman, Jean-Philippe Julien, Tom L. G. M. van den Kerkhof, Judith A. Burger, Laura K. Pritchard, Pavel Pugach, Anila Yasmeen, Jordan Crampton, Joyce Hu, Ilja Bontjer, Jonathan L. Torres, Heather Arendt, Joanne DeStefano, Wayne C. Koff, Hanneke Schuitemaker, Dirk Eggink, Ben Berkhout, Hansi Dean, Celia LaBranche, Shane Crotty, Max Crispin, David C. Montefiori, P. J. Klasse, Kelly K. Lee, John P. Moore, Ian A. Wilson, Andrew B. Ward, and Rogier W. Sanders. Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-Neutralizing Epitopes. Cell, 163(7):1702-1715, 17 Dec 2015. PubMed ID: 26687358.
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deTaeye2018
Steven W. de Taeye, Alba Torrents de la Peña, Andrea Vecchione, Enzo Scutigliani, Kwinten Sliepen, Judith A. Burger, Patricia van der Woude, Anna Schorcht, Edith E. Schermer, Marit J. van Gils, Celia C. LaBranche, David C. Montefiori, Ian A. Wilson, John P. Moore, Andrew B. Ward, and Rogier W. Sanders. Stabilization of the gp120 V3 Loop through Hydrophobic Interactions Reduces the Immunodominant V3-Directed Non-Neutralizing Response to HIV-1 Envelope Trimers. J. Biol. Chem., 293(5):1688-1701, 2 Feb 2018. PubMed ID: 29222332.
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deTaeye2019
Steven W. de Taeye, Eden P. Go, Kwinten Sliepen, Alba Torrents de la Peña, Kimberly Badal, Max Medina-Ramírez, Wen-Hsin Lee, Heather Desaire, Ian A. Wilson, John P. Moore, Andrew B. Ward, and Rogier W. Sanders. Stabilization of the V2 Loop Improves the Presentation of V2 Loop-Associated Broadly Neutralizing Antibody Epitopes on HIV-1 Envelope Trimers. J. Biol. Chem., 294(14):5616-5631, 5 Apr 2019. PubMed ID: 30728245.
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DeVico2007
Anthony DeVico, Timothy Fouts, George K. Lewis, Robert C. Gallo, Karla Godfrey, Manhattan Charurat, Ilia Harris, Lindsey Galmin, and Ranajit Pal. Antibodies to CD4-Induced Sites in HIV gp120 Correlate with the Control of SHIV Challenge in Macaques Vaccinated with Subunit Immunogens. Proc. Natl. Acad. Sci. U.S.A., 104(44):17477-17482, 30 Oct 2007. PubMed ID: 17956985.
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Dey2003
Barna Dey, Christie S. Del Castillo, and Edward A. Berger. Neutralization of Human Immunodeficiency Virus Type 1 by sCD4-17b, a Single-Chain Chimeric Protein, Based on Sequential Interaction of gp120 with CD4 and Coreceptor. J. Virol., 77(5):2859-2865, Mar 2003. PubMed ID: 12584309.
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Dey2007
Antu K. Dey, Kathryn B. David, Per J. Klasse, and John P. Moore. Specific Amino Acids in the N-Terminus of the gp41 Ectodomain Contribute to the Stabilization of a Soluble, Cleaved gp140 Envelope Glycoprotein from Human Immunodeficiency Virus Type 1. Virology, 360(1):199-208, 30 Mar 2007. PubMed ID: 17092531.
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Dey2007a
Barna Dey, Marie Pancera, Krisha Svehla, Yuuei Shu, Shi-Hua Xiang, Jeffrey Vainshtein, Yuxing Li, Joseph Sodroski, Peter D Kwong, John R Mascola, and Richard Wyatt. Characterization of Human Immunodeficiency Virus Type 1 Monomeric and Trimeric gp120 Glycoproteins Stabilized in the CD4-Bound State: Antigenicity, Biophysics, and Immunogenicity. J Virol, 81(11):5579-5593, Jun 2007. PubMed ID: 17360741.
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Dey2008
Antu K. Dey, Kathryn B. David, Neelanjana Ray, Thomas J. Ketas, Per J. Klasse, Robert W. Doms, and John P. Moore. N-Terminal Substitutions in HIV-1 gp41 Reduce the Expression of Non-Trimeric Envelope Glycoproteins on the Virus. Virology, 372(1):187-200, 1 Mar 2008. PubMed ID: 18031785.
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Dey2009
Barna Dey, Krisha Svehla, Ling Xu, Dianne Wycuff, Tongqing Zhou, Gerald Voss, Adhuna Phogat, Bimal K. Chakrabarti, Yuxing Li, George Shaw, Peter D. Kwong, Gary J. Nabel, John R. Mascola, and Richard T. Wyatt. Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site. PLoS Pathog, 5(5):e1000445, May 2009. PubMed ID: 19478876.
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Dhillon2007
Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160.
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Dieltjens2009
Tessa Dieltjens, Leo Heyndrickx, Betty Willems, Elin Gray, Lies Van Nieuwenhove, Katrijn Grupping, Guido Vanham, and Wouter Janssens. Evolution of Antibody Landscape and Viral Envelope Escape in an HIV-1 CRF02\_AG Infected Patient with 4E10-Like Antibodies. Retrovirology, 6:113, 2009. PubMed ID: 20003438.
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Ding2015
Shilei Ding, Maxime Veillette, Mathieu Coutu, Jérémie Prévost, Louise Scharf, Pamela J. Bjorkman, Guido Ferrari, James E. Robinson, Christina Stürzel, Beatrice H. Hahn, Daniel Sauter, Frank Kirchhoff, George K. Lewis, Marzena Pazgier, and Andrés Finzi. A Highly Conserved Residue of the HIV-1 gp120 Inner Domain Is Important for Antibody-Dependent Cellular Cytotoxicity Responses Mediated by Anti-cluster A Antibodies. J. Virol., 90(4):2127-2134, Feb 2016. PubMed ID: 26637462.
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Diomede2012
L. Diomede, S. Nyoka, C. Pastori, L. Scotti, A. Zambon, G. Sherman, C. M. Gray, M. Sarzotti-Kelsoe, and L. Lopalco. Passively Transmitted gp41 Antibodies in Babies Born from HIV-1 Subtype C-Seropositive Women: Correlation between Fine Specificity and Protection. J. Virol., 86(8):4129-4138, Apr 2012. PubMed ID: 22301151.
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Doores2010
Katie J. Doores and Dennis R. Burton. Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16. J. Virol., 84(20):10510-10521, Oct 2010. PubMed ID: 20686044.
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Doores2010a
Katie J. Doores, Zara Fulton, Michael Huber, Ian A. Wilson, and Dennis R. Burton. Antibody 2G12 Recognizes Di-Mannose Equivalently in Domain- and Nondomain-Exchanged Forms but Only Binds the HIV-1 Glycan Shield if Domain Exchanged. J. Virol., 84(20):10690-10699, Oct 2010. PubMed ID: 20702629.
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Doores2010b
Katie J. Doores, Camille Bonomelli, David J. Harvey, Snezana Vasiljevic, Raymond A. Dwek, Dennis R. Burton, Max Crispin, and Christopher N. Scanlan. Envelope Glycans of Immunodeficiency Virions Are Almost Entirely Oligomannose Antigens. Proc. Natl. Acad. Sci. U.S.A., 107(31):13800-13805, 3 Aug 2010. PubMed ID: 20643940.
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Doores2010c
Katie J Doores, Zara Fulton, Vu Hong, Mitul K. Patel, Christopher N. Scanlan, Mark R. Wormald, M. G. Finn, Dennis R. Burton, Ian A. Wilson, and Benjamin G. Davis. A Nonself Sugar Mimic of the HIV Glycan Shield Shows Enhanced Antigenicity. Proc. Natl. Acad. Sci. U.S.A., 107(40):17107-17112, 5 Oct 2010. PubMed ID: 20852065.
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Doores2013
Katie J. Doores, Michael Huber, Khoa M. Le, Sheng-Kai Wang, Colleen Doyle-Cooper, Anthony Cooper, Ralph Pantophlet, Chi-Huey Wong, David Nemazee, and Dennis R. Burton. 2G12-Expressing B Cell Lines May Aid in HIV Carbohydrate Vaccine Design Strategies. J. Virol., 87(4):2234-2241, Feb 2013. PubMed ID: 23221565.
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Doria-Rose2010
Nicole A. Doria-Rose, Rachel M. Klein, Marcus G. Daniels, Sijy O'Dell, Martha Nason, Alan Lapedes, Tanmoy Bhattacharya, Stephen A. Migueles, Richard T. Wyatt, Bette T. Korber, John R. Mascola, and Mark Connors. Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables. J. Virol., 84(3):1631-1636, Feb 2010. PubMed ID: 19923174.
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Drummer2013
Heidi E. Drummer, Melissa K. Hill, Anne L. Maerz, Stephanie Wood, Paul A. Ramsland, Johnson Mak, and Pantelis Poumbourios. Allosteric Modulation of the HIV-1 gp120-gp41 Association Site by Adjacent gp120 Variable Region 1 (V1) N-Glycans Linked to Neutralization Sensitivity. PLoS Pathog., 9(4):e1003218, 2013. PubMed ID: 23592978.
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DSouza1997
M. P. D'Souza, D. Livnat, J. A. Bradac, S. H. Bridges, the AIDS Clinical Trials Group Antibody Selection Working Group, and Collaborating Investigators. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. J. Infect. Dis., 175:1056-1062, 1997. Five laboratories evaluated neutralization of nine primary B clade isolates by a coded panel of seven human MAbs to HIV-1 subtype B envelope. IgG1b12, 2G12, 2F5 showed potent and broadly cross-reactive neutralizing ability; F105, 447/52-D, 729-D, 19b did not neutralize the primary isolates. PubMed ID: 9129066.
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Du2009
Sean X. Du, Rebecca J. Idiart, Ellaine B. Mariano, Helen Chen, Peifeng Jiang, Li Xu, Kristin M. Ostrow, Terri Wrin, Pham Phung, James M. Binley, Christos J. Petropoulos, John A. Ballantyne, and Robert G. Whalen. Effect of Trimerization Motifs on Quaternary Structure, Antigenicity, and Immunogenicity of a Noncleavable HIV-1 gp140 Envelope Glycoprotein. Virology, 395(1):33-44, 5 Dec 2009. PubMed ID: 19815247.
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Duenas-Decamp2010
Maria J. Duenas-Decamp and Paul R. Clapham. HIV-1 gp120 Determinants Proximal to the CD4 Binding Site Shift Protective Glycans That Are Targeted by Monoclonal Antibody 2G12. J. Virol., 84(18):9608-9612, Sep 2010. PubMed ID: 20610714.
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Dunfee2007
Rebecca L. Dunfee, Elaine R. Thomas, Jianbin Wang, Kevin Kunstman, Steven M. Wolinsky, and Dana Gabuzda. Loss of the N-Linked Glycosylation Site at Position 386 in the HIV Envelope V4 Region Enhances Macrophage Tropism and Is Associated with Dementia. Virology, 367(1):222-234, 10 Oct 2007. PubMed ID: 17599380.
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Dunlop2010
D. Cameron Dunlop, Camille Bonomelli, Fatma Mansab, Snezana Vasiljevic, Katie J. Doores, Mark R. Wormald, Angelina S. Palma, Ten Feizi, David J. Harvey, Raymond A. Dwek, Max Crispin, and Christopher N. Scanlan. Polysaccharide Mimicry of the Epitope of the Broadly Neutralizing Anti-HIV Antibody, 2G12, Induces Enhanced Antibody Responses to Self Oligomannose Glycans. Glycobiology, 20(7):812-823, Jul 2010. PubMed ID: 20181792.
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Edmonds2010
Tara G. Edmonds, Haitao Ding, Xing Yuan, Qing Wei, Kendra S. Smith, Joan A. Conway, Lindsay Wieczorek, Bruce Brown, Victoria Polonis, John T. West, David C. Montefiori, John C. Kappes, and Christina Ochsenbauer. Replication Competent Molecular Clones of HIV-1 Expressing Renilla Luciferase Facilitate the Analysis of Antibody Inhibition in PBMC. Virology, 408(1):1-13, 5 Dec 2010. PubMed ID: 20863545.
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EdwardsBH2002
Bradley H. Edwards, Anju Bansal, Steffanie Sabbaj, Janna Bakari, Mark J. Mulligan, and Paul A. Goepfert. Magnitude of Functional CD8+ T-Cell Responses to the Gag Protein of Human Immunodeficiency Virus Type 1 Correlates Inversely with Viral Load in Plasma. J. Virol., 76(5):2298-2305, Mar 2002. PubMed ID: 11836408.
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Enriquez-Navas2011
Pedro M. Enríquez-Navas, Marco Marradi, Daniel Padro, Jesús Angulo, and Soledad Penadés. A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands. Chemistry, 17(5):1547-1560, 1 Feb 2011. PubMed ID: 21268157.
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Euler2011
Zelda Euler, Evelien M. Bunnik, Judith A. Burger, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Activity of Broadly Neutralizing Antibodies, Including PG9, PG16, and VRC01, against Recently Transmitted Subtype B HIV-1 Variants from Early and Late in the Epidemic. J. Virol., 85(14):7236-7245, Jul 2011. PubMed ID: 21561918.
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Falkowska2012
Emilia Falkowska, Alejandra Ramos, Yu Feng, Tongqing Zhou, Stephanie Moquin, Laura M. Walker, Xueling Wu, Michael S. Seaman, Terri Wrin, Peter D. Kwong, Richard T. Wyatt, John R. Mascola, Pascal Poignard, and Dennis R. Burton. PGV04, an HIV-1 gp120 CD4 Binding Site Antibody, Is Broad and Potent in Neutralization but Does Not Induce Conformational Changes Characteristic of CD4. J. Virol., 86(8):4394-4403, Apr 2012. PubMed ID: 22345481.
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Feng2012
Yu Feng, Krisha McKee, Karen Tran, Sijy O'Dell, Stephen D. Schmidt, Adhuna Phogat, Mattias N. Forsell, Gunilla B. Karlsson Hedestam, John R. Mascola, and Richard T. Wyatt. Biochemically Defined HIV-1 Envelope Glycoprotein Variant Immunogens Display Differential Binding and Neutralizing Specificities to the CD4-Binding Site. J. Biol. Chem., 287(8):5673-5686, 17 Feb 2012. PubMed ID: 22167180.
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Fenyo2009
Eva Maria Fenyö, Alan Heath, Stefania Dispinseri, Harvey Holmes, Paolo Lusso, Susan Zolla-Pazner, Helen Donners, Leo Heyndrickx, Jose Alcami, Vera Bongertz, Christian Jassoy, Mauro Malnati, David Montefiori, Christiane Moog, Lynn Morris, Saladin Osmanov, Victoria Polonis, Quentin Sattentau, Hanneke Schuitemaker, Ruengpung Sutthent, Terri Wrin, and Gabriella Scarlatti. International Network for Comparison of HIV Neutralization Assays: The NeutNet Report. PLoS One, 4(2):e4505, 2009. PubMed ID: 19229336.
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Ferrantelli2002
Flavia Ferrantelli and Ruth M. Ruprecht. Neutralizing Antibodies Against HIV --- Back in the Major Leagues? Curr. Opin. Immunol., 14(4):495-502, Aug 2002. PubMed ID: 12088685.
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Ferrantelli2003
Flavia Ferrantelli, Regina Hofmann-Lehmann, Robert A. Rasmussen, Tao Wang, Weidong Xu, Pei-Lin Li, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Post-Exposure Prophylaxis with Human Monoclonal Antibodies Prevented SHIV89.6P Infection or Disease in Neonatal Macaques. AIDS, 17(3):301-309, 14 Feb 2003. PubMed ID: 12556683.
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Ferrantelli2004
Flavia Ferrantelli, Robert A. Rasmussen, Kathleen A. Buckley, Pei-Lin Li, Tao Wang, David C. Montefiori, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Complete Protection of Neonatal Rhesus Macaques against Oral Exposure to Pathogenic Simian-Human Immunodeficiency Virus by Human Anti-HIV Monoclonal Antibodies. J. Infect. Dis., 189(12):2167-2173, 15 Jun 2004. PubMed ID: 15181562.
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Ferrantelli2004a
Flavia Ferrantelli, Moiz Kitabwalla, Robert A. Rasmussen, Chuanhai Cao, Ting-Chao Chou, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Yun Bai, Joseph Cotropia, Kenneth E. Ugen, and Ruth M. Ruprecht. Potent Cross-Group Neutralization of Primary Human Immunodeficiency Virus Isolates with Monoclonal Antibodies--Implications for Acquired Immunodeficiency Syndrome Vaccine. J. Infect. Dis., 189(1):71-74, 1 Jan 2004. PubMed ID: 14702155.
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Ferrantelli2007
Flavia Ferrantelli, Kathleen A. Buckley, Robert A. Rasmussen, Alistair Chalmers, Tao Wang, Pei-Lin Li, Alison L. Williams, Regina Hofmann-Lehmann, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Time Dependence of Protective Post-Exposure Prophylaxis with Human Monoclonal Antibodies Against Pathogenic SHIV Challenge in Newborn Macaques. Virology, 358(1):69-78, 5 Feb 2007. PubMed ID: 16996554.
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Ferrari2011a
Guido Ferrari, Justin Pollara, Daniel Kozink, Tiara Harms, Mark Drinker, Stephanie Freel, M. Anthony Moody, S. Munir Alam, Georgia D. Tomaras, Christina Ochsenbauer, John C. Kappes, George M. Shaw, James A. Hoxie, James E. Robinson, and Barton F. Haynes. An HIV-1 gp120 Envelope Human Monoclonal Antibody That Recognizes a C1 Conformational Epitope Mediates Potent Antibody-Dependent Cellular Cytotoxicity (ADCC) Activity and Defines a Common ADCC Epitope in Human HIV-1 Serum. J. Virol., 85(14):7029-7036, Jul 2011. PubMed ID: 21543485.
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Floss2009
Doreen M. Floss, Markus Sack, Elsa Arcalis, Johannes Stadlmann, Heribert Quendler, Thomas Rademacher, Eva Stoger, Jürgen Scheller, Rainer Fischer, and Udo Conrad. Influence of Elastin-Like Peptide Fusions on the Quantity and Quality of a Tobacco-Derived Human Immunodeficiency Virus-Neutralizing Antibody. Plant Biotechnol. J., 7(9):899-913, Dec 2009. PubMed ID: 19843249.
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Forsell2005
Mattias N. E. Forsell, Yuxing Li, Maria Sundbäck, Krisha Svehla, Peter Liljeström, John R. Mascola, Richard Wyatt, and Gunilla B. Karlsson Hedestam. Biochemical and Immunogenic Characterization of Soluble Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers Expressed by Semliki Forest Virus. J Virol, 79(17):10902-10914, Sep 2005. PubMed ID: 16103142.
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Forsman2008
Anna Forsman, Els Beirnaert, Marlén M. I. Aasa-Chapman, Bart Hoorelbeke, Karolin Hijazi, Willie Koh, Vanessa Tack, Agnieszka Szynol, Charles Kelly, Áine McKnight, Theo Verrips, Hans de Haard, and Robin A Weiss. Llama Antibody Fragments with Cross-Subtype Human Immunodeficiency Virus Type 1 (HIV-1)-Neutralizing Properties and High Affinity for HIV-1 gp120. J. Virol., 82(24):12069-12081, Dec 2008. PubMed ID: 18842738.
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Forthal2009
Donald N. Forthal and Christiane Moog. Fc Receptor-Mediated Antiviral Antibodies. Curr. Opin. HIV AIDS, 4(5):388-393, Sep 2009. PubMed ID: 20048702.
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Forthal2010
Donald N. Forthal, Johannes S. Gach, Gary Landucci, Jakub Jez, Richard Strasser, Renate Kunert, and Herta Steinkellner. Fc-Glycosylation Influences Fc-gamma Receptor Binding and Cell-Mediated Anti-HIV Activity of Monoclonal Antibody 2G12. J Immunol, 185(11):6876-6882, 1 Dec 2010. PubMed ID: 21041724.
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Fouts1997
T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632.
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Fouts1998
T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713.
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Frankel1998
S. S. Frankel, R. M. Steinman, N. L. Michael, S. R. Kim, N. Bhardwaj, M. Pope, M. K. Louder, P. K. Ehrenberg, P. W. Parren, D. R. Burton, H. Katinger, T. C. VanCott, M. L. Robb, D. L. Birx, and J. R. Mascola. Neutralizing Monoclonal Antibodies Block Human Immunodeficiency Virus Type 1 Infection of Dendritic Cells and Transmission to T Cells. J. Virol., 72:9788-9794, 1998. Investigation of three human MAbs to elicit a neutralizing effect and block HIV-1 infection in human dendritic cells. Preincubation with NAbs IgG1b12 or a combination of 2F5/2G12 prevented infection of purified DC and transmission in DC/T-cell cultures. PubMed ID: 9811714.
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Frey2008
Gary Frey, Hanqin Peng, Sophia Rits-Volloch, Marco Morelli, Yifan Cheng, and Bing Chen. A Fusion-Intermediate State of HIV-1 gp41 Targeted by Broadly Neutralizing Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(10):3739-3744, 11 Mar 2008. PubMed ID: 18322015.
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Gach2010
Johannes S. Gach, Paul G. Furtmüller, Heribert Quendler, Paul Messner, Ralf Wagner, Hermann Katinger, and Renate Kunert. Proline Is Not Uniquely Capable of Providing the Pivot Point for Domain Swapping in 2G12, a Broadly Neutralizing Antibody against HIV-1. J. Biol. Chem., 285(2):1122-1127, 8 Jan 2010. PubMed ID: 19903812.
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Gach2013
Johannes S. Gach, Heribert Quendler, Tommy Tong, Kristin M. Narayan, Sean X. Du, Robert G. Whalen, James M. Binley, Donald N. Forthal, Pascal Poignard, and Michael B. Zwick. A Human Antibody to the CD4 Binding Site of gp120 Capable of Highly Potent but Sporadic Cross Clade Neutralization of Primary HIV-1. PLoS One, 8(8):e72054, 2013. PubMed ID: 23991039.
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Gach2014
Johannes S. Gach, Chad J. Achenbach, Veronika Chromikova, Baiba Berzins, Nina Lambert, Gary Landucci, Donald N. Forthal, Christine Katlama, Barbara H. Jung, and Robert L. Murphy. HIV-1 Specific Antibody Titers and Neutralization among Chronically Infected Patients on Long-Term Suppressive Antiretroviral Therapy (ART): A Cross-Sectional Study. PLoS One, 9(1):e85371, 2014. PubMed ID: 24454852.
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Gao2005a
Feng Gao, Eric A. Weaver, Zhongjing Lu, Yingying Li, Hua-Xin Liao, Benjiang Ma, S Munir Alam, Richard M. Scearce, Laura L. Sutherland, Jae-Sung Yu, Julie M. Decker, George M. Shaw, David C. Montefiori, Bette T. Korber, Beatrice H. Hahn, and Barton F. Haynes. Antigenicity and Immunogenicity of a Synthetic Human Immunodeficiency Virus Type 1 Group M Consensus Envelope Glycoprotein. J. Virol., 79(2):1154-1163, Jan 2005. PubMed ID: 15613343.
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Gao2007
Feng Gao, Hua-Xin Liao, Beatrice H. Hahn, Norman L. Letvin, Bette T. Korber, and Barton F. Haynes. Centralized HIV-1 Envelope Immunogens and Neutralizing Antibodies. Curr. HIV Res., 5(6):572-577, Nov 2007. PubMed ID: 18045113.
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Gao2009
Feng Gao, Richard M. Scearce, S. Munir Alam, Bhavna Hora, Shimao Xia, Julie E. Hohm, Robert J. Parks, Damon F. Ogburn, Georgia D. Tomaras, Emily Park, Woodrow E. Lomas, Vernon C. Maino, Susan A. Fiscus, Myron S. Cohen, M. Anthony Moody, Beatrice H. Hahn, Bette T. Korber, Hua-Xin Liao, and Barton F. Haynes. Cross-reactive Monoclonal Antibodies to Multiple HIV-1 Subtype and SIVcpz Envelope Glycoproteins. Virology, 394(1):91-98, 10 Nov 2009. PubMed ID: 19744690.
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Gavrilyuk2013
Julia Gavrilyuk, Hitoshi Ban, Hisatoshi Uehara, Shannon J. Sirk, Karen Saye-Francisco, Angelica Cuevas, Elise Zablowsky, Avinash Oza, Michael S. Seaman, Dennis R. Burton, and Carlos F. Barbas, 3rd. Antibody Conjugation Approach Enhances Breadth and Potency of Neutralization of Anti-HIV-1 Antibodies and CD4-IgG. J. Virol., 87(9):4985-4993, May 2013. PubMed ID: 23427154.
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Geonnotti2010
Anthony R. Geonnotti, Miroslawa Bilska, Xing Yuan, Christina Ochsenbauer, Tara G. Edmonds, John C. Kappes, Hua-Xin Liao, Barton F. Haynes, and David C. Montefiori. Differential Inhibition of Human Immunodeficiency Virus Type 1 in Peripheral Blood Mononuclear Cells and TZM-bl Cells by Endotoxin-Mediated Chemokine and Gamma Interferon Production. AIDS Res. Hum. Retroviruses, 26(3):279-291, Mar 2010. PubMed ID: 20218881.
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Georgiev2013
Ivelin S. Georgiev, Nicole A. Doria-Rose, Tongqing Zhou, Young Do Kwon, Ryan P. Staupe, Stephanie Moquin, Gwo-Yu Chuang, Mark K. Louder, Stephen D. Schmidt, Han R. Altae-Tran, Robert T. Bailer, Krisha McKee, Martha Nason, Sijy O'Dell, Gilad Ofek, Marie Pancera, Sanjay Srivatsan, Lawrence Shapiro, Mark Connors, Stephen A. Migueles, Lynn Morris, Yoshiaki Nishimura, Malcolm A. Martin, John R. Mascola, and Peter D. Kwong. Delineating Antibody Recognition in Polyclonal Sera from Patterns of HIV-1 Isolate Neutralization. Science, 340(6133):751-756, 10 May 2013. PubMed ID: 23661761.
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GoldingH2002
Hana Golding, Marina Zaitseva, Eve de Rosny, Lisa R. King, Jody Manischewitz, Igor Sidorov, Miroslaw K. Gorny, Susan Zolla-Pazner, Dimiter S. Dimitrov, and Carol D. Weiss. Dissection of Human Immunodeficiency Virus Type 1 Entry with Neutralizing Antibodies to gp41 Fusion Intermediates. J. Virol., 76(13):6780-6790, Jul 2002. PubMed ID: 12050391.
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Gonzalez2010
Nuria Gonzalez, Amparo Alvarez, and Jose Alcami. Broadly Neutralizing Antibodies and their Significance for HIV-1 Vaccines. Curr. HIV Res., 8(8):602-612, Dec 2010. PubMed ID: 21054253.
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Gopi2008
Hosahudya Gopi, M. Umashankara, Vanessa Pirrone, Judith LaLonde, Navid Madani, Ferit Tuzer, Sabine Baxter, Isaac Zentner, Simon Cocklin, Navneet Jawanda, Shendra R. Miller, Arne Schön, Jeffrey C. Klein, Ernesto Freire, Fred C. Krebs, Amos B. Smith, Joseph Sodroski, and Irwin Chaiken. Structural Determinants for Affinity Enhancement of a Dual Antagonist Peptide Entry Inhibitor of Human Immunodeficiency Virus Type-1. J. Med. Chem., 51(9):2638-2647, 8 May 2008. PubMed ID: 18402432.
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Gorny2003
Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162.
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Gorny2005
Miroslaw K. Gorny, Leonidas Stamatatos, Barbara Volsky, Kathy Revesz, Constance Williams, Xiao-Hong Wang, Sandra Cohen, Robert Staudinger, and Susan Zolla-Pazner. Identification of a New Quaternary Neutralizing Epitope on Human Immunodeficiency Virus Type 1 Virus Particles. J. Virol., 79(8):5232-5237, Apr 2005. PubMed ID: 15795308.
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Gorry2002
Paul R. Gorry, Joann Taylor, Geoffrey H. Holm, Andrew Mehle, Tom Morgan, Mark Cayabyab, Michael Farzan, Hui Wang, Jeanne E. Bell, Kevin Kunstman, John P. Moore, Steven M. Wolinsky, and Dana Gabuzda. Increased CCR5 Affinity and Reduced CCR5/CD4 Dependence of a Neurovirulent Primary Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 76(12):6277-6292, Jun 2002. PubMed ID: 12021361.
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Gray2006
Elin Solomonovna Gray, Tammy Meyers, Glenda Gray, David Charles Montefiori, and Lynn Morris. Insensitivity of Paediatric HIV-1 Subtype C Viruses to Broadly Neutralising Monoclonal Antibodies Raised against Subtype B. PLoS Med., 3(7):e255, Jul 2006. PubMed ID: 16834457.
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Gray2007a
Elin S. Gray, Penny L. Moore, Ralph A. Pantophlet, and Lynn Morris. N-Linked Glycan Modifications in gp120 of Human Immunodeficiency Virus Type 1 Subtype C Render Partial Sensitivity to 2G12 Antibody Neutralization. J. Virol., 81(19):10769-10776, Oct 2007. PubMed ID: 17634239.
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Grovit-Ferbas2000
K. Grovit-Ferbas, J. F. Hsu, J. Ferbas, V. Gudeman, and I. S. Chen. Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1. J. Virol., 74(13):5802-9, Jul 2000. URL: http://jvi.asm.org/cgi/content/full/74/13/5802. PubMed ID: 10846059.
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Grundner2002
Christoph Grundner, Tajib Mirzabekov, Joseph Sodroski, and Richard Wyatt. Solid-Phase Proteoliposomes Containing Human Immunodeficiency Virus Envelope Glycoproteins. J. Virol., 76(7):3511-3521, Apr 2002. PubMed ID: 11884575.
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Grundner2005
Christoph Grundner, Yuxing Li, Mark Louder, John Mascola, Xinzhen Yang, Joseph Sodroski, and Richard Wyatt. Analysis of the Neutralizing Antibody Response Elicited in Rabbits by Repeated Inoculation with Trimeric HIV-1 Envelope Glycoproteins. Virology, 331(1):33-46, 5 Jan 2005. PubMed ID: 15582651.
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Guenaga2015
Javier Guenaga, Natalia de Val, Karen Tran, Yu Feng, Karen Satchwell, Andrew B. Ward, and Richard T. Wyatt. Well-Ordered Trimeric HIV-1 Subtype B and C Soluble Spike Mimetics Generated by Negative Selection Display Native-Like Properties. PLoS Pathog., 11(1):e1004570, Jan 2015. PubMed ID: 25569572.
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Gunn2016
B. M. Gunn, J. R. Schneider, M. Shansab, A. R. Bastian, K. M. Fahrbach, A. D. Smith, A. E. Mahan, M. M. Karim, A. F. Licht, I. Zvonar, J. Tedesco, M. R. Anderson, A. Chapel, T. J. Suscovich, D. C. Malaspina, H. Streeck, B. D. Walker, A. Kim, G. Lauer, M. Altfeld, S. Pillai, I. Szleifer, N. L. Kelleher, P. F. Kiser, T. J. Hope, and G. Alter. Enhanced Binding of Antibodies Generated During Chronic HIV Infection to Mucus Component MUC16. Mucosal. Immunol., 9(6):1549-1558, Nov 2016. PubMed ID: 26960182.
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Gupta2013
Sandeep Gupta, Johannes S. Gach, Juan C. Becerra, Tran B. Phan, Jeffrey Pudney, Zina Moldoveanu, Sarah B. Joseph, Gary Landucci, Medalyn Jude Supnet, Li-Hua Ping, Davide Corti, Brian Moldt, Zdenek Hel, Antonio Lanzavecchia, Ruth M. Ruprecht, Dennis R. Burton, Jiri Mestecky, Deborah J. Anderson, and Donald N. Forthal. The Neonatal Fc Receptor (FcRn) Enhances Human Immunodeficiency Virus Type 1 (HIV-1) Transcytosis across Epithelial Cells. PLoS Pathog., 9(11):e1003776, Nov 2013. PubMed ID: 24278022.
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Gustchina2008
Elena Gustchina, Carole A. Bewley, and G. Marius Clore. Sequestering of the Prehairpin Intermediate of gp41 by Peptide N36Mut(e,g) Potentiates the Human Immunodeficiency Virus Type 1 Neutralizing Activity of Monoclonal Antibodies Directed against the N-Terminal Helical Repeat of gp41. J. Virol., 82(20):10032-10041, Oct 2008. PubMed ID: 18667502.
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Guzzo2018
Christina Guzzo, Peng Zhang, Qingbo Liu, Alice L. Kwon, Ferzan Uddin, Alexandra I. Wells, Hana Schmeisser, Raffaello Cimbro, Jinghe Huang, Nicole Doria-Rose, Stephen D. Schmidt, Michael A. Dolan, Mark Connors, John R. Mascola, and Paolo Lusso. Structural Constraints at the Trimer Apex Stabilize the HIV-1 Envelope in a Closed, Antibody-Protected Conformation. mBio, 9(6), 11 Dec 2018. PubMed ID: 30538178.
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Haigwood2009
Nancy L. Haigwood and Vanessa M. Hirsch. Blocking and Tackling HIV. Nat. Med., 15(8):841-842, Aug 2009. PubMed ID: 19661984.
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Haim2007
Hillel Haim, Israel Steiner, and Amos Panet. Time Frames for Neutralization during the Human Immunodeficiency Virus Type 1 Entry Phase, as Monitored in Synchronously Infected Cell Cultures. J. Virol., 81(7):3525-3534, Apr 2007. PubMed ID: 17251303.
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Haim2011
Hillel Haim, Bettina Strack, Aemro Kassa, Navid Madani, Liping Wang, Joel R. Courter, Amy Princiotto, Kathleen McGee, Beatriz Pacheco, Michael S. Seaman, Amos B. Smith, 3rd., and Joseph Sodroski. Contribution of Intrinsic Reactivity of the HIV-1 Envelope Glycoproteins to CD4-Independent Infection and Global Inhibitor Sensitivity. PLoS Pathog., 7(6):e1002101, Jun 2011. PubMed ID: 21731494.
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Haldar2011
Bijayesh Haldar, Sherri Burda, Constance Williams, Leo Heyndrickx, Guido Vanham, Miroslaw K. Gorny, and Phillipe Nyambi. Longitudinal Study of Primary HIV-1 Isolates in Drug-Naïve Individuals Reveals the Emergence of Variants Sensitive to Anti-HIV-1 Monoclonal Antibodies. PLoS One, 6(2):e17253, 2011. PubMed ID: 21383841.
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Hart2003
Melanie L. Hart, Mohammed Saifuddin, and Gregory T. Spear. Glycosylation Inhibitors and Neuraminidase Enhance Human Immunodeficiency Virus Type 1 Binding and Neutralization by Mannose-Binding Lectin. J. Gen. Virol., 84(Pt 2):353-360, Feb 2003. PubMed ID: 12560567.
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Haynes2005
Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590.
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Haynes2005a
Barton F. Haynes, M. Anthony Moody, Laurent Verkoczy, Garnett Kelsoe, and S. Munir Alam. Antibody Polyspecificity and Neutralization of HIV-1: A Hypothesis. Hum. Antibodies, 14(3-4):59-67, 2005. PubMed ID: 16720975.
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Haynes2006a
Barton F. Haynes and David C. Montefiori. Aiming to Induce Broadly Reactive Neutralizing Antibody Responses with HIV-1 Vaccine Candidates. Expert Rev. Vaccines, 5(4):579-595, Aug 2006. PubMed ID: 16989638.
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Haynes2008
Barton F. Haynes and Robin J. Shattock. Critical Issues in Mucosal Immunity for HIV-1 Vaccine Development. J. Allergy Clin. Immunol., 122(1):3-9, Jul 2008. PubMed ID: 18468671.
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Haynes2012
Barton F. Haynes, Garnett Kelsoe, Stephen C. Harrison, and Thomas B. Kepler. B-Cell-Lineage Immunogen Design in Vaccine Development with HIV-1 as a Case Study. Nat. Biotechnol., 30(5):423-433, May 2012. PubMed ID: 22565972.
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He2018
Linling He, Sonu Kumar, Joel D. Allen, Deli Huang, Xiaohe Lin, Colin J. Mann, Karen L. Saye-Francisco, Jeffrey Copps, Anita Sarkar, Gabrielle S. Blizard, Gabriel Ozorowski, Devin Sok, Max Crispin, Andrew B. Ward, David Nemazee, Dennis R. Burton, Ian A. Wilson, and Jiang Zhu. HIV-1 Vaccine Design through Minimizing Envelope Metastability. Sci. Adv., 4(11):eaau6769, Nov 2018. PubMed ID: 30474059.
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Henderson2019
Rory Henderson, Brian E. Watts, Hieu N. Ergin, Kara Anasti, Robert Parks, Shi-Mao Xia, Ashley Trama, Hua-Xin Liao, Kevin O. Saunders, Mattia Bonsignori, Kevin Wiehe, Barton F. Haynes, and S. Munir Alam. Selection of Immunoglobulin Elbow Region Mutations Impacts Interdomain Conformational Flexibility in HIV-1 Broadly Neutralizing Antibodies. Nat. Commun., 10(1):654, 8 Feb 2019. PubMed ID: 30737386.
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Herrera2003
Carolina Herrera, Catherine Spenlehauer, Michael S. Fung, Dennis R. Burton, Simon Beddows, and John P. Moore. Nonneutralizing Antibodies to the CD4-Binding Site on the gp120 Subunit of Human Immunodeficiency Virus Type 1 Do Not Interfere with the Activity of a Neutralizing Antibody against the Same Site. J. Virol., 77(2):1084-1091, Jan 2003. PubMed ID: 12502824.
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Herrera2005
Carolina Herrera, Per Johan Klasse, Elizabeth Michael, Shivani Kake, Kelly Barnes, Christopher W. Kibler, Lila. Campbell-Gardener, Zhihai Si, Joseph Sodroski, John P. Moore, and Simon Beddows. The Impact of Envelope Glycoprotein Cleavage on the Antigenicity, Infectivity, and Neutralization Sensitivity of Env-Pseudotyped Human Immunodeficiency Virus Type 1 Particles. Virology, 338(1):154-172, 20 Jul 2005. PubMed ID: 15932765.
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Herrera2006
Carolina Herrera, Per Johan Klasse, Christopher W. Kibler, Elizabeth Michael, John P. Moore, and Simon Beddows. Dominant-Negative Effect of Hetero-Oligomerization on the Function of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex. Virology, 351(1):121-132, 20 Jul 2006. PubMed ID: 16616288.
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Hessell2009
Ann J. Hessell, Eva G. Rakasz, Pascal Poignard, Lars Hangartner, Gary Landucci, Donald N. Forthal, Wayne C. Koff, David I. Watkins, and Dennis R. Burton. Broadly Neutralizing Human Anti-HIV Antibody 2G12 Is Effective in Protection against Mucosal SHIV Challenge Even at Low Serum Neutralizing Titers. PLoS Pathog., 5(5):e1000433, May 2009. PubMed ID: 19436712.
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Hildgartner2009
Alexander Hildgartner, Doris Wilflingseder, Christoph Gassner, Manfred P. Dierich, Heribert Stoiber, and Zoltán Bánki. Induction of Complement-Mediated Lysis of HIV-1 by a Combination of HIV-Specific and HLA Allotype-Specific Antibodies. Immunol. Lett., 126(1-2):85-90, 22 Sep 2009. PubMed ID: 19698750.
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Hoffenberg2013
Simon Hoffenberg, Rebecca Powell, Alexei Carpov, Denise Wagner, Aaron Wilson, Sergei Kosakovsky Pond, Ross Lindsay, Heather Arendt, Joanne DeStefano, Sanjay Phogat, Pascal Poignard, Steven P. Fling, Melissa Simek, Celia LaBranche, David Montefiori, Terri Wrin, Pham Phung, Dennis Burton, Wayne Koff, C. Richter King, Christopher L. Parks, and Michael J. Caulfield. Identification of an HIV-1 Clade A Envelope That Exhibits Broad Antigenicity and Neutralization Sensitivity and Elicits Antibodies Targeting Three Distinct Epitopes. J. Virol., 87(10):5372-5383, May 2013. PubMed ID: 23468492.
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HofmannLehmann2001
R. Hofmann-Lehmann, J. Vlasak, R. A. Rasmussen, B. A. Smith, T. W. Baba, V. Liska, F. Ferrantelli, D. C. Montefiori, H. M. McClure, D. C. Anderson, B. J. Bernacky, T. A. Rizvi, R. Schmidt, L. R. Hill, M. E. Keeling, H. Katinger, G. Stiegler, L. A. Cavacini, M. R. Posner, T. C. Chou, J. Andersen, and R. M. Ruprecht. Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge. J. Virol., 75(16):7470--80, Aug 2001. URL: http://jvi.asm.org/cgi/content/full/75/16/7470. PubMed ID: 11462019.
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Hogan2018
Michael J. Hogan, Angela Conde-Motter, Andrea P. O. Jordan, Lifei Yang, Brad Cleveland, Wenjin Guo, Josephine Romano, Houping Ni, Norbert Pardi, Celia C. LaBranche, David C. Montefiori, Shiu-Lok Hu, James A. Hoxie, and Drew Weissman. Increased Surface Expression of HIV-1 Envelope Is Associated with Improved Antibody Response in Vaccinia Prime/Protein Boost Immunization. Virology, 514:106-117, 15 Jan 2018. PubMed ID: 29175625.
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Holl2006
Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957.
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Holl2006a
Vincent Holl, Maryse Peressin, Sylvie Schmidt, Thomas Decoville, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Efficient Inhibition of HIV-1 Replication in Human Immature Monocyte-Derived Dendritic Cells by Purified Anti-HIV-1 IgG without Induction of Maturation. Blood, 107(11):4466-4474, 1 Jun 2006. PubMed ID: 16469871.
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Hong2007
Patrick W.-P. Hong, Sandra Nguyen, Sophia Young, Stephen V. Su, and Benhur Lee. Identification of the Optimal DC-SIGN Binding Site on Human Immunodeficiency Virus Type 1 gp120. J. Virol., 81(15):8325-8336, Aug 2007. PubMed ID: 17522223.
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Honnen2007
W. J. Honnen, C. Krachmarov, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and A. Pinter. Type-Specific Epitopes Targeted by Monoclonal Antibodies with Exceptionally Potent Neutralizing Activities for Selected Strains of Human Immunodeficiency Virus Type 1 Map to a Common Region of the V2 Domain of gp120 and Differ Only at Single Positions from the Clade B Consensus Sequence. J. Virol., 81(3):1424-1432, Feb 2007. PubMed ID: 17121806.
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Hoxie2010
James A. Hoxie. Toward an Antibody-Based HIV-1 Vaccine. Annu. Rev. Med., 61:135-52, 2010. PubMed ID: 19824826.
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Hraber2014
Peter Hraber, Michael S. Seaman, Robert T. Bailer, John R. Mascola, David C. Montefiori, and Bette T. Korber. Prevalence of Broadly Neutralizing Antibody Responses during Chronic HIV-1 Infection. AIDS, 28(2):163-169, 14 Jan 2014. PubMed ID: 24361678.
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Hrin2008
Renee Hrin, Donna L. Montgomery, Fubao Wang, Jon H. Condra, Zhiqiang An, William R. Strohl, Elisabetta Bianchi, Antonello Pessi, Joseph G. Joyce, and Ying-Jie Wang. Short Communication: In Vitro Synergy between Peptides or Neutralizing Antibodies Targeting the N- and C-Terminal Heptad Repeats of HIV Type 1 gp41. AIDS Res. Hum. Retroviruses, 24(12):1537-1544, Dec 2008. PubMed ID: 19102685.
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Hu2007
Qinxue Hu, Naheed Mahmood, and Robin J. Shattock. High-Mannose-Specific Deglycosylation of HIV-1 gp120 Induced by Resistance to Cyanovirin-N and the Impact on Antibody Neutralization. Virology, 368(1):145-154, 10 Nov 2007. PubMed ID: 17658575.
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Hu2017
Xintao Hu, Yuanyuan Hu, Chunhong Zhao, Hongmei Gao, Kelli M. Greene, Li Ren, Liying Ma, Yuhua Ruan, Marcella Sarzotti-Kelsoe, David C. Montefiori, Kunxue Hong, and Yiming Shao. Profiling the Neutralizing Antibody Response in Chronically HIV-1 CRF07\_BC-Infected Intravenous Drug Users Naive to Antiretroviral Therapy. Sci. Rep., 7:46308, 7 Apr 2017. PubMed ID: 28387330.
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Hu2021
Yuanyuan Hu, Sen Zou, Zheng Wang, Ying Liu, Li Ren, Yanling Hao, Shasha Sun, Xintao Hu, Yuhua Ruan, Liying Ma, Yiming Shao, and Kunxue Hong. Virus Evolution and Neutralization Sensitivity in an HIV-1 Subtype B' Infected Plasma Donor with Broadly Neutralizing Activity. Vaccines (Basel), 9(4), 25 Mar 2021. PubMed ID: 33805985.
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Huang2007
Li Huang, Weihong Lai, Phong Ho, and Chin Ho Chen. Induction of a Nonproductive Conformational Change in gp120 by a Small Molecule HIV Type 1 Entry Inhibitor. AIDS Res. Hum. Retroviruses, 23(1):28-32, Jan 2007. PubMed ID: 17263629.
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Huang2010
Kuan-Hsiang G. Huang, David Bonsall, Aris Katzourakis, Emma C. Thomson, Sarah J. Fidler, Janice Main, David Muir, Jonathan N. Weber, Alexander J. Frater, Rodney E. Phillips, Oliver G. Pybus, Philip J. R. Goulder, Myra O. McClure, Graham S. Cooke, and Paul Klenerman. B-Cell Depletion Reveals a Role for Antibodies in the Control of Chronic HIV-1 Infection. Nat. Commun., 1:102, 2010. PubMed ID: 20981030.
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Huang2012
Xin Huang, Wei Jin, Kai Hu, Sukun Luo, Tao Du, George E. Griffin, Robin J. Shattock, and Qinxue Hu. Highly Conserved HIV-1 gp120 Glycans Proximal to CD4-Binding Region Affect Viral Infectivity and Neutralizing Antibody Induction. Virology, 423(1):97-106, 5 Feb 2012. PubMed ID: 22192629.
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Huang2017a
Xun Huang, Qianqian Zhu, Xiaoxing Huang, Lifei Yang, Yufeng Song, Ping Zhu, and Paul Zhou. In Vivo Electroporation in DNA-VLP Prime-Boost Preferentially Enhances HIV-1 Envelope-Specific IgG2a, Neutralizing Antibody and CD8 T Cell Responses. Vaccine, 35(16):2042-2051, 11 Apr 2017. PubMed ID: 28318765.
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Huber2007
M. Huber and A. Trkola. Humoral Immunity to HIV-1: Neutralization and Beyond. J. Intern. Med., 262(1):5-25, Jul 2007. PubMed ID: 17598812.
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Huber2010
Michael Huber, Khoa M. Le, Katie J. Doores, Zara Fulton, Robyn L. Stanfield, Ian A. Wilson, and Dennis R. Burton. Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain Exchange. J. Virol., 84(20):10700-10707, Oct 2010. PubMed ID: 20702640.
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Huskens2007
Dana Huskens, Kristel Van Laethem, Kurt Vermeire, Jan Balzarini, and Dominique Schols. Resistance of HIV-1 to the Broadly HIV-1-Neutralizing, Anti-Carbohydrate Antibody 2G12. Virology, 360(2):294-304, 10 Apr 2007. PubMed ID: 17123566.
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Jeffs2004
S. A. Jeffs, S. Goriup, B. Kebble, D. Crane, B. Bolgiano, Q. Sattentau, S. Jones, and H. Holmes. Expression and Characterisation of Recombinant Oligomeric Envelope Glycoproteins Derived from Primary Isolates of HIV-1. Vaccine, 22(8):1032-1046, 25 Feb 2004. PubMed ID: 15161081.
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Jenabian2010
Mohammad-Ali Jenabian, Héla Saïdi, Charlotte Charpentier, Hicham Bouhlal, Dominique Schols, Jan Balzarini, Thomas W. Bell, Guido Vanham, and Laurent Bélec. Differential Activity of Candidate Microbicides against Early Steps of HIV-1 Infection upon Complement Virus Opsonization. AIDS Res. Ther., 7:16, 2010. PubMed ID: 20546571.
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Johnson2017
Jacklyn Johnson, Yinjie Zhai, Hamid Salimi, Nicole Espy, Noah Eichelberger, Orlando DeLeon, Yunxia O'Malley, Joel Courter, Amos B. Smith, III, Navid Madani, Joseph Sodroski, and Hillel Haim. Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States. J. Virol., 91(15), 1 Aug 2017. PubMed ID: 28490588.
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Joos2006
Beda Joos, Alexandra Trkola, Herbert Kuster, Leonardo Aceto, Marek Fischer, Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Hermann Katinger, and Huldrych F. Günthard. Long-Term Multiple-Dose Pharmacokinetics of Human Monoclonal Antibodies (MAbs) against Human Immunodeficiency Virus Type 1 Envelope gp120 (MAb 2G12) and gp41 (MAbs 4E10 and 2F5). Antimicrob. Agents Chemother., 50(5):1773-1779, May 2006. PubMed ID: 16641449.
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Joseph2010
Aviva Joseph, Jian Hua Zheng, Ken Chen, Monica Dutta, Cindy Chen, Gabriela Stiegler, Renate Kunert, Antonia Follenzi, and Harris Goldstein. Inhibition of In Vivo HIV Infection in Humanized Mice by Gene Therapy of Human Hematopoietic Stem Cells with a Lentiviral Vector Encoding a Broadly Neutralizing Anti-HIV Antibody. J. Virol., 84(13):6645-6653, Jul 2010. PubMed ID: 20410262.
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Joubert2010
Marisa K. Joubert, Nichole Kinsley, Alexio Capovilla, B. Trevor Sewell, Mohamed A. Jaffer, and Makobetsa Khati. A Modeled Structure of an Aptamer-gp120 Complex Provides Insight into the Mechanism of HIV-1 Neutralization. Biochemistry, 49(28):5880-5890, 20 Jul 2010. PubMed ID: 20527993.
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Joyce2008
Joseph G. Joyce, Isaac J. Krauss, Hong C. Song, David W. Opalka, Karen M. Grimm, Deborah D. Nahas, Mark T. Esser, Renee Hrin, Meizhen Feng, Vadim Y. Dudkin, Michael Chastain, John W. Shiver, and Samuel J. Danishefsky. An Oligosaccharide-Based HIV-1 2G12 Mimotope Vaccine Induces Carbohydrate-Specific Antibodies That Fail To Neutralize HIV-1 Virions. Proc. Natl. Acad. Sci. U.S.A., 105(41):15684-15689, 14 Oct 2008. PubMed ID: 18838688.
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Joyner2011
Amanda S. Joyner, Jordan R. Willis, James E.. Crowe, Jr., and Christopher Aiken. Maturation-Induced Cloaking of Neutralization Epitopes on HIV-1 Particles. PLoS Pathog., 7(9):e1002234, Sep 2011. PubMed ID: 21931551.
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Julg2005
B. Jülg and F. D. Goebel. What's New in HIV/AIDS? Neutralizing HIV Antibodies: Do They Really Protect? Infection, 33(5-6):405-407, Oct 2005. PubMed ID: 16258878.
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Julien2015
Jean-Philippe Julien, Jeong Hyun Lee, Gabriel Ozorowski, Yuanzi Hua, Alba Torrents de la Peña, Steven W. de Taeye, Travis Nieusma, Albert Cupo, Anila Yasmeen, Michael Golabek, Pavel Pugach, P. J. Klasse, John P. Moore, Rogier W. Sanders, Andrew B. Ward, and Ian A. Wilson. Design and Structure of Two HIV-1 Clade C SOSIP.664 Trimers That Increase the Arsenal of Native-Like Env Immunogens. Proc. Natl. Acad. Sci. U.S.A., 112(38):11947-11952, 22 Sep 2015. PubMed ID: 26372963.
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Kabanova2010
Anna Kabanova, Roberto Adamo, Daniela Proietti, Francesco Berti, Marta Tontini, Rino Rappuoli, and Paolo Costantino. Preparation, Characterization and Immunogenicity of HIV-1 Related High-Mannose Oligosaccharides-CRM197 Glycoconjugates. Glycoconj. J., 27(5):501-513, Jul 2010. PubMed ID: 20524062.
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Kalia2005
Vandana Kalia, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41. J. Virol., 79(4):2097-2107, Feb 2005. PubMed ID: 15681412.
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Kang2005
Sang-Moo Kang, Fu Shi Quan, Chunzi Huang, Lizheng Guo, Ling Ye, Chinglai Yang, and Richard W. Compans. Modified HIV Envelope Proteins with Enhanced Binding to Neutralizing Monoclonal Antibodies. Virology, 331(1):20-32, 5 Jan 2005. PubMed ID: 15582650.
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Kang2009
Yun Kenneth Kang, Sofija Andjelic, James M. Binley, Emma T. Crooks, Michael Franti, Sai Prasad N. Iyer, Gerald P. Donovan, Antu K. Dey, Ping Zhu, Kenneth H. Roux, Robert J. Durso, Thomas F. Parsons, Paul J. Maddon, John P. Moore, and William C. Olson. Structural and Immunogenicity Studies of a Cleaved, Stabilized Envelope Trimer Derived from Subtype A HIV-1. Vaccine, 27(37):5120-5132, 13 Aug 2009. PubMed ID: 19567243.
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Karpenko2012
Larisa I. Karpenko, Nadezhda S. Scherbakova, Anton N. Chikaev, Olga Yu. Tumanova, Leonid R. Lebedev, Lyudmila A. Shalamova, Olga G. Pyankova, Alexander B. Ryzhikov, and Alexander A. Ilyichev. Polyepitope Protein Incorporated the HIV-1 Mimotope Recognized by Monoclonal Antibody 2G12. Mol. Immunol., 50(4):193-199, Apr 2012. PubMed ID: 22341130.
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Keele2008
Brandon F. Keele, Elena E. Giorgi, Jesus F. Salazar-Gonzalez, Julie M. Decker, Kimmy T. Pham, Maria G. Salazar, Chuanxi Sun, Truman Grayson, Shuyi Wang, Hui Li, Xiping Wei, Chunlai Jiang, Jennifer L. Kirchherr, Feng Gao, Jeffery A. Anderson, Li-Hua Ping, Ronald Swanstrom, Georgia D. Tomaras, William A. Blattner, Paul A. Goepfert, J. Michael Kilby, Michael S. Saag, Eric L. Delwart, Michael P. Busch, Myron S. Cohen, David C. Montefiori, Barton F. Haynes, Brian Gaschen, Gayathri S. Athreya, Ha Y. Lee, Natasha Wood, Cathal Seoighe, Alan S. Perelson, Tanmoy Bhattacharya, Bette T. Korber, Beatrice H. Hahn, and George M. Shaw. Identification and Characterization of Transmitted and Early Founder Virus Envelopes in Primary HIV-1 Infection. Proc. Natl. Acad. Sci. U.S.A., 105(21):7552-7557, 27 May 2008. PubMed ID: 18490657.
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Kirchherr2007
Jennifer L. Kirchherr, Xiaozhi Lu, Webster Kasongo, Victor Chalwe, Lawrence Mwananyanda, Rosemary M. Musonda, Shi-Mao Xia, Richard M. Scearce, Hua-Xin Liao, David C. Montefiori, Barton F. Haynes, and Feng Gao. High Throughput Functional Analysis of HIV-1 env Genes Without Cloning. J. Virol. Methods, 143(1):104-111, Jul 2007. PubMed ID: 17416428.
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Kishko2011
Michael Kishko, Mohan Somasundaran, Frank Brewster, John L. Sullivan, Paul R. Clapham, and Katherine Luzuriaga. Genotypic and Functional Properties of Early Infant HIV-1 Envelopes. Retrovirology, 8:67, 2011. PubMed ID: 21843318.
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Kitabwalla2003
Moiz Kitabwalla, Flavia Ferrantelli, Tao Wang, Alistair Chalmers, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Ting-Chao Chou, and Ruth M. Ruprecht. Primary African HIV Clade A and D Isolates: Effective Cross-Clade Neutralization with a Quadruple Combination of Human Monoclonal Antibodies Raised against Clade B. AIDS Res. Hum. Retroviruses, 19(2):125-131, Feb 2003. PubMed ID: 12639248.
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Klein2010
Joshua S. Klein and Pamela J. Bjorkman. Few and Far Between: How HIV May Be Evading Antibody Avidity. PLoS Pathog., 6(5):e1000908, May 2010. PubMed ID: 20523901.
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Klein2010a
Joshua S. Klein, Alexandre Webster, Priyanthi N. P. Gnanapragasam, Rachel P. Galimidi, and Pamela J. Bjorkman. A Dimeric Form of the HIV-1 Antibody 2G12 Elicits Potent Antibody-Dependent Cellular Cytotoxicity. AIDS, 24(11):1633-1640, 17 Jul 2010. PubMed ID: 20597163.
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Klein2012
Florian Klein, Christian Gaebler, Hugo Mouquet, D. Noah Sather, Clara Lehmann, Johannes F. Scheid, Zane Kraft, Yan Liu, John Pietzsch, Arlene Hurley, Pascal Poignard, Ten Feizi, Lynn Morris, Bruce D. Walker, Gerd Fätkenheuer, Michael S. Seaman, Leonidas Stamatatos, and Michel C. Nussenzweig. Broad Neutralization by a Combination of Antibodies Recognizing the CD4 Binding Site and a New Conformational Epitope on the HIV-1 Envelope Protein. J. Exp. Med., 209(8):1469-1479, 30 Jul 2012. PubMed ID: 22826297.
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Klein2013
Florian Klein, Ron Diskin, Johannes F. Scheid, Christian Gaebler, Hugo Mouquet, Ivelin S. Georgiev, Marie Pancera, Tongqing Zhou, Reha-Baris Incesu, Brooks Zhongzheng Fu, Priyanthi N. P. Gnanapragasam, Thiago Y. Oliveira, Michael S. Seaman, Peter D. Kwong, Pamela J. Bjorkman, and Michel C. Nussenzweig. Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization. Cell, 153(1):126-138, 28 Mar 2013. PubMed ID: 23540694.
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Koh2010a
Willie W. L. Koh, Anna Forsman, Stéphane Hué, Gisela J. van der Velden, David L. Yirrell, Áine McKnight, Robin A. Weiss, and Marlén M. I. Aasa-Chapman. Novel Subtype C Human Immunodeficiency Virus Type 1 Envelopes Cloned Directly from Plasma: Coreceptor Usage and Neutralization Phenotypes. J. Gen. Virol., 91(9):2374-2380, Sep 2010. PubMed ID: 20484560.
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Kong2013
Leopold Kong, Jeong Hyun Lee, Katie J. Doores, Charles D. Murin, Jean-Philippe Julien, Ryan McBride, Yan Liu, Andre Marozsan, Albert Cupo, Per-Johan Klasse, Simon Hoffenberg, Michael Caulfield, C. Richter King, Yuanzi Hua, Khoa M. Le, Reza Khayat, Marc C. Deller, Thomas Clayton, Henry Tien, Ten Feizi, Rogier W. Sanders, James C. Paulson, John P. Moore, Robyn L. Stanfield, Dennis R. Burton, Andrew B. Ward, and Ian A. Wilson. Supersite of Immune Vulnerability on the Glycosylated Face of HIV-1 Envelope Glycoprotein gp120. Nat. Struct. Mol. Biol., 20(7):796-803, Jul 2013. PubMed ID: 23708606.
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Korber2009
Bette Korber and S. Gnanakaran. The Implications of Patterns in HIV Diversity for Neutralizing Antibody Induction and Susceptibility. Curr. Opin. HIV AIDS, 4(5):408-417, Sep 2009. PubMed ID: 20048705.
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Kothe2007
Denise L. Kothe, Julie M Decker, Yingying Li, Zhiping Weng, Frederic Bibollet-Ruche, Kenneth P. Zammit, Maria G. Salazar, Yalu Chen, Jesus F. Salazar-Gonzalez, Zina Moldoveanu, Jiri Mestecky, Feng Gao, Barton F. Haynes, George M. Shaw, Mark Muldoon, Bette T. M. Korber, and Beatrice H. Hahn. Antigenicity and Immunogenicity of HIV-1 Consensus Subtype B Envelope Glycoproteins. Virology, 360(1):218-234, 30 Mar 2007. PubMed ID: 17097711.
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Kovacs2012
James M. Kovacs, Joseph P. Nkolola, Hanqin Peng, Ann Cheung, James Perry, Caroline A. Miller, Michael S. Seaman, Dan H. Barouch, and Bing Chen. HIV-1 Envelope Trimer Elicits More Potent Neutralizing Antibody Responses than Monomeric gp120. Proc. Natl. Acad. Sci. U.S.A., 109(30):12111-12116, 24 Jul 2012. PubMed ID: 22773820.
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Koyama2014
Yuka Koyama, Kaori Ueno-Noto, and Keiko Takano. Affinity of HIV-1 Antibody 2G12 with Monosaccharides: A Theoretical Study Based on Explicit and Implicit Water Models. Comput. Biol. Chem., 49:36-44, Apr 2014. PubMed ID: 24583603.
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Krachmarov2005
Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306.
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Krachmarov2006
C. P. Krachmarov, W. J. Honnen, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and Abraham Pinter. Factors Determining the Breadth and Potency of Neutralization by V3-Specific Human Monoclonal Antibodies Derived from Subjects Infected with Clade A or Clade B Strains of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):7127-7135, Jul 2006. PubMed ID: 16809318.
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Kramer2007
Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119.
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Kulkarni2009
Smita S. Kulkarni, Alan Lapedes, Haili Tang, S. Gnanakaran, Marcus G. Daniels, Ming Zhang, Tanmoy Bhattacharya, Ming Li, Victoria R. Polonis, Francine E. McCutchan, Lynn Morris, Dennis Ellenberger, Salvatore T. Butera, Robert C. Bollinger, Bette T. Korber, Ramesh S. Paranjape, and David C. Montefiori. Highly Complex Neutralization Determinants on a Monophyletic Lineage of Newly Transmitted Subtype C HIV-1 Env Clones from India. Virology, 385(2):505-520, 15 Mar 2009. PubMed ID: 19167740.
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Kumar2018
Amit Kumar, Claire E. P. Smith, Elena E. Giorgi, Joshua Eudailey, David R. Martinez, Karina Yusim, Ayooluwa O. Douglas, Lisa Stamper, Erin McGuire, Celia C. LaBranche, David C. Montefiori, Genevieve G. Fouda, Feng Gao, and Sallie R. Permar. Infant Transmitted/Founder HIV-1 Viruses from Peripartum Transmission Are Neutralization Resistant to Paired Maternal Plasma. PLoS Pathog., 14(4):e1006944, Apr 2018. PubMed ID: 29672607.
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Kunert1998
R. Kunert, F. Ruker, and H. Katinger. Molecular Characterization of Five Neutralizing Anti-HIV Type 1 Antibodies: Identification of Nonconventional D Segments in the Human Monoclonal Antibodies 2G12 and 2F5. AIDS Res. Hum. Retroviruses, 14:1115-1128, 1998. Study identifies five human MAbs which were able to neutralize primary isolates of different clades in vitro and reports the nucleotide and amino acid sequences of the heavy and light chain V segments of the antibodies. PubMed ID: 9737583.
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Kwong2002
Peter D. Kwong, Michael L. Doyle, David J. Casper, Claudia Cicala, Stephanie A. Leavitt, Shahzad Majeed, Tavis D. Steenbeke, Miro Venturi, Irwin Chaiken, Michael Fung, Hermann Katinger, Paul W. I. H. Parren, James Robinson, Donald Van Ryk, Liping Wang, Dennis R. Burton, Ernesto Freire, Richard Wyatt, Joseph Sodroski, Wayne A. Hendrickson, and James Arthos. HIV-1 Evades Antibody-Mediated Neutralization through Conformational Masking of Receptor-Binding Sites. Nature, 420(6916):678-682, 12 Dec 2002. Comment in Nature. 2002 Dec 12;420(6916):623-4. PubMed ID: 12478295.
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Kwong2009a
Peter D. Kwong and Ian A. Wilson. HIV-1 and Influenza Antibodies: Seeing Antigens in New Ways. Nat. Immunol., 10(6):573-578, Jun 2009. PubMed ID: 19448659.
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Kwong2011
Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Rational Design of Vaccines to Elicit Broadly Neutralizing Antibodies to HIV-1. Cold Spring Harb. Perspect. Med., 1(1):a007278, Sep 2011. PubMed ID: 22229123.
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Kwong2012
Peter D. Kwong and John R. Mascola. Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies. Immunity, 37(3):412-425, 21 Sep 2012. PubMed ID: 22999947.
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Kwong2013
Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Broadly Neutralizing Antibodies and the Search for an HIV-1 Vaccine: The End of the Beginning. Nat. Rev. Immunol., 13(9):693-701, Sep 2013. PubMed ID: 23969737.
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Lagenaur2010
Laurel A. Lagenaur, Vadim A. Villarroel, Virgilio Bundoc, Barna Dey, and Edward A. Berger. sCD4-17b Bifunctional Protein: Extremely Broad and Potent Neutralization of HIV-1 Env Pseudotyped Viruses from Genetically Diverse Primary Isolates. Retrovirology, 7:11, 2010. PubMed ID: 20158904.
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Lambotte2009
Olivier Lambotte, Guido Ferrari, Christiane Moog, Nicole L. Yates, Hua-Xin Liao, Robert J. Parks, Charles B. Hicks, Kouros Owzar, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, and Jean-François Delfraissy. Heterogeneous Neutralizing Antibody and Antibody-Dependent Cell Cytotoxicity Responses in HIV-1 Elite Controllers. AIDS, 23(8):897-906, 15 May 2009. PubMed ID: 19414990.
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Lavine2012
Christy L. Lavine, Socheata Lao, David C. Montefiori, Barton F. Haynes, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI). High-Mannose Glycan-Dependent Epitopes Are Frequently Targeted in Broad Neutralizing Antibody Responses during Human Immunodeficiency Virus Type 1 Infection. J. Virol., 86(4):2153-2164, Feb 2012. PubMed ID: 22156525.
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Law2007
Mansun Law, Rosa M. F. Cardoso, Ian A. Wilson, and Dennis R. Burton. Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy. J. Virol., 81(8):4272-4285, Apr 2007. PubMed ID: 17267498.
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Leaman2010
Daniel P. Leaman, Heather Kinkead, and Michael B. Zwick. In-Solution Virus Capture Assay Helps Deconstruct Heterogeneous Antibody Recognition of Human Immunodeficiency Virus Type 1. J. Virol., 84(7):3382-3395, Apr 2010. PubMed ID: 20089658.
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Leaman2013
Daniel P. Leaman and Michael B. Zwick. Increased Functional Stability and Homogeneity of Viral Envelope Spikes through Directed Evolution. PLoS Pathog., 9(2):e1003184, Feb 2013. PubMed ID: 23468626.
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Li1997
A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic Neutralization of a Chimeric SIV/HIV Type 1 Virus with Combinations of Human Anti-HIV Type 1 Envelope Monoclonal Antibodies or Hyperimmune Globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233.
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Li1998
A. Li, H. Katinger, M. R. Posner, L. Cavacini, S. Zolla-Pazner, M. K. Gorny, J. Sodroski, T. C. Chou, T. W. Baba, and R. M. Ruprecht. Synergistic Neutralization of Simian-Human Immunodeficiency Virus SHIV-vpu+ by Triple and Quadruple Combinations of Human Monoclonal Antibodies and High-Titer Anti-Human Immunodeficiency Virus Type 1 Immunoglobulins. J. Virol., 72:3235-3240, 1998. PubMed ID: 9525650.
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Li2005a
Ming Li, Feng Gao, John R. Mascola, Leonidas Stamatatos, Victoria R. Polonis, Marguerite Koutsoukos, Gerald Voss, Paul Goepfert, Peter Gilbert, Kelli M. Greene, Miroslawa Bilska, Denise L Kothe, Jesus F. Salazar-Gonzalez, Xiping Wei, Julie M. Decker, Beatrice H. Hahn, and David C. Montefiori. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 79(16):10108-10125, Aug 2005. PubMed ID: 16051804.
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Li2006a
Ming Li, Jesus F. Salazar-Gonzalez, Cynthia A. Derdeyn, Lynn Morris, Carolyn Williamson, James E. Robinson, Julie M. Decker, Yingying Li, Maria G. Salazar, Victoria R. Polonis, Koleka Mlisana, Salim Abdool Karim, Kunxue Hong, Kelli M. Greene, Miroslawa Bilska, Jintao Zhou, Susan Allen, Elwyn Chomba, Joseph Mulenga, Cheswa Vwalika, Feng Gao, Ming Zhang, Bette T. M. Korber, Eric Hunter, Beatrice H. Hahn, and David C. Montefiori. Genetic and Neutralization Properties of Subtype C Human Immunodeficiency Virus Type 1 Molecular env Clones from Acute and Early Heterosexually Acquired Infections in Southern Africa. J. Virol., 80(23):11776-11790, Dec 2006. PubMed ID: 16971434.
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Li2007a
Yuxing Li, Stephen A. Migueles, Brent Welcher, Krisha Svehla, Adhuna Phogat, Mark K. Louder, Xueling Wu, George M. Shaw, Mark Connors, Richard T. Wyatt, and John R. Mascola. Broad HIV-1 Neutralization Mediated by CD4-Binding Site Antibodies. Nat. Med., 13(9):1032-1034, Sep 2007. PubMed ID: 17721546.
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Li2009c
Yuxing Li, Krisha Svehla, Mark K. Louder, Diane Wycuff, Sanjay Phogat, Min Tang, Stephen A. Migueles, Xueling Wu, Adhuna Phogat, George M. Shaw, Mark Connors, James Hoxie, John R. Mascola, and Richard Wyatt. Analysis of Neutralization Specificities in Polyclonal Sera Derived from Human Immunodeficiency Virus Type 1-Infected Individuals. J Virol, 83(2):1045-1059, Jan 2009. PubMed ID: 19004942.
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Li2012
Yuxing Li, Sijy O'Dell, Richard Wilson, Xueling Wu, Stephen D. Schmidt, Carl-Magnus Hogerkorp, Mark K. Louder, Nancy S. Longo, Christian Poulsen, Javier Guenaga, Bimal K. Chakrabarti, Nicole Doria-Rose, Mario Roederer, Mark Connors, John R. Mascola, and Richard T. Wyatt. HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully Cleaved Envelope Glycoproteins. J. Virol., 86(20):11231-11241, Oct 2012. PubMed ID: 22875963.
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Li2017
Hongru Li, Chati Zony, Ping Chen, and Benjamin K. Chen. Reduced Potency and Incomplete Neutralization of Broadly Neutralizing Antibodies against Cell-to-Cell Transmission of HIV-1 with Transmitted Founder Envs. J. Virol., 91(9), 1 May 2017. PubMed ID: 28148796.
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Liang2016
Yu Liang, Miklos Guttman, James A. Williams, Hans Verkerke, Daniel Alvarado, Shiu-Lok Hu, and Kelly K. Lee. Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan. J. Virol., 90(20):9224-9236, 15 Oct 2016. PubMed ID: 27489265.
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Liao2004
Hua-Xin Liao, S Munir Alam, John R. Mascola, James Robinson, Benjiang Ma, David C. Montefiori, Maria Rhein, Laura L. Sutherland, Richard Scearce, and Barton F. Haynes. Immunogenicity of Constrained Monoclonal Antibody A32-Human Immunodeficiency Virus (HIV) Env gp120 Complexes Compared to That of Recombinant HIV Type 1 gp120 Envelope Glycoproteins. J. Virol., 78(10):5270-5278, May 2004. PubMed ID: 15113908.
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Liao2006
Hua-Xin Liao, Laura L. Sutherland, Shi-Mao Xia, Mary E. Brock, Richard M. Scearce, Stacie Vanleeuwen, S. Munir Alam, Mildred McAdams, Eric A. Weaver, Zenaido Camacho, Ben-Jiang Ma, Yingying Li, Julie M. Decker, Gary J. Nabel, David C. Montefiori, Beatrice H. Hahn, Bette T. Korber, Feng Gao, and Barton F. Haynes. A Group M Consensus Envelope Glycoprotein Induces Antibodies That Neutralize Subsets of Subtype B and C HIV-1 Primary Viruses. Virology, 353(2):268-282, 30 Sep 2006. PubMed ID: 17039602.
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Liao2013c
Hua-Xin Liao, Chun-Yen Tsao, S. Munir Alam, Mark Muldoon, Nathan Vandergrift, Ben-Jiang Ma, Xiaozhi Lu, Laura L. Sutherland, Richard M. Scearce, Cindy Bowman, Robert Parks, Haiyan Chen, Julie H. Blinn, Alan Lapedes, Sydeaka Watson, Shi-Mao Xia, Andrew Foulger, Beatrice H. Hahn, George M. Shaw, Ron Swanstrom, David C. Montefiori, Feng Gao, Barton F. Haynes, and Bette Korber. Antigenicity and Immunogenicity of Transmitted/Founder, Consensus, and Chronic Envelope Glycoproteins of Human Immunodeficiency Virus Type 1. J. Virol., 87(8):4185-4201, Apr 2013. PubMed ID: 23365441.
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Lin2007
George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109.
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Liu2002
Xiao Song Liu, Wen Jun Liu, Kong Nan Zhao, Yue Hua Liu, Graham Leggatt, and Ian H. Frazer. Route of Administration of Chimeric BPV1 VLP Determines the Character of the Induced Immune Responses. Immunol. Cell Biol., 80(1):21-9, Feb 2002. PubMed ID: 11869359.
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Liu2011c
Pinghuang Liu, R. Glenn Overman, Nicole L. Yates, S. Munir Alam, Nathan Vandergrift, Yue Chen, Frederik Graw, Stephanie A. Freel, John C. Kappes, Christina Ochsenbauer, David C. Montefiori, Feng Gao, Alan S. Perelson, Myron S. Cohen, Barton F. Haynes, and Georgia D. Tomaras. Dynamic Antibody Specificities and Virion Concentrations in Circulating Immune Complexes in Acute to Chronic HIV-1 Infection. J. Virol., 85(21):11196-11207, Nov 2011. PubMed ID: 21865397.
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Liu2014
Pinghuang Liu, Latonya D. Williams, Xiaoying Shen, Mattia Bonsignori, Nathan A. Vandergrift, R. Glenn Overman, M. Anthony Moody, Hua-Xin Liao, Daniel J. Stieh, Kerrie L. McCotter, Audrey L. French, Thomas J. Hope, Robin Shattock, Barton F. Haynes, and Georgia D. Tomaras. Capacity for Infectious HIV-1 Virion Capture Differs by Envelope Antibody Specificity. J. Virol., 88(9):5165-5170, May 2014. PubMed ID: 24554654.
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Liu2015a
Mengfei Liu, Guang Yang, Kevin Wiehe, Nathan I. Nicely, Nathan A. Vandergrift, Wes Rountree, Mattia Bonsignori, S. Munir Alam, Jingyun Gao, Barton F. Haynes, and Garnett Kelsoe. Polyreactivity and Autoreactivity among HIV-1 Antibodies. J. Virol., 89(1):784-798, Jan 2015. PubMed ID: 25355869.
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Lorin2004
Clarisse Lorin, Lucile Mollet, Frédéric Delebecque, Chantal Combredet, Bruno Hurtrel, Pierre Charneau, Michel Brahic, and Frédéric Tangy. A Single Injection of Recombinant Measles Virus Vaccines Expressing Human Immunodeficiency Virus (HIV) Type 1 Clade B Envelope Glycoproteins Induces Neutralizing Antibodies and Cellular Immune Responses to HIV. J. Virol., 78(1):146-157, Jan 2004. PubMed ID: 14671096.
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Lorin2022
Valérie Lorin, Ignacio Fernández, Guillemette Masse-Ranson, Mélanie Bouvin-Pley, Luis M. Molinos-Albert, Cyril Planchais, Thierry Hieu, Gérard Péhau-Arnaudet, Dominik Hrebik, Giulia Girelli-Zubani, Oriane Fiquet, Florence Guivel-Benhassine, Rogier W. Sanders, Bruce D. Walker, Olivier Schwartz, Johannes F. Scheid, Jordan D. Dimitrov, Pavel Plevka, Martine Braibant, Michael S. Seaman, François Bontems, James P. Di Santo, Félix A. Rey, and Hugo Mouquet. Epitope Convergence of Broadly HIV-1 Neutralizing IgA and IgG Antibody Lineages in a Viremic Controller. J. Exp. Med., 219(3), 7 Mar 2022. PubMed ID: 35230385.
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Louder2005
Mark K. Louder, Anna Sambor, Elena Chertova, Tai Hunte, Sarah Barrett, Fallon Ojong, Eric Sanders-Buell, Susan Zolla-Pazner, Francine E. McCutchan, James D. Roser, Dana Gabuzda, Jeffrey D. Lifson, and John R. Mascola. HIV-1 Envelope Pseudotyped Viral Vectors and Infectious Molecular Clones Expressing the Same Envelope Glycoprotein Have a Similar Neutralization Phenotype, but Culture in Peripheral Blood Mononuclear Cells Is Associated with Decreased Neutralization Sensitivity. Virology, 339(2):226-238, 1 Sep 2005. PubMed ID: 16005039.
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Louis2003
John M. Louis, Issa Nesheiwat, LengChee Chang, G. Marius Clore, and Carole A. Bewley. Covalent Trimers of the Internal N-Terminal Trimeric Coiled-Coil of gp41 and Antibodies Directed against Them Are Potent Inhibitors of HIV Envelope-Mediated Cell Fusion. J. Biol. Chem., 278(22):20278-20285, 30 May 2003. PubMed ID: 12654905.
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Louis2005
John M. Louis, Carole A. Bewley, Elena Gustchina, Annie Aniana, and G. Marius Clore. Characterization and HIV-1 Fusion Inhibitory Properties of Monoclonal Fabs Obtained from a Human Non-Immune Phage Library Selected against Diverse Epitopes of the Ectodomain of HIV-1 gp41. J. Mol. Biol., 353(5):945-951, 11 Nov 2005. PubMed ID: 16216270.
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Luallen2008
Robert J. Luallen, Jianqiao Lin, Hu Fu, Karen K. Cai, Caroline Agrawal, Innocent Mboudjeka, Fang-Hua Lee, David Montefiori, David F. Smith, Robert W. Doms, and Yu Geng. An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies. J. Virol., 82(13):6447-6457, Jul 2008. PubMed ID: 18434410.
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Luallen2009
Robert J. Luallen, Hu Fu, Caroline Agrawal-Gamse, Innocent Mboudjeka, Wei Huang, Fang-Hua Lee, Lai-Xi Wang, Robert W. Doms, and Yu Geng. A Yeast Glycoprotein Shows High-Affinity Binding to the Broadly Neutralizing Human Immunodeficiency Virus Antibody 2G12 and Inhibits gp120 Interactions with 2G12 and DC-SIGN. J. Virol., 83(10):4861-4870, May 2009. PubMed ID: 19264785.
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Luallen2010
Robert J Luallen, Caroline Agrawal-Gamse, Hu Fu, David F. Smith, Robert W. Doms, and Yu Geng. Antibodies against Man-alpha1,2-Man-alpha1,2-Man Oligosaccharide Structures Recognize Envelope Glycoproteins from HIV-1 and SIV Strains. Glycobiology, 20(3):280-286, Mar 2010. PubMed ID: 19920089.
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Luo2010
Xin M. Luo, Margarida Y. Y. Lei, Rana A. Feidi, Anthony P. West, Jr., Alejandro Benjamin Balazs, Pamela J. Bjorkman, Lili Yang, and David Baltimore. Dimeric 2G12 as a Potent Protection against HIV-1. PLoS Pathog., 6(12):e1001225, 2010. PubMed ID: 21187894.
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Lusso2005
Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935.
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Lynch2011a
Rebecca M. Lynch, Rong Rong, Saikat Boliar, Anurag Sethi, Bing Li, Joseph Mulenga, Susan Allen, James E. Robinson, S. Gnanakaran, and Cynthia A. Derdeyn. The B Cell Response Is Redundant and Highly Focused on V1V2 During Early Subtype C Infection in a Zambian Seroconverter. J. Virol., 85(2):905-915, Jan 2011. PubMed ID: 20980495.
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Lynch2012
Rebecca M. Lynch, Lillian Tran, Mark K. Louder, Stephen D. Schmidt, Myron Cohen, CHAVI 001 Clinical Team Members, Rebecca DerSimonian, Zelda Euler, Elin S. Gray, Salim Abdool Karim, Jennifer Kirchherr, David C. Montefiori, Sengeziwe Sibeko, Kelly Soderberg, Georgia Tomaras, Zhi-Yong Yang, Gary J. Nabel, Hanneke Schuitemaker, Lynn Morris, Barton F. Haynes, and John R. Mascola. The Development of CD4 Binding Site Antibodies during HIV-1 Infection. J. Virol., 86(14):7588-7595, Jul 2012. PubMed ID: 22573869.
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Ma2011
Ben-Jiang Ma, S. Munir Alam, Eden P. Go, Xiaozhi Lu, Heather Desaire, Georgia D. Tomaras, Cindy Bowman, Laura L. Sutherland, Richard M. Scearce, Sampa Santra, Norman L. Letvin, Thomas B. Kepler, Hua-Xin Liao, and Barton F. Haynes. Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog., 7(9):e1002200, Sep 2011. PubMed ID: 21909262.
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Magnus2010
Carsten Magnus and Roland R. Regoes. Estimating the Stoichiometry of HIV Neutralization. PLoS Comput. Biol., 6(3):e1000713, Mar 2010. PubMed ID: 20333245.
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Magnus2016
Carsten Magnus, Lucia Reh, and Alexandra Trkola. HIV-1 Resistance to Neutralizing Antibodies: Determination of Antibody Concentrations Leading to Escape Mutant Evolution. Virus Res., 218:57-70, 15 Jun 2016. PubMed ID: 26494166.
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Malherbe2014
Delphine C. Malherbe, Franco Pissani, D. Noah Sather, Biwei Guo, Shilpi Pandey, William F. Sutton, Andrew B. Stuart, Harlan Robins, Byung Park, Shelly J. Krebs, Jason T. Schuman, Spyros Kalams, Ann J. Hessell, and Nancy L. Haigwood. Envelope variants circulating as initial neutralization breadth developed in two HIV-infected subjects stimulate multiclade neutralizing antibodies in rabbits. J Virol, 88(22):12949-67 doi, Nov 2014. PubMed ID: 25210191
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Mann2009
Axel M. Mann, Peter Rusert, Livia Berlinger, Herbert Kuster, Huldrych F. Günthard, and Alexandra Trkola. HIV Sensitivity to Neutralization Is Determined by Target and Virus Producer Cell Properties. AIDS, 23(13):1659-1667, 24 Aug 2009. PubMed ID: 19581791.
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Mannar2021
Dhiraj Mannar, Karoline Leopold, and Sriram Subramaniam. Glycan Reactive Anti-HIV-1 Antibodies bind the SARS-CoV-2 Spike Protein But Do Not Block Viral Entry. Sci. Rep., 11(1):12448, 14 Jun 2021. PubMed ID: 34127709.
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Mao2012
Youdong Mao, Liping Wang, Christopher Gu, Alon Herschhorn, Shi-Hua Xiang, Hillel Haim, Xinzhen Yang, and Joseph Sodroski. Subunit Organization of the Membrane-Bound HIV-1 Envelope Glycoprotein Trimer. Nat. Struct. Mol. Biol., 19(9):893-899, Sep 2012. PubMed ID: 22864288.
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Marradi2011
Marco Marradi, Paolo Di Gianvincenzo, Pedro M. Enríquez-Navas, Olga M. Martínez-Ávila, Fabrizio Chiodo, Eloísa Yuste, Jesús Angulo, and Soledad Penadé. Gold Nanoparticles Coated with Oligomannosides of HIV-1 Glycoprotein gp120 Mimic the Carbohydrate Epitope of Antibody 2G12. J. Mol. Biol., 410(5):798-810, 29 Jul 2011. PubMed ID: 21440555.
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Martin2008
Grégoire Martin, Yide Sun, Bernadette Heyd, Olivier Combes, Jeffrey B Ulmer, Anne Descours, Susan W Barnett, Indresh K Srivastava, and Loïc Martin. A Simple One-Step Method for the Preparation of HIV-1 Envelope Glycoprotein Immunogens Based on a CD4 Mimic Peptide. Virology, 381(2):241-250, 25 Nov 2008. PubMed ID: 18835005.
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Martin2011
Grégoire Martin, Brian Burke, Robert Thaï, Antu K. Dey, Olivier Combes, Bernadette Heyd, Anthony R. Geonnotti, David C. Montefiori, Elaine Kan, Ying Lian, Yide Sun, Toufik Abache, Jeffrey B. Ulmer, Hocine Madaoui, Raphaël Guérois, Susan W. Barnett, Indresh K. Srivastava, Pascal Kessler, and Loïc Martin. Stabilization of HIV-1 Envelope in the CD4-Bound Conformation through Specific Cross-Linking of a CD4 Mimetic. J. Biol. Chem., 286(24):21706-21716, 17 Jun 2011. PubMed ID: 21487012.
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Martines2012
Elena Martines, Isabel García, Marco Marradi, Daniel Padro, and Soledad Penadés. Dissecting the Carbohydrate Specificity of the Anti-HIV-1 2G12 Antibody by Single-Molecule Force Spectroscopy. Langmuir, 28(51):17726-17732, 21 Dec 2012. PubMed ID: 23198686.
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Martinez2009
Valérie Martinez, Marie-Claude Diemert, Martine Braibant, Valérie Potard, Jean-Luc Charuel, Francis Barin, Dominique Costagliola, Eric Caumes, Jean-Pierre Clauvel, Brigitte Autran, Lucile Musset, and ALT ANRS CO15 Study Group. Anticardiolipin Antibodies in HIV Infection Are Independently Associated with Antibodies to the Membrane Proximal External Region of gp41 and with Cell-Associated HIV DNA and Immune Activation. Clin. Infect. Dis., 48(1):123-32, 1 Jan 2009. PubMed ID: 19035778.
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Martin-Garcia2005
Julio Martín-García, Simon Cocklin, Irwin M. Chaiken, and Francisco González-Scarano. Interaction with CD4 and Antibodies to CD4-Induced Epitopes of the Envelope gp120 from a Microglial Cell-Adapted Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 79(11):6703-6713, Jun 2005. PubMed ID: 15890908.
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Marusic2009
Carla Marusic, Alessandro Vitale, Emanuela Pedrazzini, Marcello Donini, Lorenzo Frigerio, Ralph Bock, Philip J. Dix, Matthew S. McCabe, Michele Bellucci, and Eugenio Benvenuto. Plant-Based Strategies Aimed at Expressing HIV Antigens and Neutralizing Antibodies at High Levels. Nef as a Case Study. Transgenic Res., 18(4):499-512, Aug 2009. PubMed ID: 19169897.
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Marzi2007
Andrea Marzi, Daniel A. Mitchell, Chawaree Chaipan, Tanja Fisch, Robert W. Doms, Mary Carrington, Ronald C. Desrosiers, and Stefan Pöhlmann. Modulation of HIV and SIV Neutralization Sensitivity by DC-SIGN and Mannose-Binding Lectin. Virology, 368(2):322-330, 25 Nov 2007. PubMed ID: 17659761.
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Mascola1997
J. R. Mascola, M. K. Louder, T. C. VanCott, C. V. Sapan, J. S. Lambert, L. R. Muenz, B. Bunow, D. L. Birx, and M. L. Robb. Potent and Synergistic Neutralization of Human Immunodeficiency Virus (HIV) Type 1 Primary Isolates by Hyperimmune Anti-HIV Immunoglobulin Combined with Monoclonal Antibodies 2F5 and 2G12. J. Virol., 71:7198-7206, 1997. HIVIG derived from the plasma of HIV-1-infected donors, and MAbs 2F5 and 2G12 were tested against a panel of 15 clade B HIV-1 isolates, using a single concentration that is achievable in vivo (HIVIG, 2,500 microg/ml; MAbs, 25 microg/ml). While the three antibody reagents neutralized many of the viruses tested, potency varied. The virus neutralization achieved by double or triple combinations was generally equal to or greater than that predicted by the effect of individual antibodies, and the triple combination was shown to be synergistic and to have the greatest breadth and potency. Passive immunotherapy for treatment or prophylaxis of HIV-1 should consider mixtures of these potent neutralizing antibody reagents. PubMed ID: 9311792.
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Mascola1999
J. R. Mascola, M. G. Lewis, G. Stiegler, D. Harris, T. C. VanCott, D. Hayes, M. K. Louder, C. R. Brown, C. V. Sapan, S. S. Frankel, Y. Lu, M. L. Robb, H. Katinger, and D. L. Birx. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol., 73(5):4009--18, May 1999. URL: http://jvi.asm.org/cgi/content/full/73/5/4009. PubMed ID: 10196297.
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Mascola2000a
John R. Mascola, Gabriela Stiegler, Thomas C. VanCott, Hermann Katinger, Calvin B. Carpenter, Chris E. Hanson, Holly Beary, Deborah Hayes, Sarah S. Frankel, Deborah L. Birx, and Mark G. Lewis. Protection of Macaques against Vaginal Transmission of a Pathogenic HIV-1/SIV Chimeric Virus by Passive Infusion of Neutralizing Antibodies. Nat. Med., 6(2):207-210, Feb 2000. PubMed ID: 10655111.
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Mascola2001
J. R. Mascola and G. J. Nabel. Vaccines for the prevention of HIV-1 disease. Curr. Opin. Immunol., 13(4):489--95, Aug 2001. PubMed ID: 11498307.
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Mascola2002
John R. Mascola. Passive Transfer Studies to Elucidate the Role of Antibody-Mediated Protection against HIV-1. Vaccine, 20(15):1922-1925, 6 May 2002. PubMed ID: 11983246.
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Mascola2003
John R. Mascola, Mark G. Lewis, Thomas C. VanCott, Gabriela Stiegler, Hermann Katinger, Michael Seaman, Kristin Beaudry, Dan H. Barouch, Birgit Korioth-Schmitz, Georgia Krivulka, Anna Sambor, Brent Welcher, Daniel C. Douek, David C. Montefiori, John W. Shiver, Pascal Poignard, Dennis R. Burton, and Norman L. Letvin. Cellular Immunity Elicited by Human Immunodeficiency Virus Type 1/Simian Immunodeficiency Virus DNA Vaccination Does Not Augment the Sterile Protection Afforded by Passive Infusion of Neutralizing Antibodies. J. Virol., 77(19):10348-10356, Oct 2003. PubMed ID: 12970419.
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Mascola2003a
John R. Mascola. Defining the Protective Antibody Response for HIV-1. Curr. Mol. Med., 3(3):209-216, May 2003. PubMed ID: 12699358.
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Mascola2010
John R. Mascola and David C. Montefiori. The Role of Antibodies in HIV Vaccines. Annu. Rev. Immunol., 28:413-444, Mar 2010. PubMed ID: 20192810.
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Matyas2009
Gary R. Matyas, Zoltan Beck, Nicos Karasavvas, and Carl R. Alving. Lipid Binding Properties of 4E10, 2F5, and WR304 Monoclonal Antibodies that Neutralize HIV-1. Biochim. Biophys. Acta, 1788(3):660-665, Mar 2009. PubMed ID: 19100711.
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McCann2005
C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016.
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McCoy2015
Laura E. McCoy, Emilia Falkowska, Katie J. Doores, Khoa Le, Devin Sok, Marit J. van Gils, Zelda Euler, Judith A. Burger, Michael S. Seaman, Rogier W. Sanders, Hanneke Schuitemaker, Pascal Poignard, Terri Wrin, and Dennis R. Burton. Incomplete Neutralization and Deviation from Sigmoidal Neutralization Curves for HIV Broadly Neutralizing Monoclonal Antibodies. PLoS Pathog., 11(8):e1005110, Aug 2015. PubMed ID: 26267277.
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McFadden2007
Karyn McFadden, Simon Cocklin, Hosahudya Gopi, Sabine Baxter, Sandya Ajith, Naheed Mahmood, Robin Shattock, and Irwin Chaiken. A Recombinant Allosteric Lectin Antagonist of HIV-1 Envelope gp120 Interactions. Proteins, 67(3):617-629, 15 May 2007. PubMed ID: 17348010.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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McKeating1996c
J. A. McKeating. Biological Consequences of Human Immunodeficiency Virus Type 1 Envelope Polymorphism: Does Variation Matter? 1995 Fleming Lecture. J. Gen. Virol., 77:2905-2919, 1996. PubMed ID: 9000081.
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McKnight2007
Aine McKnight and Marlen M. I. Aasa-Chapman. Clade Specific Neutralising Vaccines for HIV: An Appropriate Target? Curr. HIV Res., 5(6):554-560, Nov 2007. PubMed ID: 18045111.
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McLinden2013
Robert J. McLinden, Celia C. LaBranche, Agnès-Laurence Chenine, Victoria R. Polonis, Michael A. Eller, Lindsay Wieczorek, Christina Ochsenbauer, John C. Kappes, Stephen Perfetto, David C. Montefiori, Nelson L. Michael, and Jerome H. Kim. Detection of HIV-1 Neutralizing Antibodies in a Human CD4+/CXCR4+/CCR5+ T-Lymphoblastoid Cell Assay System. PLoS One, 8(11):e77756, 2013. PubMed ID: 24312168.
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Mehandru2007
Saurabh Mehandru, Brigitta Vcelar, Terri Wrin, Gabriela Stiegler, Beda Joos, Hiroshi Mohri, Daniel Boden, Justin Galovich, Klara Tenner-Racz, Paul Racz, Mary Carrington, Christos Petropoulos, Hermann Katinger, and Martin Markowitz. Adjunctive Passive Immunotherapy in Human Immunodeficiency Virus Type 1-Infected Individuals Treated with Antiviral Therapy during Acute and Early Infection. J. Virol., 81(20):11016-11031, Oct 2007. PubMed ID: 17686878.
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Melchers2012
Mark Melchers, Ilja Bontjer, Tommy Tong, Nancy P. Y. Chung, Per Johan Klasse, Dirk Eggink, David C. Montefiori, Maurizio Gentile, Andrea Cerutti, William C. Olson, Ben Berkhout, James M. Binley, John P. Moore, and Rogier W. Sanders. Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses. J. Virol., 86(5):2488-2500, Mar 2012. PubMed ID: 22205734.
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Menendez2008
Alfredo Menendez, Daniel A. Calarese, Robyn L. Stanfield, Keith C. Chow, Chris N. Scanlan, Renate Kunert, Herman Katinger, Dennis R. Burton, Ian A. Wilson, and Jamie K. Scott. A Peptide Inhibitor of HIV-1 Neutralizing Antibody 2G12 Is Not a Structural Mimic of the Natural Carbohydrate Epitope on gp120. FASEB J., 22(5):1380-1392, May 2008. PubMed ID: 18198210.
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Miglietta2014
Riccardo Miglietta, Claudia Pastori, Assunta Venuti, Christina Ochsenbauer, and Lucia Lopalco. Synergy in Monoclonal Antibody Neutralization of HIV-1 Pseudoviruses and Infectious Molecular Clones. J. Transl. Med., 12:346, 2014. PubMed ID: 25496375.
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Miller2005
Michael D. Miller, Romas Geleziunas, Elisabetta Bianchi, Simon Lennard, Renee Hrin, Hangchun Zhang, Meiqing Lu, Zhiqiang An, Paolo Ingallinella, Marco Finotto, Marco Mattu, Adam C. Finnefrock, David Bramhill, James Cook, Debra M. Eckert, Richard Hampton, Mayuri Patel, Stephen Jarantow, Joseph Joyce, Gennaro Ciliberto, Riccardo Cortese, Ping Lu, William Strohl, William Schleif, Michael McElhaugh, Steven Lane, Christopher Lloyd, David Lowe, Jane Osbourn, Tristan Vaughan, Emilio Emini, Gaetano Barbato, Peter S. Kim, Daria J. Hazuda, John W. Shiver, and Antonello Pessi. A Human Monoclonal Antibody Neutralizes Diverse HIV-1 Isolates By Binding a Critical gp41 Epitope. Proc. Natl. Acad. Sci. U.S.A., 102(41):14759-14764, 11 Oct 2005. PubMed ID: 16203977.
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Mo1997
H. Mo, L. Stamatatos, J. E. Ip, C. F. Barbas, P. W. H. I. Parren, D. R. Burton, J. P. Moore, and D. D. Ho. Human Immunodeficiency Virus Type 1 Mutants That Escape Neutralization by Human Monoclonal Antibody IgG1b12. J. Virol., 71:6869-6874, 1997. A JRCSF resistant variant was selected by culturing in the presence of IgG1b12. The resistant virus remained sensitive to 2G12 and 2F5 and to CD4-IgG, encouraging for the possibility of combination therapy. PubMed ID: 9261412.
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Mohr2010
Emma L. Mohr, Jinhua Xiang, James H. McLinden, Thomas M. Kaufman, Qing Chang, David C. Montefiori, Donna Klinzman, and Jack T. Stapleton. GB Virus Type C Envelope Protein E2 Elicits Antibodies That React with a Cellular Antigen on HIV-1 Particles and Neutralize Diverse HIV-1 Isolates. J. Immunol., 185(7):4496-4505, 1 Oct 2010. PubMed ID: 20826757.
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Moldt2012a
Brian Moldt, Eva G. Rakasz, Niccole Schultz, Po-Ying Chan-Hui, Kristine Swiderek, Kimberly L. Weisgrau, Shari M. Piaskowski, Zachary Bergman, David I. Watkins, Pascal Poignard, and Dennis R. Burton. Highly Potent HIV-Specific Antibody Neutralization In Vitro Translates into Effective Protection against Mucosal SHIV Challenge In Vivo. Proc. Natl. Acad. Sci. U.S.A., 109(46):18921-18925, 13 Nov 2012. PubMed ID: 23100539.
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Molinos-Albert2023
Luis M. Molinos-Albert, Eduard Baquero, Melanie Bouvin-Pley, Valerie Lorin, Caroline Charre, Cyril Planchais, Jordan D. Dimitrov, Valerie Monceaux, Matthijn Vos, Laurent Hocqueloux, Jean-Luc Berger, Michael S. Seaman, Martine Braibant, Veronique Avettand-Fenoel, Asier Saez-Cirion, and Hugo Mouquet. Anti-V1/V3-glycan broadly HIV-1 neutralizing antibodies in a post-treatment controller. Cell Host Microbe, 31(8):1275-1287e8 doi, Aug 2023. PubMed ID: 37433296
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Mondor1998
I. Mondor, S. Ugolini, and Q. J. Sattentau. Human Immunodeficiency Virus Type 1 Attachment to HeLa CD4 Cells Is CD4 Independent and Gp120 Dependent and Requires Cell Surface Heparans. J. Virol., 72:3623-3634, 1998. PubMed ID: 9557643.
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Montefiori1999
D. Montefiori and T. Evans. Toward an HIV Type 1 Vaccine That Generates Potent Broadly Cross-Reactive Neutralizing Antibodies. AIDS Res. Hum. Retroviruses, 15:689-698, 1999. PubMed ID: 10357464.
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Montefiori2003
David C. Montefiori, Marcus Altfeld, Paul K. Lee, Miroslawa Bilska, Jintao Zhou, Mary N. Johnston, Feng Gao, Bruce D. Walker, and Eric S. Rosenberg. Viremia Control Despite Escape from a Rapid and Potent Autologous Neutralizing Antibody Response after Therapy Cessation in an HIV-1-Infected Individual. J. Immunol., 170(7):3906-3914, Apr 2003. PubMed ID: 12646660.
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Montefiori2005
David C. Montefiori. Neutralizing Antibodies Take a Swipe at HIV In Vivo. Nat. Med., 11(6):593-594, Jun 2005. PubMed ID: 15937465.
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Montefiori2009
David C. Montefiori and John R. Mascola. Neutralizing Antibodies against HIV-1: Can We Elicit Them with Vaccines and How Much Do We Need? Curr. Opin. HIV AIDS, 4(5):347-351, Sep 2009. PubMed ID: 20048696.
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Moody2010
M. Anthony Moody, Hua-Xin Liao, S. Munir Alam, Richard M. Scearce, M. Kelly Plonk, Daniel M. Kozink, Mark S. Drinker, Ruijun Zhang, Shi-Mao Xia, Laura L. Sutherland, Georgia D. Tomaras, Ian P. Giles, John C. Kappes, Christina Ochsenbauer-Jambor, Tara G. Edmonds, Melina Soares, Gustavo Barbero, Donald N. Forthal, Gary Landucci, Connie Chang, Steven W. King, Anita Kavlie, Thomas N. Denny, Kwan-Ki Hwang, Pojen P. Chen, Philip E. Thorpe, David C. Montefiori, and Barton F. Haynes. Anti-Phospholipid Human Monoclonal Antibodies Inhibit CCR5-Tropic HIV-1 and Induce beta-Chemokines. J. Exp. Med., 207(4):763-776, 12 Apr 2010. PubMed ID: 20368576.
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Moog2014
C. Moog, N. Dereuddre-Bosquet, J.-L. Teillaud, M. E. Biedma, V. Holl, G. Van Ham, L. Heyndrickx, A. Van Dorsselaer, D. Katinger, B. Vcelar, S. Zolla-Pazner, I. Mangeot, C. Kelly, R. J. Shattock, and R. Le Grand. Protective Effect of Vaginal Application of Neutralizing and Nonneutralizing Inhibitory Antibodies Against Vaginal SHIV Challenge in Macaques. Mucosal Immunol., 7(1):46-56, Jan 2014. PubMed ID: 23591718.
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Moore1995c
J. P. Moore and D. D. Ho. HIV-1 Neutralization: The Consequences of Adaptation to Growth on Transformed T-Cells. AIDS, 9(suppl A):S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579.
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Moore1996
J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711.
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Moore1997
J. Moore and A. Trkola. HIV Type 1 Coreceptors, Neutralization Serotypes and Vaccine Development. AIDS Res. Hum. Retroviruses, 13:733-736, 1997. PubMed ID: 9171216.
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Moore2001
J. P. Moore, P. W. Parren, and D. R. Burton. Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development. J. Virol., 75(13):5721--9, Jul 2001. URL: http://jvi.asm.org/cgi/content/full/75/13/5721. PubMed ID: 11390574.
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Moore2006
Penny L. Moore, Emma T. Crooks, Lauren Porter, Ping Zhu, Charmagne S. Cayanan, Henry Grise, Paul Corcoran, Michael B. Zwick, Michael Franti, Lynn Morris, Kenneth H. Roux, Dennis R. Burton, and James M. Binley. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1. J. Virol., 80(5):2515-2528, Mar 2006. PubMed ID: 16474158.
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Moore2009
Penny L. Moore, Elin S. Gray, and Lynn Morris. Specificity of the Autologous Neutralizing Antibody Response. Curr. Opin. HIV AIDS, 4(5):358-363, Sep 2009. PubMed ID: 20048698.
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Moore2012
Penny L. Moore, Elin S. Gray, C. Kurt Wibmer, Jinal N. Bhiman, Molati Nonyane, Daniel J. Sheward, Tandile Hermanus, Shringkhala Bajimaya, Nancy L. Tumba, Melissa-Rose Abrahams, Bronwen E. Lambson, Nthabeleng Ranchobe, Lihua Ping, Nobubelo Ngandu, Quarraisha Abdool Karim, Salim S. Abdool Karim, Ronald I. Swanstrom, Michael S. Seaman, Carolyn Williamson, and Lynn Morris. Evolution of an HIV Glycan-Dependent Broadly Neutralizing Antibody Epitope through Immune Escape. Nat. Med., 18(11):1688-1692, Nov 2012. PubMed ID: 23086475.
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Mouquet2011
Hugo Mouquet, Florian Klein, Johannes F. Scheid, Malte Warncke, John Pietzsch, Thiago Y. K. Oliveira, Klara Velinzon, Michael S. Seaman, and Michel C. Nussenzweig. Memory B Cell Antibodies to HIV-1 gp140 Cloned from Individuals Infected with Clade A and B Viruses. PLoS One, 6(9):e24078, 2011. PubMed ID: 21931643.
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Mouquet2012a
Hugo Mouquet, Louise Scharf, Zelda Euler, Yan Liu, Caroline Eden, Johannes F. Scheid, Ariel Halper-Stromberg, Priyanthi N. P. Gnanapragasam, Daniel I. R. Spencer, Michael S. Seaman, Hanneke Schuitemaker, Ten Feizi, Michel C. Nussenzweig, and Pamela J. Bjorkman. Complex-Type N-Glycan Recognition by Potent Broadly Neutralizing HIV Antibodies. Proc. Natl. Acad. Sci. U.S.A, 109(47):E3268-E3277, 20 Nov 2012. PubMed ID: 23115339.
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Moyo2018
Thandeka Moyo, June Ereño-Orbea, Rajesh Abraham Jacob, Clara E. Pavillet, Samuel Mundia Kariuki, Emily N. Tangie, Jean-Philippe Julien, and Jeffrey R. Dorfman. Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11. J. Virol., 92(14), 15 Jul 2018. PubMed ID: 29618644.
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Murin2014
Charles D. Murin, Jean-Philippe Julien, Devin Sok, Robyn L. Stanfield, Reza Khayat, Albert Cupo, John P. Moore, Dennis R. Burton, Ian A. Wilson, and Andrew B. Ward. Structure of 2G12 Fab2 in Complex with Soluble and Fully Glycosylated HIV-1 Env by Negative-Stain Single-Particle Electron Microscopy. J. Virol., 88(17):10177-10188, 1 Sep 2014. PubMed ID: 24965454.
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Naarding2007
Marloes A. Naarding, Elly Baan, Georgios Pollakis, and William A. Paxton. Effect of Chloroquine on Reducing HIV-1 Replication In Vitro and the DC-SIGN Mediated Transfer of Virus to CD4+ T-Lymphocytes. Retrovirology, 4:6, 2007. PubMed ID: 17263871.
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Nabatov2004
Alexey A. Nabatov, Georgios Pollakis, Thomas Linnemann, Aletta Kliphius, Moustapha I. M. Chalaby, and William A. Paxton. Intrapatient Alterations in the Human Immunodeficiency Virus Type 1 gp120 V1V2 and V3 Regions Differentially Modulate Coreceptor Usage, Virus Inhibition by CC/CXC Chemokines, Soluble CD4, and the b12 and 2G12 Monoclonal Antibodies. J. Virol., 78(1):524-530, Jan 2004. PubMed ID: 14671134.
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Nabel2005
Gary J. Nabel. Close to the Edge: Neutralizing the HIV-1 Envelope. Science, 308(5730):1878-1879, 24 Jun 2005. PubMed ID: 15976295.
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Nakowitsch2005
Sabine Nakowitsch, Heribert Quendler, Helga Fekete, Renate Kunert, Hermann Katinger, and Gabriela Stiegler. HIV-1 Mutants Escaping Neutralization by the Human Antibodies 2F5, 2G12, and 4E10: In Vitro Experiments Versus Clinical Studies. AIDS, 19(17):1957-1966, 18 Nov 2005. PubMed ID: 16260901.
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Nandi2010
Avishek Nandi, Christine L. Lavine, Pengcheng Wang, Inna Lipchina, Paul A. Goepfert, George M. Shaw, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, Philippa Easterbrook, James E. Robinson, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology. Epitopes for Broad and Potent Neutralizing Antibody Responses during Chronic Infection with Human Immunodeficiency Virus Type 1. Virology, 396(2):339-348, 20 Jan 2010. PubMed ID: 19922969.
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Narayan2013
Kristin M. Narayan, Nitish Agrawal, Sean X. Du, Janelle E. Muranaka, Katherine Bauer, Daniel P. Leaman, Pham Phung, Kay Limoli, Helen Chen, Rebecca I. Boenig, Terri Wrin, Michael B. Zwick, and Robert G. Whalen. Prime-Boost Immunization of Rabbits with HIV-1 gp120 Elicits Potent Neutralization Activity against a Primary Viral Isolate. PLoS One, 8(1):e52732, 9 Jan 2013. PubMed ID: 23326351.
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Nie2010
Jianhui Nie, Chuntao Zhang, Wei Liu, Xueling Wu, Feng Li, Suting Wang, Fuxiong Liang, Aijing Song, and Youchun Wang. Genotypic and Phenotypic Characterization of HIV-1 CRF01\_AE env Molecular Clones from Infections in China. J. Acquir. Immune Defic. Syndr., 53(4):440-450, 1 Apr 2010. PubMed ID: 20090544.
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Nie2020
Jianhui Nie, Weijin Huang, Qiang Liu, and Youchun Wang. HIV-1 Pseudoviruses Constructed in China Regulatory Laboratory. Emerg. Microbes Infect., 9(1):32-41, 2020. PubMed ID: 31859609.
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Nishiyama2009
Yasuhiro Nishiyama, Stephanie Planque, Yukie Mitsuda, Giovanni Nitti, Hiroaki Taguchi, Lei Jin, Jindrich Symersky, Stephane Boivin, Marcin Sienczyk, Maria Salas, Carl V. Hanson, and Sudhir Paul. Toward Effective HIV Vaccination: Induction of Binary Epitope Reactive Antibodies with Broad HIV Neutralizing Activity. J. Biol. Chem., 284(44):30627-30642, 30 Oct 2009. PubMed ID: 19726674.
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Nogal2020
Bartek Nogal, Laura E. McCoy, Marit J. van Gils, Christopher A. Cottrell, James E. Voss, Raiees Andrabi, Matthias Pauthner, Chi-Hui Liang, Terrence Messmer, Rebecca Nedellec, Mia Shin, Hannah L. Turner, Gabriel Ozorowski, Rogier W. Sanders, Dennis R. Burton, and Andrew B. Ward. HIV Envelope Trimer-Elicited Autologous Neutralizing Antibodies Bind a Region Overlapping the N332 Glycan Supersite. Sci. Adv., 6(23):eaba0512, Jun 2020. PubMed ID: 32548265.
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Nolan2009
Katrina M. Nolan, Gregory Q. Del Prete, Andrea P. O. Jordan, Beth Haggarty, Josephine Romano, George J. Leslie, and James A. Hoxie. Characterization of a Human Immunodeficiency Virus Type 1 V3 Deletion Mutation That Confers Resistance to CCR5 Inhibitors and the Ability to Use Aplaviroc-Bound Receptor. J. Virol., 83(8):3798-3809, Apr 2009. PubMed ID: 19193800.
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Nora2008
Tamara Nora, Francine Bouchonnet, Béatrice Labrosse, Charlotte Charpentier, Fabrizio Mammano, François Clavel, and Allan J. Hance. Functional Diversity of HIV-1 Envelope Proteins Expressed by Contemporaneous Plasma Viruses. Retrovirology, 5:23, 2008. PubMed ID: 18312646.
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Ofek2004
Gilad Ofek, Min Tang, Anna Sambor, Hermann Katinger, John R. Mascola, Richard Wyatt, and Peter D. Kwong. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope. J. Virol., 78(19):10724-10737, Oct 2004. PubMed ID: 15367639.
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Ohagen2003
Asa Ohagen, Amy Devitt, Kevin J. Kunstman, Paul R. Gorry, Patrick P. Rose, Bette Korber, Joann Taylor, Robert Levy, Robert L. Murphy, Steven M. Wolinsky, and Dana Gabuzda. Genetic and Functional Analysis of Full-Length Human Immunodeficiency Virus Type 1 env Genes Derived from Brain and Blood of Patients with AIDS. J. Virol., 77(22):12336-12345, Nov 2003. PubMed ID: 14581570.
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Opalka2004
David Opalka, Antonello Pessi, Elisabetta Bianchi, Gennaro Ciliberto, William Schleif, Michael McElhaugh, Renee Danzeisen, Romas Geleziunas, Michael Miller, Debra M. Eckert, David Bramhill, Joseph Joyce, James Cook, William Magilton, John Shiver, Emilio Emini, and Mark T. Esser. Analysis of the HIV-1 gp41 Specific Immune Response Using a Multiplexed Antibody Detection Assay. J. Immunol. Methods, 287(1-2):49-65, Apr 2004. PubMed ID: 15099755.
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ORourke2009
Sara M. O'Rourke, Becky Schweighardt, William G. Scott, Terri Wrin, Dora P. A. J. Fonseca, Faruk Sinangil, and Phillip W. Berman. Novel Ring Structure in the gp41 Trimer of Human Immunodeficiency Virus Type 1 That Modulates Sensitivity and Resistance to Broadly Neutralizing Antibodies. J. Virol., 83(15):7728-7738, Aug 2009. PubMed ID: 19474108.
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ORourke2010
Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Dora P. A. J. Fonseca, Karianne Terry, Terri Wrin, Faruk Sinangil, and Phillip W. Berman. Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus. J. Virol., 84(21):11200-11209, Nov 2010. PubMed ID: 20702624.
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Overbaugh2012
Julie Overbaugh and Lynn Morris. The Antibody Response against HIV-1. Cold Spring Harb. Perspect. Med., 2(1):a007039, Jan 2012. PubMed ID: 22315717.
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Pahar2006
Bapi Pahar, Mayra A. Cantu, Wei Zhao, Marcelo J. Kuroda, Ronald S. Veazey, David C. Montefiori, John D. Clements, Pyone P. Aye, Andrew A. Lackner, Karin Lovgren-Bengtsson, and Karol Sestak. Single Epitope Mucosal Vaccine Delivered via Immuno-Stimulating Complexes Induces Low Level of Immunity Against Simian-HIV. Vaccine, 24(47-48):6839-6849, 17 Nov 2006. PubMed ID: 17050045.
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Pancera2005
Marie Pancera and Richard Wyatt. Selective Recognition of Oligomeric HIV-1 Primary Isolate Envelope Glycoproteins by Potently Neutralizing Ligands Requires Efficient Precursor Cleavage. Virology, 332(1):145-156, 5 Feb 2005. PubMed ID: 15661147.
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Pantophlet2003
Ralph Pantophlet, Erica Ollmann Saphire, Pascal Poignard, Paul W. H. I. Parren, Ian A. Wilson, and Dennis R. Burton. Fine Mapping of the Interaction of Neutralizing and Nonneutralizing Monoclonal Antibodies with the CD4 Binding Site of Human Immunodeficiency Virus Type 1 gp120. J. Virol., 77(1):642-658, Jan 2003. PubMed ID: 12477867.
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Pantophlet2003b
Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582.
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Pantophlet2004
R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540.
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Pantophlet2006
Ralph Pantophlet and Dennis R. Burton. GP120: Target for Neutralizing HIV-1 Antibodies. Annu. Rev. Immunol., 24:739-769, 2006. PubMed ID: 16551265.
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Pantophlet2009
Ralph Pantophlet, Meng Wang, Rowena O. Aguilar-Sino, and Dennis R. Burton. The Human Immunodeficiency Virus Type 1 Envelope Spike of Primary Viruses Can Suppress Antibody Access to Variable Regions. J. Virol., 83(4):1649-1659, Feb 2009. PubMed ID: 19036813.
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Pantophlet2010
Ralph Pantophlet. Antibody Epitope Exposure and Neutralization of HIV-1. Curr. Pharm. Des., 16(33):3729-3743, 2010. PubMed ID: 21128886.
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Park2000
E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031.
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Parren1997
P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324.
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Parren1998
P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629.
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Parren1998a
P. W. Parren, M. Wang, A. Trkola, J. M. Binley, M. Purtscher, H. Katinger, J. P. Moore, and D. R. Burton. Antibody neutralization-resistant primary isolates of human immunodeficiency virus type 1. J. Virol., 72:10270-4, 1998. PubMed ID: 9811774.
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Parren1999
P. W. Parren, J. P. Moore, D. R. Burton, and Q. J. Sattentau. The Neutralizing Antibody Response to HIV-1: Viral Evasion and Escape from Humoral Immunity. AIDS, 13(Suppl A):S137-162, 1999. PubMed ID: 10885772.
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Pashov2005
Anastas Pashov, Stewart MacLeod, Rinku Saha, Marty Perry, Thomas C. VanCott, and Thomas Kieber-Emmons. Concanavalin A Binding to HIV Envelope Protein Is Less Sensitive to Mutations in Glycosylation Sites than Monoclonal Antibody 2G12. Glycobiology, 15(10):994-1001, Oct 2005. PubMed ID: 15917430.
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Pashov2005a
Anastas Pashov, Gabriela Canziani, Stewart Macleod, Jason Plaxco, Behjatolah Monzavi-Karbassi, and Thomas Kieber-Emmons. Targeting Carbohydrate Antigens in HIV Vaccine Development. Vaccine, 23(17-18):2168-2175, 18 Mar 2005. PubMed ID: 15755589.
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Pashov2006
Anastas D. Pashov, Jason Plaxco, Srinivas V. Kaveri, Behjatolah Monzavi-Karbassi, Donald Harn, and Thomas Kieber-Emmons. Multiple Antigenic Mimotopes of HIV Carbohydrate Antigens: Relating Structure and Antigenicity. J. Biol. Chem., 281(40):29675-29683, 6 Oct 2006. PubMed ID: 16899462.
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Patel2008
Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735.
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Peachman2010a
Kristina K. Peachman, Lindsay Wieczorek, Victoria R. Polonis, Carl R. Alving, and Mangala Rao. The Effect of sCD4 on the Binding and Accessibility of HIV-1 gp41 MPER Epitopes to Human Monoclonal Antibodies. Virology, 408(2):213-223, 20 Dec 2010. PubMed ID: 20961591.
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Pegu2017
Amarendra Pegu, Ann J. Hessell, John R. Mascola, and Nancy L. Haigwood. Use of Broadly Neutralizing Antibodies for HIV-1 Prevention. Immunol. Rev., 275(1):296-312, Jan 2017. PubMed ID: 28133803.
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Pejchal2011
Robert Pejchal, Katie J. Doores, Laura M. Walker, Reza Khayat, Po-Ssu Huang, Sheng-Kai Wang, Robyn L. Stanfield, Jean-Philippe Julien, Alejandra Ramos, Max Crispin, Rafael Depetris, Umesh Katpally, Andre Marozsan, Albert Cupo, Sebastien Maloveste, Yan Liu, Ryan McBride, Yukishige Ito, Rogier W. Sanders, Cassandra Ogohara, James C. Paulson, Ten Feizi, Christopher N. Scanlan, Chi-Huey Wong, John P. Moore, William C. Olson, Andrew B. Ward, Pascal Poignard, William R. Schief, Dennis R. Burton, and Ian A. Wilson. A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield. Science, 334(6059):1097-1103, 25 Nov 2011. PubMed ID: 21998254.
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Perdomo2008
Maria F. Perdomo, Michael Levi, Matti Sällberg, and Anders Vahlne. Neutralization of HIV-1 by Redirection of Natural Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(34):12515-12520, 26 Aug 2008. PubMed ID: 18719129.
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Peressin2011
M. Peressin, V. Holl, S. Schmidt, T. Decoville, D. Mirisky, A. Lederle, M. Delaporte, K. Xu, A. M. Aubertin, and C. Moog. HIV-1 Replication in Langerhans and Interstitial Dendritic Cells Is Inhibited by Neutralizing and Fc-Mediated Inhibitory Antibodies. J. Virol., 85(2):1077-1085, Jan 2011. PubMed ID: 21084491.
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Perez2009
Lautaro G. Perez, Matthew R. Costa, Christopher A. Todd, Barton F. Haynes, and David C. Montefiori. Utilization of Immunoglobulin G Fc Receptors by Human Immunodeficiency Virus Type 1: A Specific Role for Antibodies against the Membrane-Proximal External Region of gp41. J. Virol., 83(15):7397-7410, Aug 2009. PubMed ID: 19458010.
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Peters2008a
Paul J. Peters, Maria J. Duenas-Decamp, W. Matthew Sullivan, Richard Brown, Chiambah Ankghuambom, Katherine Luzuriaga, James Robinson, Dennis R. Burton, Jeanne Bell, Peter Simmonds, Jonathan Ball, and Paul R. Clapham. Variation in HIV-1 R5 Macrophage-Tropism Correlates with Sensitivity to Reagents that Block Envelope: CD4 Interactions But Not with Sensitivity to Other Entry Inhibitors. Retrovirology, 5:5, 2008. PubMed ID: 18205925.
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Pham2014
Tram N. Q. Pham, Sabelo Lukhele, Fadi Hajjar, Jean-Pierre Routy, and Éric A. Cohen. HIV Nef and Vpu Protect HIV-Infected CD4+ T Cells from Antibody-Mediated Cell Lysis through Down-Modulation of CD4 and BST2. Retrovirology, 11:15, 2014. PubMed ID: 24498878.
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Phogat2007
S. Phogat, R. T. Wyatt, and G. B. Karlsson Hedestam. Inhibition of HIV-1 Entry by Antibodies: Potential Viral and Cellular Targets. J. Intern. Med., 262(1):26-43, Jul 2007. PubMed ID: 17598813.
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Pinter2004
Abraham Pinter, William J. Honnen, Yuxian He, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection. J. Virol., 78(10):5205-5215, May 2004. PubMed ID: 15113902.
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Pinter2005
Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930.
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Platis2009a
Dimitris Platis and Nikolaos E. Labrou. Application of a PEG/Salt Aqueous Two-Phase Partition System for the Recovery of Monoclonal Antibodies from Unclarified Transgenic Tobacco Extract. Biotechnol. J., 4(9):1320-1327, Sep 2009. PubMed ID: 19557796.
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Platt2012
Emily J. Platt, Michelle M. Gomes, and David Kabat. Kinetic Mechanism for HIV-1 Neutralization by Antibody 2G12 Entails Reversible Glycan Binding That Slows Cell Entry. Proc. Natl. Acad. Sci. U.S.A., 109(20):7829-7834, 15 May 2012. PubMed ID: 22547820.
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Pluckthun2010
Andreas Plückthun. HIV: Antibodies with a Split Personality. Nature, 467(7315):537-538, 30 Sep 2010. PubMed ID: 20882002.
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Poignard1996
P. Poignard, P. J. Klasse, and Q. J. Sattentau. Antibody Neutralization of HIV-1. Immunol. Today, 17:239-246, 1996. Comprehensive review of HIV envelope gp120 and gp41 antibody binding domains, and different cross-reactivity groups of MAbs ability to neutralize primary isolates. The distinction between neutralization of laboratory strains and primary isolates is discussed. The only three epitopes that have confirmed broad neutralization against a spectrum of isolates are gp120 epitopes for IgG1b12 and 2G12, and the gp41 epitope of 2F5. PubMed ID: 8991386.
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Poignard1999
P. Poignard, R. Sabbe, G. R. Picchio, M. Wang, R. J. Gulizia, H. Katinger, P. W. Parren, D. E. Mosier, and D. R. Burton. Neutralizing Antibodies Have Limited Effects on the Control of Established HIV-1 Infection In Vivo. Immunity, 10:431-438, 1999. PubMed ID: 10229186.
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Poignard2001
P. Poignard, E. O. Saphire, P. W. Parren, and D. R. Burton. gp120: Biologic aspects of structural features. Annu. Rev. Immunol., 19:253--74, 2001. URL: http://immunol.annualreviews.org/cgi/content/full/19/1/253. PubMed ID: 11244037.
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Pollara2013
Justin Pollara, Mattia Bonsignori, M. Anthony Moody, Marzena Pazgier, Barton F. Haynes, and Guido Ferrari. Epitope Specificity of Human Immunodeficiency Virus-1 Antibody Dependent Cellular Cytotoxicity (ADCC) Responses. Curr. HIV Res., 11(5):378-387, Jul 2013. PubMed ID: 24191939.
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Poon2005
B. Poon, J. F. Hsu, V. Gudeman, I. S. Y. Chen, and K. Grovit-Ferbas. Formaldehyde-Treated, Heat-Inactivated Virions with Increased Human Immunodeficiency Virus Type 1 Env Can Be Used To Induce High-Titer Neutralizing Antibody Responses. J. Virol., 79(16):10210-10217, Aug 2005. PubMed ID: 16051814.
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Prevost2017
Jérémie Prévost, Daria Zoubchenok, Jonathan Richard, Maxime Veillette, Beatriz Pacheco, Mathieu Coutu, Nathalie Brassard, Matthew S. Parsons, Kiat Ruxrungtham, Torsak Bunupuradah, Sodsai Tovanabutra, Kwan-Ki Hwang, M. Anthony Moody, Barton F. Haynes, Mattia Bonsignori, Joseph Sodroski, Daniel E. Kaufmann, George M. Shaw, Agnes L. Chenine, and Andrés Finzi. Influence of the Envelope gp120 Phe 43 Cavity on HIV-1 Sensitivity to Antibody-Dependent Cell-Mediated Cytotoxicity Responses. J. Virol., 91(7), 1 Apr 2017. PubMed ID: 28100618.
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Prevost2018
Jérémie Prévost, Jonathan Richard, Shilei Ding, Beatriz Pacheco, Roxanne Charlebois, Beatrice H Hahn, Daniel E Kaufmann, and Andrés Finzi. Envelope Glycoproteins Sampling States 2/3 Are Susceptible to ADCC by Sera from HIV-1-Infected Individuals. Virology, 515:38-45, Feb 2018. PubMed ID: 29248757.
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Prigent2018
Julie Prigent, Annaëlle Jarossay, Cyril Planchais, Caroline Eden, Jérémy Dufloo, Ayrin Kök, Valérie Lorin, Oxana Vratskikh, Thérèse Couderc, Timothée Bruel, Olivier Schwartz, Michael S. Seaman, Ohlenschläger, Jordan D. Dimitrov, and Hugo Mouquet. Conformational Plasticity in Broadly Neutralizing HIV-1 Antibodies Triggers Polyreactivity. Cell Rep., 23(9):2568-2581, 29 May 2018. PubMed ID: 29847789.
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Pugach2004
Pavel Pugach, Shawn E. Kuhmann, Joann Taylor, Andre J. Marozsan, Amy Snyder, Thomas Ketas, Steven M. Wolinsky, Bette T. Korber, and John P. Moore. The Prolonged Culture of Human Immunodeficiency Virus Type 1 in Primary Lymphocytes Increases its Sensitivity to Neutralization by Soluble CD4. Virology, 321(1):8-22, 30 Mar 2004. PubMed ID: 15033560.
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Pugach2008
Pavel Pugach, Thomas J. Ketas, Elizabeth Michael, and John P. Moore. Neutralizing Antibody and Anti-Retroviral Drug Sensitivities of HIV-1 Isolates Resistant to Small Molecule CCR5 Inhibitors. Virology, 377(2):401-407, 1 Aug 2008. PubMed ID: 18519143.
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Pugach2015
Pavel Pugach, Gabriel Ozorowski, Albert Cupo, Rajesh Ringe, Anila Yasmeen, Natalia de Val, Ronald Derking, Helen J. Kim, Jacob Korzun, Michael Golabek, Kevin de Los Reyes, Thomas J. Ketas, Jean-Philippe Julien, Dennis R. Burton, Ian A. Wilson, Rogier W. Sanders, P. J. Klasse, Andrew B. Ward, and John P. Moore. A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene. J. Virol., 89(6):3380-3395, Mar 2015. PubMed ID: 25589637.
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Quakkelaar2007a
Esther D. Quakkelaar, Floris P. J. van Alphen, Brigitte D. M. Boeser-Nunnink, Ad C. van Nuenen, Ralph Pantophlet, and Hanneke Schuitemaker. Susceptibility of Recently Transmitted Subtype B Human Immunodeficiency Virus Type 1 Variants to Broadly Neutralizing Antibodies. J. Virol., 81(16):8533-8542, Aug 2007. PubMed ID: 17522228.
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Rademacher2008
Thomas Rademacher, Markus Sack, Elsa Arcalis, Johannes Stadlmann, Simone Balzer, Friedrich Altmann, Heribert Quendler, Gabriela Stiegler, Renate Kunert, Rainer Fischer, and Eva Stoger. Recombinant Antibody 2G12 Produced in Maize Endosperm Efficiently Neutralizes HIV-1 and Contains Predominantly Single-GlcNAc N-Glycans. Plant Biotechnol. J., 6(2):189-201, Feb 2008. PubMed ID: 17979949.
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Rainwater2007
Stephanie M. J. Rainwater, Xueling Wu, Ruth Nduati, Rebecca Nedellec, Donald Mosier, Grace John-Stewart, Dorothy Mbori-Ngacha, and Julie Overbaugh. Cloning and Characterization of Functional Subtype A HIV-1 Envelope Variants Transmitted Through Breastfeeding. Curr. HIV Res., 5(2):189-197, Mar 2007. PubMed ID: 17346133.
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Raja2003
Aarti Raja, Miro Venturi, Peter Kwong, and Joseph Sodroski. CD4 Binding Site Antibodies Inhibit Human Immunodeficiency Virus gp120 Envelope Glycoprotein Interaction with CCR5. J. Virol., 77(1):713-718, Jan 2003. PubMed ID: 12477875.
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Raviv2005
Yossef Raviv, Mathias Viard, Julian W. Bess, Jr., Elena Chertova, and Robert Blumenthal. Inactivation of Retroviruses with Preservation of Structural Integrity by Targeting the Hydrophobic Domain of the Viral Envelope. J. Virol., 79(19):12394-12400, Oct 2005. PubMed ID: 16160166.
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Reeves2005
Jacqueline D. Reeves, Fang-Hua Lee, John L. Miamidian, Cassandra B. Jabara, Marisa M. Juntilla, and Robert W. Doms. Enfuvirtide Resistance Mutations: Impact on Human Immunodeficiency Virus Envelope Function, Entry Inhibitor Sensitivity, and Virus Neutralization. J. Virol., 79(8):4991-4999, Apr 2005. PubMed ID: 15795284.
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Ren2018
Yanqin Ren, Maria Korom, Ronald Truong, Dora Chan, Szu-Han Huang, Colin C. Kovacs, Erika Benko, Jeffrey T. Safrit, John Lee, Hermes Garbán, Richard Apps, Harris Goldstein, Rebecca M. Lynch, and R. Brad Jones. Susceptibility to Neutralization by Broadly Neutralizing Antibodies Generally Correlates with Infected Cell Binding for a Panel of Clade B HIV Reactivated from Latent Reservoirs. J. Virol., 92(23), 1 Dec 2018. PubMed ID: 30209173.
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Revilla2011
Ana Revilla, Elena Delgado, Elizabeth C. Christian, Justin Dalrymple, Yolanda Vega, Cristina Carrera, Maria González-Galeano, Antonio Ocampo, Rafael Ojea de Castro, Maria J. Lezaún, Raúl Rodriguez, Ana Mariño, Patricia Ordóñez, Gustavo Cilla, Ramón Cisterna, Juan M. Santamaria, Santiago Prieto, Aza Rakhmanova, Anna Vinogradova, Maritza Ríos, Lucía Pérez-Álvarez, Rafael Nájera, David C. Montefiori, Michael S. Seaman, and Michael M. Thomson. Construction and Phenotypic Characterization of HIV Type 1 Functional Envelope Clones of subtypes G and F. AIDS Res. Hum. Retroviruses, 27(8):889-901, Aug 2011. PubMed ID: 21226626.
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Richard2014
Jonathan Richard, Maxime Veillette, Laurie-Anne Batraville, Mathieu Coutu, Jean-Philippe Chapleau, Mattia Bonsignori, Nicole Bernard, Cécile Tremblay, Michel Roger, Daniel E. Kaufmann, and Andrés Finzi. Flow Cytometry-Based Assay to Study HIV-1 gp120 Specific Antibody-Dependent Cellular Cytotoxicity Responses. J. Virol. Methods, 208:107-.14, Nov 2014. PubMed ID: 25125129.
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Richman2003
Douglas D. Richman, Terri Wrin, Susan J. Little, and Christos J. Petropoulos. Rapid Evolution of the Neutralizing Antibody Response to HIV Type 1 Infection. Proc. Natl. Acad. Sci. U.S.A., 100(7):4144-4149, 1 Apr 2003. PubMed ID: 12644702.
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Ringe2010
Rajesh Ringe, Madhuri Thakar, and Jayanta Bhattacharya. Variations in Autologous Neutralization and CD4 Dependence of b12 Resistant HIV-1 Clade C env Clones Obtained at Different Time Points from Antiretroviral Naïve Indian Patients with Recent Infection. Retrovirology, 7:76, 2010. PubMed ID: 20860805.
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Rits-Volloch2006
Sophia Rits-Volloch, Gary Frey, Stephen C. Harrison, and Bing Chen. Restraining the Conformation of HIV-1 gp120 by Removing a Flexible Loop. EMBO J., 25(20):5026-5035, 18 Oct 2006. PubMed ID: 17006538.
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RobertGuroff2000
Marjorie Robert-Guroff. IgG Surfaces as an Important Component in Mucosal Protection. Nat. Med., 6(2):129-130, Feb 2000. PubMed ID: 10655090.
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Rudometova2022
N. B. Rudometova, N. S. Shcherbakova, D. N. Shcherbakov, O. S. Taranov, B. N. Zaitsev, and L. I. Karpenko. Construction and Characterization of HIV-1 env-Pseudoviruses of the Recombinant Form CRF63_02A and Subtype A6. Bull Exp Biol Med, 172(6):729-733 doi, Apr 2022. PubMed ID: 35501651
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Ruprecht2011
Claudia R. Ruprecht, Anders Krarup, Lucy Reynell, Axel M. Mann, Oliver F. Brandenberg, Livia Berlinger, Irene A. Abela, Roland R. Regoes, Huldrych F. Günthard, Peter Rusert, and Alexandra Trkola. MPER-Specific Antibodies Induce gp120 Shedding and Irreversibly Neutralize HIV-1. J. Exp. Med., 208(3):439-454, 14 Mar 2011. PubMed ID: 21357743.
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Rusert2005
Peter Rusert, Herbert Kuster, Beda Joos, Benjamin Misselwitz, Cornelia Gujer, Christine Leemann, Marek Fischer, Gabriela Stiegler, Hermann Katinger, William C Olson, Rainer Weber, Leonardo Aceto, Huldrych F Günthard, and Alexandra Trkola. Virus Isolates during Acute and Chronic Human Immunodeficiency Virus Type 1 Infection Show Distinct Patterns of Sensitivity to Entry Inhibitors. J. Virol., 79(13):8454-8469, Jul 2005. PubMed ID: 15956589.
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Rusert2009
Peter Rusert, Axel Mann, Michael Huber, Viktor von Wyl, Huldrych F. Günthar, and Alexandra Trkola. Divergent Effects of Cell Environment on HIV Entry Inhibitor Activity. AIDS, 23(11):1319-1327, 17 Jul 2009. PubMed ID: 19579289.
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Russell2011
Elizabeth S. Russell, Jesse J. Kwiek, Jessica Keys, Kirston Barton, Victor Mwapasa, David C. Montefiori, Steven R. Meshnick, and Ronald Swanstrom. The Genetic Bottleneck in Vertical Transmission of Subtype C HIV-1 Is Not Driven by Selection of Especially Neutralization-Resistant Virus from the Maternal Viral Population. J Virol, 85(16):8253-8262, Aug 2011. PubMed ID: 21593171.
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Sabin2010
Charles Sabin, Davide Corti, Victor Buzon, Mike S. Seaman, David Lutje Hulsik, Andreas Hinz, Fabrizia Vanzetta, Gloria Agatic, Chiara Silacci, Lara Mainetti, Gabriella Scarlatti, Federica Sallusto, Robin Weiss, Antonio Lanzavecchia, and Winfried Weissenhorn. Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41. PLoS Pathog., 6(11):e1001195, 2010. PubMed ID: 21124990.
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Safrit2004
Jeffrey T. Safrit, Ruth Ruprecht, Flavia Ferrantelli, Weidong Xu, Moiz Kitabwalla, Koen Van Rompay, Marta Marthas, Nancy Haigwood, John R. Mascola, Katherine Luzuriaga, Samuel Adeniyi Jones, Bonnie J. Mathieson, Marie-Louise Newell, and Ghent IAS Working Group on HIV in Women Children. Immunoprophylaxis to Prevent Mother-to-Child Transmission of HIV-1. J. Acquir. Immune Defic. Syndr., 35(2):169-177, 1 Feb 2004. PubMed ID: 14722451.
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Sagar2012
Manish Sagar, Hisashi Akiyama, Behzad Etemad, Nora Ramirez, Ines Freitas, and Suryaram Gummuluru. Transmembrane Domain Membrane Proximal External Region but Not Surface Unit-Directed Broadly Neutralizing HIV-1 Antibodies Can Restrict Dendritic Cell-Mediated HIV-1 Trans-Infection. J. Infect. Dis., 205(8):1248-1257, 15 Apr 2012. PubMed ID: 22396600.
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Sainsbury2010
Frank Sainsbury, Markus Sack, Johannes Stadlmann, Heribert Quendler, Rainer Fischer, and George P. Lomonossoff. Rapid Transient Production in Plants by Replicating and Non-Replicating Vectors Yields High Quality Functional Anti-HIV Antibody. PLoS One, 5(11):e13976, 2010. PubMed ID: 21103044.
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Sajadi2012
Mohammad M. Sajadi, George K. Lewis, Michael S. Seaman, Yongjun Guan, Robert R. Redfield, and Anthony L. DeVico. Signature Biochemical Properties of Broadly Cross-Reactive HIV-1 Neutralizing Antibodies in Human Plasma. J. Virol., 86(9):5014-5025, May 2012. PubMed ID: 22379105.
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Sanchez-Merino2016
V. Sanchez-Merino, A. Fabra-Garcia, N. Gonzalez, D. Nicolas, A. Merino-Mansilla, C. Manzardo, J. Ambrosioni, A. Schultz, A. Meyerhans, J. R. Mascola, J. M. Gatell, J. Alcami, J. M. Miro, and E. Yuste. Detection of Broadly Neutralizing Activity within the First Months of HIV-1 Infection. J. Virol., 90(11):5231-5245, 1 Jun 2016. PubMed ID: 26984721.
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Sanders2002
Rogier W. Sanders, Miro Venturi, Linnea Schiffner, Roopa Kalyanaraman, Hermann Katinger, Kenneth O. Lloyd, Peter D. Kwong, and John P. Moore. The Mannose-Dependent Epitope for Neutralizing Antibody 2G12 on Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Virol., 76(14):7293-7305, Jul 2002. PubMed ID: 12072528.
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Sanders2002a
Rogier W. Sanders, Mika Vesanen, Norbert Schuelke, Aditi Master, Linnea Schiffner, Roopa Kalyanaraman, Maciej Paluch, Ben Berkhout, Paul J. Maddon, William C. Olson, Min Lu, and John P. Moore. Stabilization of the Soluble, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1. J. Virol., 76(17):8875-8889, Sep 2002. PubMed ID: 12163607.
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Sanders2013
Rogier W. Sanders, Ronald Derking, Albert Cupo, Jean-Philippe Julien, Anila Yasmeen, Natalia de Val, Helen J. Kim, Claudia Blattner, Alba Torrents de la Peña, Jacob Korzun, Michael Golabek, Kevin de los Reyes, Thomas J. Ketas, Marit J. van Gils, C. Richter King, Ian A. Wilson, Andrew B. Ward, P. J. Klasse, and John P. Moore. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but not Non-Neutralizing Antibodies. PLoS Pathog., 9(9):e1003618, Sep 2013. PubMed ID: 24068931.
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Sanders2015
Rogier W. Sanders, Marit J. van Gils, Ronald Derking, Devin Sok, Thomas J. Ketas, Judith A. Burger, Gabriel Ozorowski, Albert Cupo, Cassandra Simonich, Leslie Goo, Heather Arendt, Helen J. Kim, Jeong Hyun Lee, Pavel Pugach, Melissa Williams, Gargi Debnath, Brian Moldt, Mariëlle J. van Breemen, Gözde Isik, Max Medina-Ramírez, Jaap Willem Back, Wayne C. Koff, Jean-Philippe Julien, Eva G. Rakasz, Michael S. Seaman, Miklos Guttman, Kelly K. Lee, Per Johan Klasse, Celia LaBranche, William R. Schief, Ian A. Wilson, Julie Overbaugh, Dennis R. Burton, Andrew B. Ward, David C. Montefiori, Hansi Dean, and John P. Moore. HIV-1 Neutralizing Antibodies Induced by Native-Like Envelope Trimers. Science, 349(6244):aac4223, 10 Jul 2015. PubMed ID: 26089353.
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Sather2014
D. Noah Sather, Sara Carbonetti, Delphine C. Malherbe, Franco Pissani, Andrew B. Stuart, Ann J. Hessell, Mathew D. Gray, Iliyana Mikell, Spyros A. Kalams, Nancy L. Haigwood, and Leonidas Stamatatos. Emergence of Broadly Neutralizing Antibodies and Viral Coevolution in Two Subjects during the Early Stages of Infection with Human Immunodeficiency Virus Type 1. J. Virol., 88(22):12968-12981, Nov 2014. PubMed ID: 25122781.
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Q. J. Sattentau. Neutralization of HIV-1 by Antibody. Curr. Opin. Immunol., 8:540-545, 1996. Review. PubMed ID: 8794008.
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Sattentau2010
Quentin J. Sattentau and Andrew J. McMichael. New Templates for HIV-1 Antibody-Based Vaccine Design. F1000 Biol. Rep., 2:60, 2010. PubMed ID: 21173880.
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Saunders2017
Kevin O. Saunders, Nathan I. Nicely, Kevin Wiehe, Mattia Bonsignori, R. Ryan Meyerhoff, Robert Parks, William E. Walkowicz, Baptiste Aussedat, Nelson R. Wu, Fangping Cai, Yusuf Vohra, Peter K. Park, Amanda Eaton, Eden P. Go, Laura L. Sutherland, Richard M. Scearce, Dan H. Barouch, Ruijun Zhang, Tarra Von Holle, R. Glenn Overman, Kara Anasti, Rogier W. Sanders, M. Anthony Moody, Thomas B. Kepler, Bette Korber, Heather Desaire, Sampa Santra, Norman L. Letvin, Gary J. Nabel, David C. Montefiori, Georgia D. Tomaras, Hua-Xin Liao, S. Munir Alam, Samuel J. Danishefsky, and Barton F. Haynes. Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman Primates. Cell Rep., 18(9):2175-2188, 28 Feb 2017. PubMed ID: 28249163.
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Savarino2001
A. Savarino, L. Gennero, H. C. Chen, D. Serrano, F. Malavasi, J. R. Boelaert, and K. Sperber. Anti-HIV effects of chloroquine: mechanisms of inhibition and spectrum of activity. AIDS, 15(17):2221--9, 23 Nov 2001. PubMed ID: 11698694.
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Scanlan2002
Christopher N. Scanlan, Ralph Pantophlet, Mark R. Wormald, Erica Ollmann Saphire, Robyn Stanfield, Ian A. Wilson, Hermann Katinger, Raymond A. Dwek, Pauline M. Rudd, and Dennis R. Burton. The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2G12 Recognizes a Cluster of Alpha1→2 Mannose Residues on the Outer Face of gp120. J. Virol., 76(14):7306-7321, Jul 2002. PubMed ID: 12072529.
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Scanlan2007
Christopher N. Scanlan, Gayle E. Ritchie, Kavitha Baruah, Max Crispin, David J. Harvey, Bernhard B. Singer, Lothar Lucka, Mark R. Wormald, Paul Wentworth, Jr., Nicole Zitzmann, Pauline M. Rudd, Dennis R Burton, and Raymond A. Dwek. Inhibition of Mammalian Glycan Biosynthesis Produces Non-Self Antigens for a Broadly Neutralising, HIV-1 Specific Antibody. J. Mol. Biol., 372(1):16-22, 7 Sep 2007. PubMed ID: 17631311.
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Scheid2009
Johannes F. Scheid, Hugo Mouquet, Niklas Feldhahn, Michael S. Seaman, Klara Velinzon, John Pietzsch, Rene G. Ott, Robert M. Anthony, Henry Zebroski, Arlene Hurley, Adhuna Phogat, Bimal Chakrabarti, Yuxing Li, Mark Connors, Florencia Pereyra, Bruce D. Walker, Hedda Wardemann, David Ho, Richard T. Wyatt, John R. Mascola, Jeffrey V. Ravetch, and Michel C. Nussenzweig. Broad Diversity of Neutralizing Antibodies Isolated from Memory B Cells in HIV-Infected Individuals. Nature, 458(7238):636-640, 2 Apr 2009. PubMed ID: 19287373.
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Schief2009
William R. Schief, Yih-En Andrew Ban, and Leonidas Stamatatos. Challenges for Structure-Based HIV Vaccine Design. Curr. Opin. HIV AIDS, 4(5):431-440, Sep 2009. PubMed ID: 20048708.
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Schiffner2016
Torben Schiffner, Natalia de Val, Rebecca A. Russell, Steven W. de Taeye, Alba Torrents de la Peña, Gabriel Ozorowski, Helen J. Kim, Travis Nieusma, Florian Brod, Albert Cupo, Rogier W. Sanders, John P. Moore, Andrew B. Ward, and Quentin J. Sattentau. Chemical Cross-Linking Stabilizes Native-Like HIV-1 Envelope Glycoprotein Trimer Antigens. J. Virol., 90(2):813-828, 28 Oct 2015. PubMed ID: 26512083.
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Schiffner2018
Torben Schiffner, Jesper Pallesen, Rebecca A. Russell, Jonathan Dodd, Natalia de Val, Celia C. LaBranche, David Montefiori, Georgia D. Tomaras, Xiaoying Shen, Scarlett L. Harris, Amin E. Moghaddam, Oleksandr Kalyuzhniy, Rogier W. Sanders, Laura E. McCoy, John P. Moore, Andrew B. Ward, and Quentin J. Sattentau. Structural and Immunologic Correlates of Chemically Stabilized HIV-1 Envelope Glycoproteins. PLoS Pathog., 14(5):e1006986, May 2018. PubMed ID: 29746590.
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Schonning1998
K. Schonning, A. Bolmstedt, J. Novotny, O. S. Lund, S. Olofsson, and J. E. Hansen. Induction of Antibodies against Epitopes Inaccessible on the HIV Type 1 Envelope Oligomer by Immunization with Recombinant Monomeric Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:1451-1456, 1998. PubMed ID: 9824323.
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Schorcht2020
Anna Schorcht, Tom L. G. M. van den Kerkhof, Christopher A. Cottrell, Joel D. Allen, Jonathan L. Torres, Anna-Janina Behrens, Edith E. Schermer, Judith A. Burger, Steven W. de Taeye, Alba Torrents de la Peña, Ilja Bontjer, Stephanie Gumbs, Gabriel Ozorowski, Celia C. LaBranche, Natalia de Val, Anila Yasmeen, Per Johan Klasse, David C. Montefiori, John P. Moore, Hanneke Schuitemaker, Max Crispin, Marit J. van Gils, Andrew B. Ward, and Rogier W. Sanders. Neutralizing Antibody Responses Induced by HIV-1 Envelope Glycoprotein SOSIP Trimers Derived from Elite Neutralizers. J. Virol., 94(24), 23 Nov 2020. PubMed ID: 32999024.
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Schulke2002
Norbert Schulke, Mika S. Vesanen, Rogier W. Sanders, Ping Zhu, Min Lu, Deborah J. Anselma, Anthony R. Villa, Paul W. H. I. Parren, James M. Binley, Kenneth H. Roux, Paul J. Maddon, John P. Moore, and William C. Olson. Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein. J. Virol., 76(15):7760-76, Aug 2002. PubMed ID: 12097589.
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Schultz2018
Anke Schultz, Anja Germann, Martina Fuss, Marcella Sarzotti-Kelsoe, Daniel A. Ozaki, David C. Montefiori, Heiko Zimmermann, and Hagen von Briesen. Validation of an Automated System for Aliquoting of HIV-1 Env-Pseudotyped Virus Stocks. PLoS One, 13(1):1-20, Jan 2018. PubMed ID: 29300769.
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Schweighardt2007
Becky Schweighardt, Yang Liu, Wei Huang, Colombe Chappey, Yolanda S. Lie, Christos J. Petropoulos, and Terri Wrin. Development of an HIV-1 Reference Panel of Subtype B Envelope Clones Isolated from the Plasma of Recently Infected Individuals. J. Acquir. Immune Defic. Syndr., 46(1):1-11, 1 Sep 2007. PubMed ID: 17514017.
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Sellhorn2012
George Sellhorn, Zane Kraft, Zachary Caldwell, Katharine Ellingson, Christine Mineart, Michael S. Seaman, David C. Montefiori, Eliza Lagerquist, and Leonidas Stamatatos. Engineering, Expression, Purification, and Characterization of Stable Clade A/B Recombinant Soluble Heterotrimeric gp140 Proteins. J. Virol., 86(1):128-142, Jan 2012. PubMed ID: 22031951.
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Selvarajah2005
Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142.
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Shan2007
Meimei Shan, Per Johan Klasse, Kaustuv Banerjee, Antu K Dey, Sai Prasad N. Iyer, Robert Dionisio, Dustin Charles, Lila Campbell-Gardener, William C. Olson, Rogier W. Sanders, and John P. Moore. HIV-1 gp120 Mannoses Induce Immunosuppressive Responses from Dendritic Cells. PLoS Pathog., 3(11):e169, Nov 2007. PubMed ID: 17983270.
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Shang2011
Hong Shang, Xiaoxu Han, Xuanling Shi, Teng Zuo, Mark Goldin, Dan Chen, Bing Han, Wei Sun, Hao Wu, Xinquan Wang, and Linqi Zhang. Genetic and Neutralization Sensitivity of Diverse HIV-1 env Clones from Chronically Infected Patients in China. J. Biol. Chem., 286(16):14531-14541, 22 Apr 2011. PubMed ID: 21325278.
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Shen2010
Xiaoying Shen, S. Moses Dennison, Pinghuang Liu, Feng Gao, Frederick Jaeger, David C. Montefiori, Laurent Verkoczy, Barton F. Haynes, S. Munir Alam, and Georgia D. Tomaras. Prolonged Exposure of the HIV-1 gp41 Membrane Proximal Region with L669S Substitution. Proc. Natl. Acad. Sci. U.S.A., 107(13):5972-5977, 30 Mar 2010. PubMed ID: 20231447.
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Sheppard2007a
Neil C. Sheppard, Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins. Clin. Vaccine Immunol., 14(2):157-167, Feb 2007. PubMed ID: 17167037.
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Si2001
Zhihai Si, Mark Cayabyab, and Joseph Sodroski. Envelope Glycoprotein Determinants of nEutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys. J. Virol., 75(9):4208-4218, May 2001. PubMed ID: 11287570.
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Siddappa2010
Nagadenahalli B. Siddappa, Jennifer D. Watkins, Klemens J. Wassermann, Ruijiang Song, Wendy Wang, Victor G. Kramer, Samir Lakhashe, Michael Santosuosso, Mark C. Poznansky, Francis J. Novembre, François Villinger, James G. Else, David C. Montefiori, Robert A. Rasmussen, and Ruth M. Ruprecht. R5 Clade C SHIV Strains with Tier 1 or 2 Neutralization Sensitivity: Tools to Dissect Env Evolution and to Develop AIDS Vaccines in Primate Models. PLoS One, 5(7):e11689, 2010. PubMed ID: 20657739.
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Simek2009
Melissa D. Simek, Wasima Rida, Frances H. Priddy, Pham Pung, Emily Carrow, Dagna S. Laufer, Jennifer K. Lehrman, Mark Boaz, Tony Tarragona-Fiol, George Miiro, Josephine Birungi, Anton Pozniak, Dale A. McPhee, Olivier Manigart, Etienne Karita, André Inwoley, Walter Jaoko, Jack DeHovitz, Linda-Gail Bekker, Punnee Pitisuttithum, Robert Paris, Laura M. Walker, Pascal Poignard, Terri Wrin, Patricia E. Fast, Dennis R. Burton, and Wayne C. Koff. Human Immunodeficiency Virus Type 1 Elite Neutralizers: Individuals with Broad and Potent Neutralizing Activity Identified by Using a High-Throughput Neutralization Assay together with an Analytical Selection Algorithm. J. Virol., 83(14):7337-7348, Jul 2009. PubMed ID: 19439467.
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Simonich2016
Cassandra A. Simonich, Katherine L. Williams, Hans P. Verkerke, James A. Williams, Ruth Nduati, Kelly K. Lee, and Julie Overbaugh. HIV-1 Neutralizing Antibodies with Limited Hypermutation from an Infant. Cell, 166(1):77-87, 30 Jun 2016. PubMed ID: 27345369.
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Singh2003
Suddham Singh, Jiahong Ni, and Lai-Xi Wang. Chemoenzymatic Synthesis of High-Mannose Type HIV-1 gp120 Glycopeptides. Bioorg. Med. Chem. Lett., 13(3):327-330, 10 Feb 2003. PubMed ID: 12565922.
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Singh2011
Harvir Singh, Kevin A. Henry, Sampson S. T. Wu, Andrzej Chruscinski, Paul J. Utz, and Jamie K. Scott. Reactivity Profiles of Broadly Neutralizing Anti-HIV-1 Antibodies Are Distinct from Those of Pathogenic Autoantibodies. AIDS, 25(10):1247-1257, 19 Jun 2011. PubMed ID: 21508803.
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Sirois2007
Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757.
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Sliepen2019
Kwinten Sliepen, Byung Woo Han, Ilja Bontjer, Petra Mooij, Fernando Garces, Anna-Janina Behrens, Kimmo Rantalainen, Sonu Kumar, Anita Sarkar, Philip J. M. Brouwer, Yuanzi Hua, Monica Tolazzi, Edith Schermer, Jonathan L. Torres, Gabriel Ozorowski, Patricia van der Woude, Alba Torrents de la Pena, Marielle J. van Breemen, Juan Miguel Camacho-Sanchez, Judith A. Burger, Max Medina-Ramirez, Nuria Gonzalez, Jose Alcami, Celia LaBranche, Gabriella Scarlatti, Marit J. van Gils, Max Crispin, David C. Montefiori, Andrew B. Ward, Gerrit Koopman, John P. Moore, Robin J. Shattock, Willy M. Bogers, Ian A. Wilson, and Rogier W. Sanders. Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence. Nat Commun, 10(1):2355 doi, May 2019. PubMed ID: 31142746
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Smalls-Mantey2012
Adjoa Smalls-Mantey, Nicole Doria-Rose, Rachel Klein, Andy Patamawenu, Stephen A. Migueles, Sung-Youl Ko, Claire W. Hallahan, Hing Wong, Bai Liu, Lijing You, Johannes Scheid, John C. Kappes, Christina Ochsenbauer, Gary J. Nabel, John R. Mascola, and Mark Connors. Antibody-Dependent Cellular Cytotoxicity against Primary HIV-Infected CD4+ T Cells Is Directly Associated with the Magnitude of Surface IgG Binding. J. Virol., 86(16):8672-8680, Aug 2012. PubMed ID: 22674985.
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Sok2014a
Devin Sok, Katie J. Doores, Bryan Briney, Khoa M. Le, Karen L. Saye-Francisco, Alejandra Ramos, Daniel W. Kulp, Jean-Philippe Julien, Sergey Menis, Lalinda Wickramasinghe, Michael S. Seaman, William R. Schief, Ian A. Wilson, Pascal Poignard, and Dennis R. Burton. Promiscuous Glycan Site Recognition by Antibodies to the High-Mannose Patch of gp120 Broadens Neutralization of HIV. Sci. Transl. Med., 6(236):236ra63, 14 May 2014. PubMed ID: 24828077.
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Sok2016
Devin Sok, Matthias Pauthner, Bryan Briney, Jeong Hyun Lee, Karen L. Saye-Francisco, Jessica Hsueh, Alejandra Ramos, Khoa M. Le, Meaghan Jones, Joseph G. Jardine, Raiza Bastidas, Anita Sarkar, Chi-Hui Liang, Sachin S. Shivatare, Chung-Yi Wu, William R. Schief, Chi-Huey Wong, Ian A. Wilson, Andrew B. Ward, Jiang Zhu, Pascal Poignard, and Dennis R. Burton. A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans. Immunity, 45(1):31-45, 19 Jul 2016. PubMed ID: 27438765.
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Spenlehauer2001
C. Spenlehauer, C. A. Gordon, A. Trkola, and J. P. Moore. A luciferase-reporter gene-expressing T-cell line facilitates neutralization and drug-sensitivity assays that use either R5 or X4 strains of human immunodeficiency virus type 1. Virology, 280(2):292--300, 15 Feb 2001. PubMed ID: 11162843.
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Srivastava2005
Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830.
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Stamatatos2009
Leonidas Stamatatos, Lynn Morris, Dennis R. Burton, and John R. Mascola. Neutralizing Antibodies Generated during Natural HIV-1 Infection: Good News for an HIV-1 Vaccine? Nat. Med., 15(8):866-870, Aug 2009. PubMed ID: 19525964.
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Stephenson2016
Kathryn E. Stephenson and Dan H. Barouch. Broadly Neutralizing Antibodies for HIV Eradication. Curr. HIV/AIDS Rep., 13(1):31-37, Feb 2016. PubMed ID: 26841901.
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Stewart-Jones2016
Guillaume B. E. Stewart-Jones, Cinque Soto, Thomas Lemmin, Gwo-Yu Chuang, Aliaksandr Druz, Rui Kong, Paul V. Thomas, Kshitij Wagh, Tongqing Zhou, Anna-Janina Behrens, Tatsiana Bylund, Chang W. Choi, Jack R. Davison, Ivelin S. Georgiev, M. Gordon Joyce, Young Do Kwon, Marie Pancera, Justin Taft, Yongping Yang, Baoshan Zhang, Sachin S. Shivatare, Vidya S. Shivatare, Chang-Chun D. Lee, Chung-Yi Wu, Carole A. Bewley, Dennis R. Burton, Wayne C. Koff, Mark Connors, Max Crispin, Ulrich Baxa, Bette T. Korber, Chi-Huey Wong, John R. Mascola, and Peter D. Kwong. Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G. Cell, 165(4):813-826, 5 May 2016. PubMed ID: 27114034.
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Stiegler2001
G. Stiegler, R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 17(18):1757--65, 10 Dec 2001. PubMed ID: 11788027.
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Stiegler2002
Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Heribert Stoiber, Renate Kunert, Nelson L. Michael, Linda L. Jagodzinski, Christoph Ammann, Walter Jäger, Jeffrey Jacobson, Norbert Vetter, and Hermann Katinger. Antiviral Activity of the Neutralizing Antibodies 2F5 and 2G12 in Asymptomatic HIV-1-Infected Humans: A Phase I Evaluation. AIDS, 16(15):2019-2025, 18 Oct 2002. PubMed ID: 12370500.
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Strasser2009
Richard Strasser, Alexandra Castilho, Johannes Stadlmann, Renate Kunert, Heribert Quendler, Pia Gattinger, Jakub Jez, Thomas Rademacher, Friedrich Altmann, Lukas Mach, and Herta Steinkellner. Improved Virus Neutralization by Plant-Produced Anti-HIV Antibodies with a Homogeneous beta1,4-Galactosylated N-Glycan Profile. J. Biol. Chem., 284(31):20479-20485, 31 Jul 2009. PubMed ID: 19478090.
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Sullivan1998
N. Sullivan, Y. Sun, Q. Sattentau, M. Thali, D. Wu, G. Denisova, J. Gershoni, J. Robinson, J. Moore, and J. Sodroski. CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization. J. Virol., 72:4694-4703, 1998. A study of the sCD4 inducible MAb 17bi, and the MAb CG10 that recognizes a gp120-CD4 complex. These epitopes are minimally accessible upon attachment of gp120 to the cell. The CD4-binding induced changes in gp120 were studied, exploring the sequestering of chemokine receptor binding sites from the humoral response. PubMed ID: 9573233.
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Sundling2012
Christopher Sundling, Yuxing Li, Nick Huynh, Christian Poulsen, Richard Wilson, Sijy O'Dell, Yu Feng, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. High-Resolution Definition of Vaccine-Elicited B Cell Responses Against the HIV Primary Receptor Binding Site. Sci. Transl. Med., 4(142):142ra96, 11 Jul 2012. PubMed ID: 22786681.
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Swanson2010
Michael D. Swanson, Harry C. Winter, Irwin J. Goldstein, and David M. Markovitz. A Lectin Isolated from Bananas Is a Potent Inhibitor of HIV Replication. J. Biol. Chem., 285(12):8646-55, 19 Mar 2010. PubMed ID: 20080975.
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Takefman1998
D. M. Takefman, B. L. Sullivan, B. E. Sha, and G. T. Spear. Mechanisms of Resistance of HIV-1 Primary Isolates to Complement-Mediated Lysis. Virology, 246:370-378, 1998. PubMed ID: 9657955.
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Tasca2008
Silvana Tasca, Siu-Hong Ho, and Cecilia Cheng-Mayer. R5X4 Viruses Are Evolutionary, Functional, and Antigenic Intermediates in the Pathway of a Simian-Human Immunodeficiency Virus Coreceptor Switch. J. Virol., 82(14):7089-7099, Jul 2008. PubMed ID: 18480460.
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Taylor2008
Brian M. Taylor, J. Scott Foulke, Robin Flinko, Alonso Heredia, Anthony DeVico, and Marvin Reitz. An Alteration of Human Immunodeficiency Virus gp41 Leads to Reduced CCR5 Dependence and CD4 Independence. J. Virol., 82(11):5460-5471, Jun 2008. PubMed ID: 18353949.
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Thenin2012a
Suzie Thenin, Emmanuelle Roch, Tanawan Samleerat, Thierry Moreau, Antoine Chaillon, Alain Moreau, Francis Barin, and Martine Braibant. Naturally Occurring Substitutions of Conserved Residues in Human Immunodeficiency Virus Type 1 Variants of Different Clades Are Involved in PG9 and PG16 Resistance to Neutralization. J. Gen. Virol., 93(7):1495-1505, Jul 2012. PubMed ID: 22492917.
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Thida2019
Win Thida, Takeo Kuwata, Yosuke Maeda, Tetsu Yamashiro, Giang Van Tran, Kinh Van Nguyen, Masafumi Takiguchi, Hiroyuki Gatanaga, Kazuki Tanaka, and Shuzo Matsushita. The Role of Conventional Antibodies Targeting the CD4 Binding Site and CD4-Induced Epitopes in the Control of HIV-1 CRF01\_AE Viruses. Biochem. Biophys. Res. Commun., 508(1):46-51, 1 Jan 2019. PubMed ID: 30470571.
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Todd2012
Christopher A. Todd, Kelli M. Greene, Xuesong Yu, Daniel A. Ozaki, Hongmei Gao, Yunda Huang, Maggie Wang, Gary Li, Ronald Brown, Blake Wood, M. Patricia D'Souza, Peter Gilbert, David C. Montefiori, and Marcella Sarzotti-Kelsoe. Development and Implementation of an International Proficiency Testing Program for a Neutralizing Antibody Assay for HIV-1 in TZM-bl Cells. J. Immunol. Methods, 375(1-2):57-67, 31 Jan 2012. PubMed ID: 21968254.
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Tokarev2015
Andrey Tokarev, Charlotte Stoneham, Mary K. Lewinski, Amey Mukim, Savitha Deshmukh, Thomas Vollbrecht, Celsa A. Spina, and John Guatelli. Pharmacologic Inhibition of Nedd8 Activation Enzyme Exposes CD4-Induced Epitopes within Env on Cells Expressing HIV-1. J. Virol., 90(5):2486-2502, 16 Dec 2015. PubMed ID: 26676780.
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Tomaras2008
Georgia D. Tomaras, Nicole L. Yates, Pinghuang Liu, Li Qin, Genevieve G. Fouda, Leslie L. Chavez, Allan C. Decamp, Robert J. Parks, Vicki C. Ashley, Judith T. Lucas, Myron Cohen, Joseph Eron, Charles B. Hicks, Hua-Xin Liao, Steven G. Self, Gary Landucci, Donald N. Forthal, Kent J. Weinhold, Brandon F. Keele, Beatrice H. Hahn, Michael L. Greenberg, Lynn Morris, Salim S. Abdool Karim, William A. Blattner, David C. Montefiori, George M. Shaw, Alan S. Perelson, and Barton F. Haynes. Initial B-Cell Responses to Transmitted Human Immunodeficiency Virus Type 1: Virion-Binding Immunoglobulin M (IgM) and IgG Antibodies Followed by Plasma Anti-gp41 Antibodies with Ineffective Control of Initial Viremia. J. Virol., 82(24):12449-12463, Dec 2008. PubMed ID: 18842730.
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Tomaras2011
Georgia D. Tomaras, James M. Binley, Elin S. Gray, Emma T. Crooks, Keiko Osawa, Penny L. Moore, Nancy Tumba, Tommy Tong, Xiaoying Shen, Nicole L. Yates, Julie Decker, Constantinos Kurt Wibmer, Feng Gao, S. Munir Alam, Philippa Easterbrook, Salim Abdool Karim, Gift Kamanga, John A. Crump, Myron Cohen, George M. Shaw, John R. Mascola, Barton F. Haynes, David C. Montefiori, and Lynn Morris. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals. J. Virol., 85(21):11502-11519, Nov 2011. PubMed ID: 21849452.
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Tong2012
Tommy Tong, Ema T. Crooks, Keiko Osawa, and James M. Binley. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes. J. Virol., 86(7):3574-3587, Apr 2012. PubMed ID: 22301141.
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Trkola1995a
A. Trkola, A. B. Pomales, H. Yuan, B. Korber, P. J. Maddon, G. P. Allaway, H. Katinger, C. F. Barbas III, D. R. Burton, D. D. Ho, and J. P. Moore. Cross-Clade Neutralization of Primary Isolates of Human Immunodeficiency Virus Type 1 by Human Monoclonal Antibodies and Tetrameric CD4-IgG. J. Virol., 69:6609-6617, 1995. Three MAbs, IgG1b12, 2G12, and 2F5 tetrameric CD4-IgG2 were tested for their ability to neutralize primary isolates from clades A-F. 2F5 and CD4-IgG2 were able to neutralize within and outside clade B with a high potency. IgG1b12 and 2G12 could potently neutralize isolates from within clade B, but showed a reduction in efficacy outside of clade B. 2F5 neutralization was dependent on the presence of the sequence: LDKW. PubMed ID: 7474069.
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Trkola1996
A. Trkola, M. Purtscher, T. Muster, C. Ballaun, A. Buchacher, N. Sullivan, K. Srinivasan, J. Sodroski, J. P. Moore, and H. Katinger. Human Monoclonal Antibody 2G12 Defines a Distinctive Neutralization Epitope on the gp120 Glycoprotein of Human Immunodeficiency Virus Type 1. J. Virol., 70:1100-1108, 1996. PubMed ID: 8551569.
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Trkola1996b
A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796.
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Trkola1998
A. Trkola, T. Ketas, V. N. Kewalramani, F. Endorf, J. M. Binley, H. Katinger, J. Robinson, D. R. Littman, and J. P. Moore. Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Primary Isolates to Antibodies and CD4-Based Reagents Is Independent of Coreceptor Usage. J. Virol., 72:1876-1885, 1998. PubMed ID: 9499039.
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Trkola2005
Alexandra Trkola, Herbert Kuster, Peter Rusert, Beda Joos, Marek Fischer, Christine Leemann, Amapola Manrique, Michael Huber, Manuela Rehr, Annette Oxenius, Rainer Weber, Gabriela Stiegler, Brigitta Vcelar, Hermann Katinger, Leonardo Aceto, and Huldrych F. Günthard. Delay of HIV-1 Rebound after Cessation of Antiretroviral Therapy through Passive Transfer of Human Neutralizing Antibodies. Nat. Med., 11(6):615-622, Jun 2005. PubMed ID: 15880120.
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Yates2018
Nicole L. Yates, Allan C. deCamp, Bette T. Korber, Hua-Xin Liao, Carmela Irene, Abraham Pinter, James Peacock, Linda J. Harris, Sheetal Sawant, Peter Hraber, Xiaoying Shen, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayapan, Phillip W. Berman, Merlin L. Robb, Giuseppe Pantaleo, Susan Zolla-Pazner, Barton F. Haynes, S. Munir Alam, David C. Montefiori, and Georgia D. Tomaras. HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees. J. Virol., 92(8), 15 Apr 2018. PubMed ID: 29386288.
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Ye2006
Ling Ye, Yuliang Sun, Jianguo Lin, Zhigao Bu, Qingyang Wu, Shibo Jiang, David A. Steinhauer, Richard W. Compans, and Chinglai Yang. Antigenic Properties of a Transport-Competent Influenza HA/HIV Env Chimeric Protein. Virology, 352(1):74-85, 15 Aug 2006. PubMed ID: 16725170.
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Yee2011
Michael Yee, Krystyna Konopka, Jan Balzarini, and Nejat Düzgüneş. Inhibition of HIV-1 Env-Mediated Cell-Cell Fusion by Lectins, Peptide T-20, and Neutralizing Antibodies. Open Virol. J., 5:44-51, 2011. PubMed ID: 21660189.
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Yoshimura2010
Kazuhisa Yoshimura, Shigeyoshi Harada, Junji Shibata, Makiko Hatada, Yuko Yamada, Chihiro Ochiai, Hirokazu Tamamura, and Shuzo Matsushita. Enhanced Exposure of Human Immunodeficiency Virus Type 1 Primary Isolate Neutralization Epitopes through Binding of CD4 Mimetic Compounds. J. Virol., 84(15):7558-7568, Aug 2010. PubMed ID: 20504942.
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Yu2018
Wen-Han Yu, Peng Zhao, Monia Draghi, Claudia Arevalo, Christina B. Karsten, Todd J. Suscovich, Bronwyn Gunn, Hendrik Streeck, Abraham L. Brass, Michael Tiemeyer, Michael Seaman, John R. Mascola, Lance Wells, Douglas A. Lauffenburger, and Galit Alter. Exploiting Glycan Topography for Computational Design of Env Glycoprotein Antigenicity. PLoS Comput. Biol., 14(4):e1006093, Apr 2018. PubMed ID: 29677181.
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Yuan2005
Wen Yuan, Stewart Craig, Xinzhen Yang, and Joseph Sodroski. Inter-Subunit Disulfide Bonds in Soluble HIV-1 Envelope Glycoprotein Trimers. Virology, 332(1):369-383, 5 Feb 2005. PubMed ID: 15661168.
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Yuan2006
Wen Yuan, Jessica Bazick, and Joseph Sodroski. Characterization of the Multiple Conformational States of Free Monomeric and Trimeric Human Immunodeficiency Virus Envelope Glycoproteins after Fixation by Cross-Linker. J. Virol., 80(14):6725-6737, Jul 2006. PubMed ID: 16809278.
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ZederLutz2001
G. Zeder-Lutz, J. Hoebeke, and M. H. Van Regenmortel. Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies. Eur. J. Biochem., 268(10):2856--66, May 2001. PubMed ID: 11358501.
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Zhang2002
Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155.
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Zhang2007
Mei-Yun Zhang and Dimiter S. Dimitrov. Novel Approaches for Identification of Broadly Cross-Reactive HIV-1 Neutralizing Human Monoclonal Antibodies and Improvement of Their Potency. Curr. Pharm. Des., 13(2):203-212, 2007. PubMed ID: 17269928.
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Zhang2008
Mei-Yun Zhang, Bang K. Vu, Anil Choudhary, Hong Lu, Michael Humbert, Helena Ong, Munir Alam, Ruth M. Ruprecht, Gerald Quinnan, Shibo Jiang, David C. Montefiori, John R. Mascola, Christopher C. Broder, Barton F. Haynes, and Dimiter S. Dimitrov. Cross-Reactive Human Immunodeficiency Virus Type 1-Neutralizing Human Monoclonal Antibody That Recognizes a Novel Conformational Epitope on gp41 and Lacks Reactivity against Self-Antigens. J. Virol., 82(14):6869-6879, Jul 2008. PubMed ID: 18480433.
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Zhang2010
Mei-Yun Zhang, Andrew Rosa Borges, Roger G. Ptak, Yanping Wang, Antony S. Dimitrov, S. Munir Alam, Lindsay Wieczorek, Peter Bouma, Timothy Fouts, Shibo Jiang, Victoria R. Polonis, Barton F. Haynes, Gerald V. Quinnan, David C. Montefiori, and Dimiter S. Dimitrov. Potent and Broad Neutralizing Activity of a Single Chain Antibody Fragment against Cell-Free and Cell-Associated HIV-1. mAbs, 2(3):266-274, May-Jun 2010. PubMed ID: 20305395.
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Zolla-Pazner2005
Susan Zolla-Pazner. Improving on Nature: Focusing the Immune Response on the V3 Loop. Hum. Antibodies, 14(3-4):69-72, 2005. PubMed ID: 16720976.
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Zwick2001c
M. B. Zwick, M. Wang, P. Poignard, G. Stiegler, H. Katinger, D. R. Burton, and P. W. Parren. Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J. Virol., 75(24):12198--208, Dec 2001. URL: http://jvi.asm.org/cgi/content/full/75/24/12198. PubMed ID: 11711611.
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Zwick2003a
Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015.
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Sengupta2023
Srona Sengupta, Josephine Zhang, Madison C. Reed, Jeanna Yu, Aeryon Kim, Tatiana N. Boronina, Nathan L. Board, James O. Wrabl, Kevin Shenderov, Robin A. Welsh, Weiming Yang, Andrew E. Timmons, Rebecca Hoh, Robert N. Cole, Steven G. Deeks, Janet D. Siliciano, Robert F. Siliciano, and Scheherazade Sadegh-Nasseri. A cell-free antigen processing system informs HIV-1 epitope selection and vaccine design. J Exp Med, 220(7):e20221654 doi, Jul 2023. PubMed ID: 37058141
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Displaying record number 625
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Vaccine Details
Notes
Showing 14 of
14 notes.
-
ICR39.13: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs.
Holl2006
(neutralization, dendritic cells)
-
ICR 39.13g: UK Medical Research Council AIDS reagent: ARP390.
-
ICR 39.13g: Called ARP390/391, but no such entry was found at the UK Medical Research Council AIDS reagent web site: Herpesvirus saimiri-immortalized CD4+ T lymphocytes (HVS T cells) were used to isolate virus and perform HIV-1 neutralization assays, and compared with a standard PBMC protocol -- neutralization sensitivities to a panel of MAbs and to homologous or heterologous plasma/sera were similar for HVS T cells (CN-2 cells) and PBMCs.
Vella2002
-
ICR 39.13g: The most variable amino acids in the V3 loop were replaced with serines to make the immunodominant V3 loop less immunogenic -- these changes did not affect the ability of sCD4 or MAbs to V1/V2, C1 and C4 to bind -- ICR 39.13g was not affected by V3 serine substitutions -- mice injected with serine substituted gp120 had a reduced response relative to wildtype, and no enhanced immunogenicity of conserved regions.
Peet1998
-
ICR 39.13g: Variants of LAI have differing neutralization susceptibility to 39.13g.
Klasse1996
-
ICR 39.13g: Post-attachment neutralization mechanism, in contrast to MAb 39.3b.
Armstrong1996
-
ICR 39.13g: Called 39.13g Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
-
ICR 39.13g: The gp41 mutation 582(Ala to Thr) results in conformational changes in gp120 that confer neutralization resistance to a class of conformation sensitive neutralizing MAbs -- ICR 39.13g required moderately higher concentrations to neutralize the mutant than wild type.
Klasse1993b
-
ICR 39.13g: Kinetics of neutralization studied -- no lag for 39.3b, while ICR 39.13g and ICR 41.1i have lags of 5 and 15 min respectively -- mediates neutralization with 2.3 molecules of IgG.
McLain1994
-
ICR 39.13g: Strongly inhibits CD4 inducible MAb 48d.
Thali1993
-
ICR 39.13g: Conformational, does not bind denatured gp120 -- weak neutralization of IIIB -- strong inhibition of HIV+ human sera binding to IIIB gp120.
Moore1993a
-
ICR 39.13g: Neutralization activity against HXB10, RF, SF-2 and MN strains of HIV-1.
McKeating1993a
-
ICR 39.13g: Binds to a conformational epitope involved in CD4 binding -- exerts a synergistic effect in combination with V3 directed MAbs.
McKeating1992a
-
ICR 39.13g: Cross-competes with MAbs ICR 39.3b and 15e.
Cordell1991
References
Showing 15 of
15 references.
Isolation Paper
Cordell1991
J. Cordell, J. P. Moore, C. J. Dean, P. J. Klasse, R. A. Weiss, and J. A. McKeating. Rat Monoclonal Antibodies to Nonoverlapping Epitopes of Human Immunodeficiency Virus Type I gp120 Block CD4 Binding In Vitro. Virology, 185:72-79, 1991. PubMed ID: 1718090.
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McKeating1992a
J. A. McKeating, J. Cordell, C. J. Dean, and P. Balfe. Synergistic Interaction between Ligands Binding to the CD4 Binding Site and V3 Domain of Human Immunodeficiency Virus Type I gp120. Virology, 191:732-742, 1992. PubMed ID: 1280382.
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McKeating1992b
J. A. McKeating, M. Thali, C. Furman, S. Karwowska, M. K. Gorny, J. Cordell, S. Zolla-Pazner, J. Sodroski, and R. A. Weiss. Amino Acid Residues of the Human Immunodeficiency Virus Type 1 gp120 Critical for the Binding of Rat and Human Neutralizing Antibodies That Block the gp120-sCD4 Interaction. Virology, 190:134-142, 1992. PubMed ID: 1382339.
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McKeating1993a
J. A. McKeating, C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, S. C. Kayman, Z. Wu, A. Pinter, C. Dean, J. Sodroski, and R. A. Weiss. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol., 67:4932-4944, 1993. Substitutions in the V2 loop can result in complete dissociation of gp120 and gp41, suggesting alterations in V2 can affect subunit assembly. Other substitutions allowed gp120-gp41 association and expression, but inhibited viral entry or syncytia. Binding of some neutralizing MAbs was altered by V2 substitutions. For MAb CRA-4, changes at residues 191/192/193 (YSL/GSS), and for 11/68b, changes at residues 183/184 (PI/SG), within V2, and for both MAbs a position 435 (Y/H) change in C4, abrogate binding. These MAbs can bind to V1 and V2 domains in the absence of C4 domain, so the C4 substitution probably results in conformational change. PubMed ID: 7687306.
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Moore1993a
J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308.
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Thali1993
M. Thali, J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski. Characterization of Conserved Human Immunodeficiency Virus Type 1 gp120 Neutralization Epitopes Exposed upon gp120-CD4 Binding. J. Virol., 67:3978-3988, 1993. Five regions are likely to contribute to the 48d and 17b discontinuous epitopes, either directly or through local conformational effects: the hydrophobic ring-like structure formed by the disulfide bond that links C3 and C4, the base of the stem-loop that contains V1 and V2, and the hydrophobic region in C2 from Arg 252 to Asp 262. Additionally changes in Glu 370, and Met 475 in C5, affected binding and neutralization. The hydrophobic character of these critical regions is consistent with the limited exposure on gp120 prior to CD4 binding. PubMed ID: 7685405.
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Klasse1993b
P. Klasse, J. A. McKeating, M. Schutten, M. S. Reitz, Jr., and M. Robert-Guroff. An Immune-Selected Point Mutation in the Transmembrane Protein of Human Immunodeficiency Virus Type 1 (HXB2-Env:Ala 582(--> Thr)) Decreases Viral Neutralization by Monoclonal Antibodies to the CD4-Binding Site. Virology, 196:332-337, 1993. PubMed ID: 8356803.
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McLain1994
L. McLain and N. J. Dimmock. Single- and Multi-Hit Kinetics of Immunoglobulin G Neutralization of Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies. J. Gen. Virol., 75:1457-1460, 1994. PubMed ID: 8207410.
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Beretta1994
A. Beretta and A.G. Dalgleish. B-Cell Epitopes. AIDS, 8(suppl 1):S133-S145, 1994.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Armstrong1996
S. J. Armstrong and N. J. Dimmock. Varying temperature-dependence of post-attachment neutralization of human immunodeficiency virus type 1 by monoclonal antibodies to gp120: identification of a very early fusion-independent event as a neutralization target. J. Gen. Virol., 77:1397-1402, 1996. PubMed ID: 8757979.
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Klasse1996
P. J. Klasse and Q. J. Sattentau. Altered CD4 Interactions of HIV Type 1 LAI Variants Selected for the Capacity to Induce Membrane Fusion in the Presence of a Monoclonal Antibody to Domain 2 of CD4. AIDS Res. Hum. Retroviruses, 12:1015-1021, 1996. PubMed ID: 8827217.
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Peet1998
N. M. Peet, J. A. McKeating, J. B. de Souza, I. M. Roitt, P. J. Delves, and T. Lund. The Effect of Low-Profile Serine Substitutions in the V3 Loop of HIV-1. Virology, 251:59-70, 1998. PubMed ID: 9813203.
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Vella2002
Cherelyn Vella, Natalie N. Zheng, Philippa Easterbrook, and Rod S. Daniels. Herpesvirus saimiri-Immortalized Human Lymphocytes: Novel Hosts for Analyzing HIV Type 1 in Vitro Neutralization. AIDS Res. Hum. Retroviruses, 18(13):933-946, 1 Sep 2002. PubMed ID: 12230936.
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Holl2006
Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957.
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Displaying record number 627
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MAb ID |
15e (1.5e, 1.5E, 15E, N70-1.5e) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
James Robinson, Tulane University, LA, and David Ho, ADARC, NY, NY |
Epitope |
(Discontinuous epitope)
|
Ab Type |
gp120 CD4bs |
Neutralizing |
L View neutralization details |
Species
(Isotype)
|
human(IgG1κ) |
Patient |
N70 |
Immunogen |
HIV-1 infection |
Keywords |
adjuvant comparison, antibody binding site, antibody generation, antibody interactions, antibody sequence, assay or method development, binding affinity, brain/CSF, co-receptor, effector function, enhancing activity, glycosylation, HAART, ART, kinetics, neutralization, review, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity |
Notes
Showing 86 of
86 notes.
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15e: The first cryo-EM structure of a cross-linked vaccine antigen was solved. The 4.2 Å structure of HIV-1 BG505 SOSIP soluble recombinant Env in complex with a bNAb PGV04 Fab fragment revealed how cross-linking affects key properties of the trimer. SOSIP and GLA-SOSIP trimers were compared for antigenicity by ELISA, using a large panel of mAbs previously determined to react with BG505 Env. Non-NAbs like 15e globally lost reactivity (7-fold median loss of binding), likely because of covalent stabilization of the cross-linked ‘closed’ form of the GLA-SOSIP trimer that binds non-NAbs weakly or not at all. V3-specific non-NAbs showed 2.1–3.3-fold reduced binding. Three autologous rabbit monoclonal NAbs to the N241/N289 ‘glycan-hole’ surface, showed a median ˜1.5-fold reduction in binding. V3 non-NAb 4025 showed residual binding to the GLA-SOSIP trimer. By contrast, bNAbs broadly retained reactivity significantly better than non-NAbs, with exception of PGT145 (3.3-5.3 fold loss of binding in ELISA and SPR).
Schiffner2018
(vaccine antigen design, binding affinity, structure)
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1.5E: LANL database note: This monoclonal antibody is a CHAVI reagent (http://chavi.org/); Species: human; Category: CD4 BS; Contact person: James Robinson
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15e: This study investigated the ability of native, membrane-expressed JR-FL Env trimers to elicit NAbs. Rabbits were immunized with virus-like particles (VLPs) expressing trimers (trimer VLP sera) and DNA expressing native Env trimer, followed by a protein boost (DNA trimer sera). N197 glycan- and residue 230- removal conferred sensitivity to Trimer VLP sera and DNA trimer sera respectively, showing for the first time that strain-specific holes in the "glycan fence" can allow the development of tier 2 NAbs to native spikes. All 3 sera neutralized via quaternary epitopes and exploited natural gaps in the glycan defenses of the second conserved region of JR-FL gp120. 4E10 was used as a reference Ab.
Crooks2015
(glycosylation, neutralization)
-
15e: A new trimeric immunogen, BG505 SOSIP.664 gp140, was developed that bound and activated most known neutralizing antibodies but generally did not bind antibodies lacking neuralizing activity. This highly stable immunogen mimics the Env spike of subtype A transmitted/founder (T/F) HIV-1 strain, BG505. Anti-CD4bs non-NAb 15e did not neutralize BG505.T332N, the pseudoviral equivalent of the immunogen BG505 SOSIP.664 gp140, and did not recognize or bind the immunogen either.
Sanders2013
(assay or method development, neutralization, binding affinity)
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15e: The neutralization profile of 1F7, a human CD4bs mAb, is reported and compared to other bnNAbs. 1F7 neutralization breadth was superior to that of 15e. 15e did not recognize Env JR-FL trimers, but 15e mutants, N262A and P470T promoted binding.
Gach2013
(neutralization)
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15e: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 15e is discussed as the CD4bs-targeting, neutralizing anti-gp120 mAb exhibiting ADCC activity and having a discontinuous epitope.
Pollara2013
(effector function, review)
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Lists 7 mAbs derived from patient N70: 15E, 1.9B, 2.3A, 2.3B, 2.1H, F91, 1.7B.
Robinson1992
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Describes the generation of 1.5e IgG1 mAb from patient N70. The antibody reacted with multiple strains, suggesting a conserved epitope.
Robinson1990c
(antibody generation)
-
1.5E: This study reports the isolation of a panel of Env vaccine elicited CD4bs-directed macaque mAbs and genetic and functional features that distinguish these Abs from CD4bs MAbs produced during chronic HIV-1 infection. 1.5E was used as a Non-bNAb which was similar in function to non human primates mAbs.
Sundling2012
(vaccine-induced immune responses)
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15E: Different adjuvants, including Freund's adjuvant (FCA/FIA), MF59, Carbopol-971P and 974P were compared on their ability to elicit antibody responses in rabbits. Combination of Carbopol-971P and MF59 induced potent adjuvant activity with significantly higher titer nAbs than FCA/FIA. There was no difference in binding of this MAb to gp140 SF162 with FIA, MF59, C974 and C974+MF59 adjuvants, but there was 3-fold decrease of antigenicity with C971 and C971+MF59 as compared to the unadjuvanted sample.
Lai2012
(adjuvant comparison)
-
15e: The goal of this study was to improve the humoral response to HIV-1 by targeting trimeric Env gp140 to B cells. The gp140 was fused to a proliferation-inducing ligand (APRIL), B cell activation factor (BAFF) and CD40 ligand (CD40L). These fusion proteins increased the expression of activation-induced-cytidine deaminase (AID) responsible for somatic hypermutation, Ab affinity maturation, and Ab class switching. The Env-APRIL induced high anti-Env responses against tier1 viruses. 15e was used in BN-PAGE trimer shift assay to deplete the trimers and was not as effective as b12 and 2F5.
Melchers2012
(neutralization)
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15e: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared. Binding to E168K+ N189A WT VLPs was stronger than binding to the parent WT VLPs, uncleaved VLPs. There was no significant correlation between E168K+N189A WT VLP binding and 15e neutralization, while trimer VLP ELISA binding and neutralization exhibited a significant correlation. BN-PAGE shifts using digested E168K + N189A WT trimer VLPs exhibited prominence compared to WT VLPs.
Tong2012
(neutralization, binding affinity)
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15e: Crystal structures of gp120 and gp41 in complex with CD4 and/or MAbs 17b, 48d, b12, b13, 412d, X5, 211C, C11, 15e, m6, m9 and F105 were used to determine the structure and the mobility of the gp41-interactive region of gp120. Elements determined to maintain the gp120-gp41 interaction were the gp120 termini and a newly described invariant 7-stranded β-sandwich. Structurally plastic elements of gp120 responsible for the various gp120 conformation changes due to receptor- or Ab-binding were structured into 3 layers, with the V1/V2 loops emanating from layer 2 and the highly glycosylated outer domain from layer 3.
Pancera2010a
(antibody binding site, structure)
-
15e: A mathematical framework is designed to determine the number of Abs required to neutralize a single trimer called the stoichiometry of trimer neutralization (N). 15 different virus antibody combinations divided into five groups based on antibody binding sites were used in the designed model. 15e was classified into CD4BS group as it interferes with CD4 binding site. The number of 15e Abs to neutralize a single trimer was determined to equal 1.
Magnus2010
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15e: Unlike the MPER MAbs tested, 15e did not show any Env-independent virus capture. MAb competition assays revealed that 15e did not compete with b12 for capture of virus, but it did compete with b6, indicating that it binds to uncleaved Envs.
Leaman2010
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15e: A set of Env variants with deletions in V1/V2 was constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Sensitivity of the evolved ΔV1V2 viruses was evaluated to study accessibility of their neutralization epitopes. 15e bound better to the ΔV1V2 variants than to the full-length trimer, indicating better exposure of 15e epitope when the V1V2 domain is removed.
Bontjer2010
(binding affinity)
-
15e: Both parent and GnTI (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps) viruses were resistant to neutralization by 15e, while the N301Q mutant virus was markedly more susceptible to neutralization by 15e. This suggests that removal of a key glycan had a greater effect on exposing the 15e epitope, than replacing complex glycans with smaller ones did. 15e did not complex with, nor did it deplete, Env trimers on blue native polyacrylamide gel electrophoresis (BN-PAGE), correlating with its inability to neutralize.
Binley2010
(glycosylation, neutralization, binding affinity)
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1.5E: A panel of 109 HIV-1 pseudoviruses was assessed for neutralization sensitivities to 1.5E MAb and patient plasma pools from genetically diverse HIV-1 positive samples. Clustering analyses revealed that the 109 viruses could be divided to 4 sub-groups, based on their neutralization sensitivity to the plasma pools: very high (Tier 1A), above-average (Tier 1B), moderate (Tier 2), and low (Tier 3) sensitivity. 2 Tier 1A, 5 Tier 1B, 1 Tier 2 but no Tier 3 viruses were found to be sensitive to neutralization by 1.5E.
Seaman2010
(neutralization)
-
1.5E: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 did not show binding to 1.5E.
Wu2010
(binding affinity)
-
15e: Broadly neutralizing sera from elite neutralizers exhibited significant sensitivities to mutations I165A, N332A, and N160K. 15e binding was tested for pseudoviruses with the mutations relative to the WT. 15e binding was not significantly affected by the three mutations.
Walker2010
(binding affinity)
-
15e: OD (GSL)(δβ20-21)(hCD4-TM) glycoprotein variant was constructed by eliminating V1 and V2 regions, truncating V3, and deleting cleavage, fusion, and interhelical domains from Env derivatives from R3A TA1 virus. In addition, the variant was membrane-anchored, the β20-β21 hairpin was truncated, and the central 20 amino acids of the V3 loop were replaced with a basic hexapeptide. Although this variant showed increased binding to b12 and 2G12, it did not bind to 15e.
Wu2009a
(binding affinity)
-
15e: Subtype A gp140 SOSIP trimers were recognized by 15e. Sera from rabbits immunized with SOSIP gp140 was used in virus competition assay. 15e was able to capture the virus effectively.
Kang2009
-
15e: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:4-39*02, IGHD:2-8, D-RF:1, IGHJ:6. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner.
Gorny2009
(antibody sequence)
-
15e: 15e neutralized Tier 1 viruses but not Tier 2 viruses. Crystal structure of F105 in complex with gp120 revealed small differences in recognition of gp120 by F105, where all four strands of the bridging sheet were displaced to uncover a hydrophobic region which served for F105 binding. A monomeric disulfide gp120 variant was not bound by 15e, suggesting that 15e relies on access to the hydrophobic surface for binding. Structure analyses revealed that 15e, and other CD4BS Abs that access this hydrophobic region, induce conformation changes in gp120 that are poorly compatible with functional viral spike. 15e was not able to bind to cleavage-defective envelope glycoproteins.
Chen2009
(neutralization, kinetics, binding affinity)
-
15e: This report investigated whether mannose removal alters gp120 immunogenicity in mice. Approximately 55 mannose residues were removed from gp120 by mannosidase digestion creating D-gp120 for immunization. 15e was able to bind to D-gp120 comparably as to the untreated gp120, indicating that the mannosidase digestion did not affect the antigenicity of gp120.
Banerjee2009
(binding affinity)
-
15e: Molecules designed to eliminate binding by 15e while preserving epitopes of other neutralizing Abs are discussed.
Lin2007
(review)
-
15e: This review summarizes 15e Ab epitope, properties and neutralization activity.
Kramer2007
(review)
-
15e: Sera from gp120 DNA prime-protein boost immunized rabbits competed for binding to 15e while sera from rabbits immunized with protein-only regimen did not, indicating elicitation of 15e-like Abs in animals immunized with DNA prime-protein boost regimen. Competitive virus capture assay also revealed higher titers of 15e Abs in animals immunized with DNA prime-protein boost than in protein-only immunized animals.
Vaine2008
(vaccine antigen design)
-
15e: Five amino acids in the gp41 N-terminal region that promote gp140 trimerization (I535, Q543, S553, K567 and R588) were considered. Their influence on the function and antigenic properties of JR-FL Env expressed on the surfaces of pseudoviruses and Env-transfected cells was studied. Various non-neutralizing antibodies bind less strongly to the Env mutant, but neutralizing antibody binding is unaffected. 15e captured significantly fewer mutant pseudovirions than wild type, and 15e failed to inhibit infection by either pseudovirus.
Dey2008
(binding affinity)
-
15e: Molecular mechanism of neutralization by MPER antibodies, 2F5 and 4E10, was studied using preparations of trimeric HIV-1 Env protein in the prefusion, the prehairpin intermediate and postfusion conformations. MAb 15e was used to analyze antigenic properties of construct 92UG-gp140-Fd, derived from isolate 92UG037.8 and stabilized by a C-terminal foldon tag. 92UG-gp140-Fd failed to bind 15e, despite high affinity of 15e for 92UG-gp120 core.
Frey2008
(binding affinity)
-
15e: Most of the sera from guinea pigs immunized with gp120 protein or with three types of VLPs containing disulfide-shackled functional trimers (SOS-VLP), uncleaved nonfunctional Env (UNC-VLP), naked VLP bearing no Env, weakly or ineffectively inhibited virus capture compared to 15e Ab.
Crooks2007
(neutralization)
-
15e: Interactions of this Ab with gp120 monomer and two cleavage-defective gp140 trimers were studied. It was shown that 15e recognized the soluble monomer and trimers much more efficiently than the GA-treated (cross-linked) monomers and trimers, indicating that the 15e epitope was affected by cross-linking. This Ab was associated with a large entropy change upon gp120 binding. 15e successfully recognized untreated but not cross-linked proteins expressed on cell surfaces indicating existence of multiple conformational states of gp120 on cell surface. This Ab was shown to have a kinetic disadvantage as it bound to gp120 much slower than the highly neutralizing Abs 2G12 and IgG1b12.
Yuan2006
(antibody binding site, antibody interactions, kinetics, binding affinity)
-
15e: This Ab was used to determine the degree to which fixation of gp120 in its CD4-bound conformation restricts antigenic recognition. 15e was not able to bind well to the stabilized gp120.
Zhou2007
(antibody binding site, binding affinity)
-
15e: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed.
Srivastava2005
(antibody binding site, neutralization, vaccine antigen design, review)
-
15e: Ab neutralization of viruses with mixtures of neutralization-sensitive and neutralization-resistant envelope glycoproteins was measured. It was concluded that binding of a single Ab molecule is sufficient to inactivate function of an HIV-1 glycoprotein trimer. The inhibitory effect of the Ab was similar for neutralization-resistant and -sensitive viruses indicating that the major determinant of neutralization potency of an Ab is the efficiency with which it binds to the trimer. It was also indicated that each functional trimer on the virus surface supports HIV-1 entry independently, meaning that every trimer on the viral surface must be bound by an Ab for neutralization of the virus to be achieved.
Yang2005b
(neutralization)
-
15e: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1.
McCann2005
(antibody binding site, review)
-
15e: MAbs were investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. 15e did not neutralize in standard format.
Crooks2005
(assay or method development, neutralization)
-
15e: A reverse capture assay was developed to assess what kind of human MAbs were produced in EBV B-cell transformation assays performed on PBMC sampled at different time-points from three HIV-1 infected patients on HAART. The reverse capture assay was validated by the solid phase MAbs that could not capture biotin-MAbs of the same or overlapping specificity when reacted with patient virus envelope glycoproteins preincubated with or without sCD4. Reverse capture assay showed that the produced Abs from the patients did not block binding of biotin-labeled 15e in early samples from the patients, indicating no detection of CD4bs Abs. CD4bs Abs were only detected in significant numbers in one patient at week 168 after diagnosis.
Robinson2005
(assay or method development, HAART, ART)
-
15e: Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). 15e-like Abs were generated in the SHIV-infected macaque, and may have been present at very low titers in macaques immunized with ΔV2gp140 and ΔV2ΔV3gp140. No 15e Abs were detected in the sera from F162gp140 immunized animals.
Derby2006
(antibody binding site)
-
15e: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120, including 15e.
Pantophlet2004
(vaccine antigen design)
-
15e: A set of HIV-1 chimeras that altered V3 net charge and glycosylation patterns in V1V2 and V3, involving inserting V1V2 loops from a late stage primary isolate taken after the R5 to X4 switch, were studied with regard to phenotype, co-receptor usage, and MAb neutralization. The loops were cloned into a HXB2 envelope with a LAI viral backbone. It was observed that the addition of the late-stage isolate V1V2 region and the loss of V3-linked glycosylation site in the context of high positive charge gave an X4 phenotype. R5X4, R5, and X4 viruses were generated, and sCD4, 2G12 and b12 neutralization resistance patterns were modified by addition of the late stage V1V2, glycosylation changes, and charge in concert, while neutralization by 2F5 was unaffected. 15e, 17b, and 48d could not neutralize any of the variants tested.
Nabatov2004
(antibody binding site, co-receptor)
-
15e: This review summarizes MAbs directed to HIV-1 Env. There are 51 CD4BS MAbs and Fabs in the database; most, like this MAb, neutralize TCLA strains only.
Gorny2003
(review)
-
15e: A gp120 molecule was designed to focus the immune response onto the IgG1b12 epitope. Ala substitutions that enhance the binding of IgG1b12 and reduce the binding of non-neutralizing MAbs were combined with additional N-linked glycosylation site sequons inhibiting binding of non-neutralizing MAbs; b12 bound to the mutated gp120. C1 and C5 were also removed, but this compromised b12 binding.
Pantophlet2003b
(vaccine antigen design)
-
15e: scFv 4KG5 reacts with a conformational epitope that is formed by the V1V2 and V3 loops and the bridging sheet (C4) region of gp120 and is influenced by carbohydrates. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120 JRFL. MAbs to the following regions diminished 4KG5 binding: V2 loop, V3 loop, V3-C4 region, CD4BS. MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected by these loops. This was one of the CD4BS MAbs used.
Zwick2003a
(antibody interactions)
-
15e: Called 1.5e. Thermodynamics of binding to gp120 was measured using isothermal titration calorimetry for sCD4, 17b, b12, 48d, F105, 2G12 and C11 to intact YU2 and the HXBc2 core. The free energy of binding was similar. Enthalpy and entropy changes were divergent, but compensated. Not only CD4 but MAb ligands induced thermodynamic changes in gp120 that were independent of whether the core or the full gp120 protein was used. Non-neutralizing CD4BS and CD4i MAbs (17b, 48d, 1.5e, b6, F105 and F91) had large entropy contributions to free energy (mean: 26.1 kcal/mol) of binding to the gp120 monomer, but the potent CD4BS neutralizing MAb b6 had a much smaller value of 5.7 kcal/mol, The high values suggest surface burial or protein folding an ordering of amino acids. These results suggest that while the trimeric Env complex has four surfaces, a non-neutralizing face (occluded on the oligomer), a variable face, a neutralizing face and a silent face (protected by carbohydrate masking), gp120 monomers further protect receptor binding sites by conformational or entropic masking, requiring a large energy handicap for Ab binding not faced by other anti-gp120 Abs.
Kwong2002
(antibody binding site)
-
15e: This paper shows that binding of CD4BS MAbs to Env blocks the conformational shift that allows co-receptor CCR5 binding and CD4-independent mediated cell fusion. CD4BS MAbs F105, 15e, and IgG1b12 as well as their Fab fragments inhibited CD4-independent binding of the V1/V2 loop-deleted gp120 glycoproteins of R5 HIV-1 isolates ADA, YU2 and JRFL and to CCR5 in a concentration dependent manner.
Raja2003
(co-receptor)
-
15e: UK Medical Research Council AIDS reagent: ARP3016.
-
15e: Alanine scanning mutagenesis was used to compare substitutions that affected anti-CD4BS NAb b12 -- rec gp120s were engineered to contain combinations of Alanine substitutions that enhanced b12 binding, and while binding of b12 to these gp120 monomers was generally maintained or increased, binding by five non-neutralizing anti-CD4bs MAbs (b3, b6, F105, 15e, and F91) was reduced or completely abolished.
Pantophlet2003
(antibody binding site)
-
15e: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain.
Zhang2002
(antibody binding site)
-
15e: A series of mutational changes were introduced into the YU2 gp120 that favored different conformations -- 375 S/W seems to favor a conformation of gp120 closer to the CD4-bound state, and is readily bound by sCD4 and CD4i MAbs (17b, 48d, 49e, 21c and 23e) but binding of anti-CD4BS MAbs (F105, 15e, IgG1b12, 21h and F91 was markedly reduced -- IgG1b12 failed to neutralize this mutant, while neutralization by 2G12 was enhanced -- 2F5 did not neutralize either WT or mutant, probably due to polymorphism in the YU2 epitope -- another mutant, 423 I/P, disrupted the gp120 bridging sheet, favored a different conformation and did not bind CD4, CCR5, or CD4i antibodies, but did bind to CD4BS MAbs.
Xiang2002
(antibody binding site)
-
15e: Mutations in two glycosylation sites in the V2 region of HIV-1 ADA at positions 190 and 197 (187 DNTSYRLINCNTS 199) cause the virus to become CD4-independent and able to enter cells through CCR5 alone -- these same mutations tended to increase the neutralization sensitivity of the virus, including to 15e.
Kolchinsky2001
(antibody binding site)
-
15e: Six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes.
Park2000
(antibody binding site)
-
15e: Called 1.5e -- the HIV-1 virus YU2 entry can be enhanced by MAbs binding to the CD4BS, V3 loop, and CD4i epitopes -- the activation for this enhanced entry state could be conferred on HxB2 by introducing the YU2 V3 loop, or the YU2 V3 and V1/V2 loops -- a similar effect is observed by sub-neutralizing concentrations of sCD4 and the effect is dependent of CCR5 -- 1.5e enhances and does not neutralize YU2 env even at 50 ug/ml.
Sullivan1998b
(antibody binding site)
-
15e: CD4BS MAbs 15e, 21h, and F91 bind with even lower affinity than 205-43-1 and 205-42-15 to JRFL oligomer.
Fouts1998
(antibody binding site)
-
15e: No detectable neutralizing activity among primary isolates with different co-receptor usage -- some neutralization of TCLA strains.
Trkola1998
(variant cross-reactivity)
-
15e: Competes with CG-10 binding, a MAb raised against a gp120 CD4 complex, this was probably due to the disruption of CD4-gp120 by 15e.
Sullivan1998
(antibody binding site, antibody interactions)
-
15e: A panel of MAbs were shown to bind with similar or greater affinity and similar competition profiles to a deglycosylated or variable loop deleted core gp120 protein (Delta V1, V2, and V3), thus such a core protein produces a structure closely approximating full length folded monomer -- CD4BS MAbs 15e, F91 and IgG1b12 bound better to the deleted protein than to wild type.
Binley1998
(antibody binding site)
-
15e: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope.
Parren1998
(antibody binding site)
-
15e: Summary of the implications of the crystal structure of the core of gp120 bound to CD4 and 17b with what is known about mutations that reduce NAb binding -- probable mechanism of neutralization by CD4BS Ab is direct interference with CD4 binding.
Wyatt1998
(structure)
-
15e: Neutralizes TCLA strains, but not primary isolates.
Parren1997
-
15e: Called 1.5E -- Binds to 7/7 isolates from breakthrough cases from a MN gp120 vaccine trial.
Berman1997
(variant cross-reactivity)
-
15e: Does not bind to HXBc2 gp120 if the 19 C-term amino acids, in conjunction with C1 positions 31-93, are deleted.
Wyatt1997
(antibody binding site)
-
15e: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env -- 15e could only achieve 50% neutralization, but could act synergistically with anti-V3 MAb 694/98-D to achieve 90%.
Li1997
(antibody interactions)
-
15e: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 15e bound monomer, did not bind oligomer or neutralize JRFL.
Fouts1997
(antibody binding site)
-
15e: 15e is V H4 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals.
Wisnewski1996
(antibody sequence)
-
15e: Neutralizes HIV-1 LAI less potently than V3 specific MAbs.
McDougal1996
-
15e: Inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study.
Trkola1996b
(antibody binding site)
-
15e: Anti-CD4BS MAbs 15e, 21h, and IgG1b12 did not cause gp120 dissociation from virus, or exposure of the gp41 epitope of MAb 50-69, in contrast to CD4i MAb 48d and anti-V3 neutralizing MAbs.
Poignard1996b
(antibody interactions)
-
15e: gp120 binding enhanced by anti-V3 MAb 5G11 and anti-V2 MAb G3-136 -- binding inhibited by other CD4 binding site MAbs, antibodies that bind to gp120 only when CD4 is bound, and CD4-IgG.
Moore1996
(antibody interactions)
-
15e: Called 1.5e -- Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
(variant cross-reactivity)
-
15e: The V4 and V5 domains are essential for 1.5e binding, in contrast to the V1, V2, and V3 loops.
Lee1995
(antibody binding site)
-
15e: Binds with higher affinity to monomer than to oligomer, moderate association rate.
Sattentau1995a
(antibody binding site)
-
15e: Cross-reactive with gp120 proteins from clades B and D, less so with A and C, and not reactive with clade E and F.
Moore1994b
(subtype comparisons)
-
15e: MAbs against the glycosphingolipid GalCer block HIV infection of normally susceptible CD4 negative cells from the brain and colon -- anti-CD4 MAbs moderately inhibit gp120 binding to GalCer, possibly through steric hindrance -- binding of GalCer to gp120 inhibited but did not completely block 15e binding.
Cook1994
(antibody binding site, brain/CSF)
-
15e: A mutation in gp41, 582 A/T, confers resistance to neutralization (also confers resistance to MAbs F105, 48d, 21h and 17b)..
Thali1994
(antibody binding site)
-
15e: Heavy chain is V HIV, V2-1 -- light chain is V_kappaI, Hum01/012. Compared to 21h and F105.
Bagley1994
(antibody sequence)
-
15e: Called 15E -- a neutralization escape mutant (HXB2 A281V) was selected by growth of HXB2 in the presence of broadly neutralizing sera -- 15E neutralization was not affected by this mutation.
Watkins1993
(antibody binding site)
-
15e: Binding to Delta V1/2 and Delta V1/2/3 mutant glycoproteins is greater than binding to wildtype gp120.
Wyatt1993
(antibody binding site)
-
15e: Conformational, does not bind denatured gp120 -- neutralizes IIIB -- reactive with SF-2 gp120 -- strong inhibition of HIV+ human sera binding to IIIB gp120.
Moore1993a
(antibody binding site, variant cross-reactivity)
-
15e: Called N70-1.5e -- does not enhance infection of HIV-1 IIIB and MN.
Thali1992a
(enhancing activity)
-
15e: Amino acid substitutions in HXB2 that strongly inhibit binding, similar to Ho1992, some additional, 88, 102, 117, 113, 257, 368, 370, 421, 427, 457, 470, 480 Thali1992a.
Ho1992,Thali1992a
(antibody binding site)
-
15e: Precipitation of Delta 297-329 env glycoprotein, with a deleted V3 loop, is much more efficient that precipitation of wild type.
Wyatt1992
(antibody binding site)
-
15e: gp120 mutants that affect 15e epitope binding: 113, 257, 368, 370, 421, 427, 475 -- four of these coincide with amino acids important for the CD4 binding domain.
Ho1992
(antibody binding site)
-
15e: Binds to gp120 of HIV-1 IIIB, but not RF -- mediates ADCC -- deletion of the V3 loop from gp120 does not alter ADCC activity.
Koup1991
(effector function, variant cross-reactivity)
-
15e: Cross-competes with MAbs ICR 39.13g and ICR 39.3b.
Cordell1991
(antibody interactions)
-
15e: Broadly neutralizing, binds multiple strains, competes with CD4 for gp120 binding, DTT reduction of env abrogates binding -- more potent blocking of gp120-sCD4 binding than MAbs G3-536 and G3-537..
Ho1991a
(adjuvant comparison, variant cross-reactivity)
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Isolation Paper
Robinson1990c
J. E. Robinson, D. Holton, S. Pacheco-Morell, J. Liu, and H. McMurdo. Identification of Conserved and Variable Epitopes of Human Immunodeficiency Virus Type-1 (HIV-1) gp120 by Human Monoclonal Antibodies Produced by EBV Transformed Cell Lines. AIDS Res. Hum. Retroviruses, 6:567-579, 1990. PubMed ID: 1694449.
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Bagley1994
J. Bagley, P. J. Dillon, C. Rosen, J. Robinson, J. Sodroski, and W. A. Marasco. Structural Characterization of Broadly Neutralizing Human Monoclonal Antibodies Against the CD4 Binding Site of HIV-1 gp120. Mol. Immunol., 31(15):1149-1160, 1994. This paper is a detailed study of the V-D-J heavy chain usage and V-J light chain usage for the three monoclonals that bind to the HIV-1 envelope CD4 binding site: F105, 15e and 21h. Different germline genes were used, and there was evidence for antigen-drive clonal selection of somatic mutations. Eight positions in the heavy chain and two in the light chain complementarity determining positions were identical in the three Mabs. PubMed ID: 7935503.
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Banerjee2009
Kaustuv Banerjee, Sofija Andjelic, Per Johan Klasse, Yun Kang, Rogier W. Sanders, Elizabeth Michael, Robert J. Durso, Thomas J. Ketas, William C. Olson, and John P. Moore. Enzymatic Removal of Mannose Moieties Can Increase the Immune Response to HIV-1 gp120 In Vivo. Virology, 389(1-2):108-121, 20 Jun 2009. PubMed ID: 19410272.
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Berman1997
P. W. Berman, A. M. Gray, T. Wrin, J. C. Vennari, D. J. Eastman, G. R. Nakamura, D. P. Francis, G. Gorse, and D. H. Schwartz. Genetic and Immunologic Characterization of Viruses Infecting MN-rgp120-Vaccinated Volunteers. J. Infect. Dis., 176:384-397, 1997. PubMed ID: 9237703.
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Binley1997
J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287.
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Binley1998
J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908.
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Binley2010
James M Binley, Yih-En Andrew Ban, Emma T. Crooks, Dirk Eggink, Keiko Osawa, William R. Schief, and Rogier W. Sanders. Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization. J. Virol., 84(11):5637-5655, Jun 2010. PubMed ID: 20335257.
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Bontjer2010
Ilja Bontjer, Mark Melchers, Dirk Eggink, Kathryn David, John P. Moore, Ben Berkhout, and Rogier W. Sanders. Stabilized HIV-1 Envelope Glycoprotein Trimers Lacking the V1V2 Domain, Obtained by Virus Evolution. J. Biol. Chem, 285(47):36456-36470, 19 Nov 2010. PubMed ID: 20826824.
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Chen2009
Lei Chen, Young Do Kwon, Tongqing Zhou, Xueling Wu, Sijy O'Dell, Lisa Cavacini, Ann J. Hessell, Marie Pancera, Min Tang, Ling Xu, Zhi-Yong Yang, Mei-Yun Zhang, James Arthos, Dennis R. Burton, Dimiter S. Dimitrov, Gary J. Nabel, Marshall R. Posner, Joseph Sodroski, Richard Wyatt, John R. Mascola, and Peter D. Kwong. Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120. Science, 326(5956):1123-1127, 20 Nov 2009. PubMed ID: 19965434.
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Cook1994
D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533.
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Cordell1991
J. Cordell, J. P. Moore, C. J. Dean, P. J. Klasse, R. A. Weiss, and J. A. McKeating. Rat Monoclonal Antibodies to Nonoverlapping Epitopes of Human Immunodeficiency Virus Type I gp120 Block CD4 Binding In Vitro. Virology, 185:72-79, 1991. PubMed ID: 1718090.
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Crooks2005
Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980.
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Crooks2007
Emma T. Crooks, Penny L. Moore, Michael Franti, Charmagne S. Cayanan, Ping Zhu, Pengfei Jiang, Robbert P. de Vries, Cheryl Wiley, Irina Zharkikh, Norbert Schülke, Kenneth H. Roux, David C. Montefiori, Dennis R. Burton, and James M. Binley. A Comparative Immunogenicity Study of HIV-1 Virus-Like Particles Bearing Various Forms of Envelope Proteins, Particles Bearing no Envelope and Soluble Monomeric gp120. Virology, 366(2):245-262, 30 Sep 2007. PubMed ID: 17580087.
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Crooks2015
Ema T. Crooks, Tommy Tong, Bimal Chakrabarti, Kristin Narayan, Ivelin S. Georgiev, Sergey Menis, Xiaoxing Huang, Daniel Kulp, Keiko Osawa, Janelle Muranaka, Guillaume Stewart-Jones, Joanne Destefano, Sijy O'Dell, Celia LaBranche, James E. Robinson, David C. Montefiori, Krisha McKee, Sean X. Du, Nicole Doria-Rose, Peter D. Kwong, John R. Mascola, Ping Zhu, William R. Schief, Richard T. Wyatt, Robert G. Whalen, and James M. Binley. Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site. PLoS Pathog, 11(5):e1004932, May 2015. PubMed ID: 26023780.
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Derby2006
Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322.
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Dey2008
Antu K. Dey, Kathryn B. David, Neelanjana Ray, Thomas J. Ketas, Per J. Klasse, Robert W. Doms, and John P. Moore. N-Terminal Substitutions in HIV-1 gp41 Reduce the Expression of Non-Trimeric Envelope Glycoproteins on the Virus. Virology, 372(1):187-200, 1 Mar 2008. PubMed ID: 18031785.
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Fouts1997
T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632.
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Fouts1998
T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713.
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Frey2008
Gary Frey, Hanqin Peng, Sophia Rits-Volloch, Marco Morelli, Yifan Cheng, and Bing Chen. A Fusion-Intermediate State of HIV-1 gp41 Targeted by Broadly Neutralizing Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(10):3739-3744, 11 Mar 2008. PubMed ID: 18322015.
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Gach2013
Johannes S. Gach, Heribert Quendler, Tommy Tong, Kristin M. Narayan, Sean X. Du, Robert G. Whalen, James M. Binley, Donald N. Forthal, Pascal Poignard, and Michael B. Zwick. A Human Antibody to the CD4 Binding Site of gp120 Capable of Highly Potent but Sporadic Cross Clade Neutralization of Primary HIV-1. PLoS One, 8(8):e72054, 2013. PubMed ID: 23991039.
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Gorny2003
Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162.
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Gorny2009
Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295.
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Ho1991a
D. D. Ho, J. A. McKeating, X. L. Li, T. Moudgil, E. S. Daar, N.-C. Sun, and J. E. Robinson. Conformational Epitope of gp120 Important in CD4 Binding and Human Immunodeficiency Virus Type 1 Neutralization Identified by a Human Monoclonal Antibody. J. Virol., 65:489-493, 1991. A description of the neutralizing human MAb 15e. It binds to HIV-1 with a broad specificity, and blocks gp120 binding to CD4, and is a discontinuous epitope; DTT reduction of env abrogates binding. PubMed ID: 1702163.
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Ho1992
D. D. Ho, M. S. C. Fung, H. Yoshiyama, Y. Cao, and J. E. Robinson. Discontinuous Epitopes on gp120 Important in HIV-1 Neutralization. AIDS Res. Hum. Retroviruses, 8:1337-1339, 1992. Further description of the human MAb 15e and the murine MAb G3-4. gp120 mutants that affect 15e epitope binding: 113, 257, 368, 370, 421, 427, 475; four of these coincide with amino acids important for the CD4 binding domain. G3-4 is neutralizing and behaves like a discontinuous epitope, and partially blocks sCD4 binding. PubMed ID: 1281654.
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Kang2009
Yun Kenneth Kang, Sofija Andjelic, James M. Binley, Emma T. Crooks, Michael Franti, Sai Prasad N. Iyer, Gerald P. Donovan, Antu K. Dey, Ping Zhu, Kenneth H. Roux, Robert J. Durso, Thomas F. Parsons, Paul J. Maddon, John P. Moore, and William C. Olson. Structural and Immunogenicity Studies of a Cleaved, Stabilized Envelope Trimer Derived from Subtype A HIV-1. Vaccine, 27(37):5120-5132, 13 Aug 2009. PubMed ID: 19567243.
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Kolchinsky2001
P. Kolchinsky, E. Kiprilov, P. Bartley, R. Rubinstein, and J. Sodroski. Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops. J. Virol., 75(7):3435--43, Apr 2001. URL: http://jvi.asm.org/cgi/content/full/75/7/3435. PubMed ID: 11238869.
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Koup1991
R. A. Koup, J. E. Robinson, Q. V. Nguyen, C. A. Pikora, B. Blais, A. Roskey, D. Panicali, and J. L. Sullivan. Antibody-Dependent Cell-Mediated Cytotoxicity Directed by a Human Monoclonal Antibody Reactive with gp120 of HIV-1. AIDS, 5:1309-1314, 1991. PubMed ID: 1722676.
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Kramer2007
Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119.
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Kwong2002
Peter D. Kwong, Michael L. Doyle, David J. Casper, Claudia Cicala, Stephanie A. Leavitt, Shahzad Majeed, Tavis D. Steenbeke, Miro Venturi, Irwin Chaiken, Michael Fung, Hermann Katinger, Paul W. I. H. Parren, James Robinson, Donald Van Ryk, Liping Wang, Dennis R. Burton, Ernesto Freire, Richard Wyatt, Joseph Sodroski, Wayne A. Hendrickson, and James Arthos. HIV-1 Evades Antibody-Mediated Neutralization through Conformational Masking of Receptor-Binding Sites. Nature, 420(6916):678-682, 12 Dec 2002. Comment in Nature. 2002 Dec 12;420(6916):623-4. PubMed ID: 12478295.
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Lai2012
Rachel P. J. Lai, Michael S. Seaman, Paul Tonks, Frank Wegmann, David J. Seilly, Simon D. W. Frost, Celia C. LaBranche, David C. Montefiori, Antu K. Dey, Indresh K. Srivastava, Quentin Sattentau, Susan W. Barnett, and Jonathan L. Heeney. Mixed Adjuvant Formulations Reveal a New Combination That Elicit Antibody Response Comparable to Freund's Adjuvants. PLoS One, 7(4):e35083, 2012. PubMed ID: 22509385.
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Leaman2010
Daniel P. Leaman, Heather Kinkead, and Michael B. Zwick. In-Solution Virus Capture Assay Helps Deconstruct Heterogeneous Antibody Recognition of Human Immunodeficiency Virus Type 1. J. Virol., 84(7):3382-3395, Apr 2010. PubMed ID: 20089658.
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Lee1995
C.-N. Lee, J. Robinson, G. Mazzara, Y.-L. Cheng, M. Essex, and T.-H. Lee. Contribution of hypervariable domains to the conformation of a broadly neutralizing glycoprotein 120 epitope. AIDS Res. Hum. Retroviruses, 11:777-781, 1995. Deletion of the V4 or V5 domains, in contrast to the V1, V2 and V3 domains of gp120, affect the broadly neutralizing epitope recognized by 1.5e by disturbing the overall conformation of the envelope protein. PubMed ID: 7546903.
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Li1997
A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic Neutralization of a Chimeric SIV/HIV Type 1 Virus with Combinations of Human Anti-HIV Type 1 Envelope Monoclonal Antibodies or Hyperimmune Globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233.
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Lin2007
George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109.
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Magnus2010
Carsten Magnus and Roland R. Regoes. Estimating the Stoichiometry of HIV Neutralization. PLoS Comput. Biol., 6(3):e1000713, Mar 2010. PubMed ID: 20333245.
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McCann2005
C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016.
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McDougal1996
J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Melchers2012
Mark Melchers, Ilja Bontjer, Tommy Tong, Nancy P. Y. Chung, Per Johan Klasse, Dirk Eggink, David C. Montefiori, Maurizio Gentile, Andrea Cerutti, William C. Olson, Ben Berkhout, James M. Binley, John P. Moore, and Rogier W. Sanders. Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses. J. Virol., 86(5):2488-2500, Mar 2012. PubMed ID: 22205734.
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Moore1993a
J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308.
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Moore1994b
J. P. Moore, F. E. McCutchan, S.-W. Poon, J. Mascola, J. Liu, Y. Cao, and D. D. Ho. Exploration of Antigenic Variation in gp120 from Clades A through F of Human Immunodeficiency Virus Type 1 by Using Monoclonal Antibodies. J. Virol., 68:8350-8364, 1994. Four of five anti-V3 MAbs were slightly cross-reactive within clade B, but not very reactive outside clade B. Two discontinuous CD4 binding site Mabs appear to be pan-reactive. Anti-V2 MAbs were only sporadically reactive inside and outside of clade B. PubMed ID: 7525988.
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Moore1994d
J. P. Moore, Y. Cao, D. D. Ho, and R. A. Koup. Development of the anti-gp120 antibody response during seroconversion to human immunodeficiency virus type 1. J. Virol., 68:5142-5155, 1994. Three seroconverting individuals were studied. The earliest detectable anti-gp120 antibodies were both conformational and anti-V3 loop, and could be detected only after the peak viremia has passed. No uniform pattern of autologous neutralizing anti-CD4BS or anti-V3 MAbs was observed. PubMed ID: 8035514.
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Moore1996
J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711.
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Nabatov2004
Alexey A. Nabatov, Georgios Pollakis, Thomas Linnemann, Aletta Kliphius, Moustapha I. M. Chalaby, and William A. Paxton. Intrapatient Alterations in the Human Immunodeficiency Virus Type 1 gp120 V1V2 and V3 Regions Differentially Modulate Coreceptor Usage, Virus Inhibition by CC/CXC Chemokines, Soluble CD4, and the b12 and 2G12 Monoclonal Antibodies. J. Virol., 78(1):524-530, Jan 2004. PubMed ID: 14671134.
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Pancera2010a
Marie Pancera, Shahzad Majeed, Yih-En Andrew Ban, Lei Chen, Chih-chin Huang, Leopold Kong, Young Do Kwon, Jonathan Stuckey, Tongqing Zhou, James E. Robinson, William R. Schief, Joseph Sodroski, Richard Wyatt, and Peter D. Kwong. Structure of HIV-1 gp120 with gp41-Interactive Region Reveals Layered Envelope Architecture and Basis of Conformational Mobility. Proc. Natl. Acad. Sci. U.S.A., 107(3):1166-1171, 19 Jan 2010. PubMed ID: 20080564.
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Pantophlet2003
Ralph Pantophlet, Erica Ollmann Saphire, Pascal Poignard, Paul W. H. I. Parren, Ian A. Wilson, and Dennis R. Burton. Fine Mapping of the Interaction of Neutralizing and Nonneutralizing Monoclonal Antibodies with the CD4 Binding Site of Human Immunodeficiency Virus Type 1 gp120. J. Virol., 77(1):642-658, Jan 2003. PubMed ID: 12477867.
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Pantophlet2003b
Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582.
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Pantophlet2004
R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540.
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Park2000
E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031.
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Parren1997
P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324.
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Parren1998
P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629.
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Poignard1996b
P. Poignard, T. Fouts, D. Naniche, J. P. Moore, and Q. J. Sattentau. Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J. Exp. Med., 183:473-484, 1996. Binding of Anti-V3 and the CD4I neutralizing MAbs induces shedding of gp120 on cells infected with the T-cell line-adapted HIV-1 molecular clone Hx10. This was shown by significant increases of gp120 in the supernatant, and exposure of a gp41 epitope that is masked in the oligomer. MAbs binding either to the V2 loop or to CD4BS discontinuous epitopes do not induce gp120 dissociation. This suggests HIV neutralization probably is caused by several mechanisms, and one of the mechanisms may involve gp120 dissociation. PubMed ID: 8627160.
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Pollara2013
Justin Pollara, Mattia Bonsignori, M. Anthony Moody, Marzena Pazgier, Barton F. Haynes, and Guido Ferrari. Epitope Specificity of Human Immunodeficiency Virus-1 Antibody Dependent Cellular Cytotoxicity (ADCC) Responses. Curr. HIV Res., 11(5):378-387, Jul 2013. PubMed ID: 24191939.
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Raja2003
Aarti Raja, Miro Venturi, Peter Kwong, and Joseph Sodroski. CD4 Binding Site Antibodies Inhibit Human Immunodeficiency Virus gp120 Envelope Glycoprotein Interaction with CCR5. J. Virol., 77(1):713-718, Jan 2003. PubMed ID: 12477875.
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Robinson1992
J. Robinson, H. Yoshiyama, D. Holton, S. Elliot, and D.D. Ho. Distinct Antigenic Sites on HIV gp120 Identified by a Panel of Human Monoclonal Antibodies. J. Cell Biochem., Suppl 16E:71, 1992.
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Robinson2005
James E. Robinson, Debra Holton Elliott, Effie A. Martin, Kathryne Micken, and Eric S. Rosenberg. High Frequencies of Antibody Responses to CD4 Induced Epitopes in HIV Infected Patients Started on HAART during Acute Infection. Hum Antibodies, 14(3-4):115-121, 2005. PubMed ID: 16720981.
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Sanders2013
Rogier W. Sanders, Ronald Derking, Albert Cupo, Jean-Philippe Julien, Anila Yasmeen, Natalia de Val, Helen J. Kim, Claudia Blattner, Alba Torrents de la Peña, Jacob Korzun, Michael Golabek, Kevin de los Reyes, Thomas J. Ketas, Marit J. van Gils, C. Richter King, Ian A. Wilson, Andrew B. Ward, P. J. Klasse, and John P. Moore. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but not Non-Neutralizing Antibodies. PLoS Pathog., 9(9):e1003618, Sep 2013. PubMed ID: 24068931.
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Sattentau1995a
Q. J. Sattentau and J. P. Moore. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med., 182:185-196, 1995. This study suggests that antibodies specific for one of five different binding regions on gp120 are associated with viral neutralization: V2, V3, C4, the CD4 binding site, and a complex discontinuous epitope that does not interfere with CD4 binding. Kinetic binding properties of a set of MAbs that bind to these regions were studied, analyzing binding to both functional oligomeric LAI gp120 and soluble monomeric LAI BH10 gp120; neutralization ID$_50$s were also evaluated. It was found that the neutralization ID$_50$s was related to the ability to bind oligomeric, not monomeric, gp120, and concluded that with the exception of the V3 loop, regions of gp120 that are immunogenic will be poorly presented on cell-line-adapted virions. Further, the association rate, estimated as the t$_1/2$ to reach equilibrium binding to multimeric, virion associated, gp120, appears to be a major factor relating to affinity and potency of the neutralization response to cell-line-adapted virus. PubMed ID: 7540648.
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Seaman2010
Michael S. Seaman, Holly Janes, Natalie Hawkins, Lauren E. Grandpre, Colleen Devoy, Ayush Giri, Rory T. Coffey, Linda Harris, Blake Wood, Marcus G. Daniels, Tanmoy Bhattacharya, Alan Lapedes, Victoria R Polonis, Francine E. McCutchan, Peter B. Gilbert, Steve G. Self, Bette T. Korber, David C. Montefiori, and John R. Mascola. Tiered Categorization of a Diverse Panel of HIV-1 Env Pseudoviruses for Assessment of Neutralizing Antibodies. J Virol, 84(3):1439-1452, Feb 2010. PubMed ID: 19939925.
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Srivastava2005
Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830.
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Sullivan1998
N. Sullivan, Y. Sun, Q. Sattentau, M. Thali, D. Wu, G. Denisova, J. Gershoni, J. Robinson, J. Moore, and J. Sodroski. CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization. J. Virol., 72:4694-4703, 1998. A study of the sCD4 inducible MAb 17bi, and the MAb CG10 that recognizes a gp120-CD4 complex. These epitopes are minimally accessible upon attachment of gp120 to the cell. The CD4-binding induced changes in gp120 were studied, exploring the sequestering of chemokine receptor binding sites from the humoral response. PubMed ID: 9573233.
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Sullivan1998b
N. Sullivan, Y. Sun, J. Binley, J. Lee, C. F. Barbas III, P. W. H. I. Parren, D. R. Burton, and J. Sodroski. Determinants of human immunodeficiency virus type 1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies. J. Virol., 72:6332-8, 1998. PubMed ID: 9658072.
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Sundling2012
Christopher Sundling, Yuxing Li, Nick Huynh, Christian Poulsen, Richard Wilson, Sijy O'Dell, Yu Feng, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. High-Resolution Definition of Vaccine-Elicited B Cell Responses Against the HIV Primary Receptor Binding Site. Sci. Transl. Med., 4(142):142ra96, 11 Jul 2012. PubMed ID: 22786681.
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Takeda1992
A. Takeda, J. E. Robinson, D. D. Ho, C. Debouck, N. L. Haigwood, and F. A. Ennis. Distinction of human immunodeficiency virus type 1 neutralization and infection enhancement by human monoclonal antibodies to glycoprotein 120. J Clin Inv, 89:1952-1957, 1992. Complement receptors for IgG on monocytic cells can serve as a means for MAb mediated enhancement of HIV-1 infection. MAbs N70-1.5 and N70-2.3a bind distinct discontinuous epitopes in gp120. N70-1.5 is a potent neutralizing MAb with no enhancing activity, while N70-2.3a doesn't neutralize and mediates enhancement of HIV-1 infection. PubMed ID: 1376330.
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Thali1991
M. Thali, U. Olshevsky, C. Furman, D. Gabuzda, M. Posner, and J. Sodroski. Characterization of a discontinuous human immunodeficiency virus type 1 gp120 epitope recognized by a broadly reactive neutralizing human monoclonal antibody. J. Virol., 65(11):6188-6193, 1991. An early detailed characterization of the mutations that inhibit the neutralization capacity of the MAb F105, that binds to a discontinuous epitope and inhibits CD4 binding to gp120. PubMed ID: 1717717.
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Thali1992a
M. Thali, C. Furman, D. D. Ho, J. Robinson, S. Tilley, A. Pinter, and J. Sodroski. Discontinuous, Conserved Neutralization Epitopes Overlapping the CD4-Binding Region of Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. J. Virol., 66:5635-5641, 1992. Maps the relationship between amino acid substitutions that reduce CD4-gp120 interaction, and amino acid substitutions that reduce the binding of discontinuous epitope MAbs that inhibit CD4 binding. PubMed ID: 1380099.
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Thali1993
M. Thali, J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski. Characterization of Conserved Human Immunodeficiency Virus Type 1 gp120 Neutralization Epitopes Exposed upon gp120-CD4 Binding. J. Virol., 67:3978-3988, 1993. Five regions are likely to contribute to the 48d and 17b discontinuous epitopes, either directly or through local conformational effects: the hydrophobic ring-like structure formed by the disulfide bond that links C3 and C4, the base of the stem-loop that contains V1 and V2, and the hydrophobic region in C2 from Arg 252 to Asp 262. Additionally changes in Glu 370, and Met 475 in C5, affected binding and neutralization. The hydrophobic character of these critical regions is consistent with the limited exposure on gp120 prior to CD4 binding. PubMed ID: 7685405.
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Thali1994
M. Thali, M. Charles, C. Furman, L. Cavacini, M. Posner, J. Robinson, and J. Sodroski. Resistance to Neutralization by Broadly Reactive Antibodies to the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein Conferred by a gp41 Amino Acid Change. J. Virol., 68:674-680, 1994. A T->A amino acid substitution at position 582 of gp41 conferred resistance to neutralization to 30\% of HIV positive sera (Wilson et al. J Virol 64:3240-48 (1990)). Monoclonal antibodies that bound to the CD4 binding site were unable to neutralize this virus, but the mutation did not reduce the neutralizing capacity of a V2 region MAb G3-4, V3 region MAbs, or gp41 neutralizing MAb 2F5. PubMed ID: 7507184.
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Tong2012
Tommy Tong, Ema T. Crooks, Keiko Osawa, and James M. Binley. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes. J. Virol., 86(7):3574-3587, Apr 2012. PubMed ID: 22301141.
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Trkola1996b
A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796.
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Trkola1998
A. Trkola, T. Ketas, V. N. Kewalramani, F. Endorf, J. M. Binley, H. Katinger, J. Robinson, D. R. Littman, and J. P. Moore. Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Primary Isolates to Antibodies and CD4-Based Reagents Is Independent of Coreceptor Usage. J. Virol., 72:1876-1885, 1998. PubMed ID: 9499039.
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Vaine2008
Michael Vaine, Shixia Wang, Emma T. Crooks, Pengfei Jiang, David C. Montefiori, James Binley, and Shan Lu. Improved Induction of Antibodies against Key Neutralizing Epitopes by Human Immunodeficiency Virus Type 1 gp120 DNA Prime-Protein Boost Vaccination Compared to gp120 Protein-Only Vaccination. J. Virol., 82(15):7369-7378, Aug 2008. PubMed ID: 18495775.
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Walker2010
Laura M. Walker, Melissa D. Simek, Frances Priddy, Johannes S. Gach, Denise Wagner, Michael B. Zwick, Sanjay K. Phogat, Pascal Poignard, and Dennis R. Burton. A Limited Number of Antibody Specificities Mediate Broad and Potent Serum Neutralization in Selected HIV-1 Infected Individuals. PLoS Pathog., 6(8), 2010. PubMed ID: 20700449.
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Watkins1993
B. A. Watkins, M. S. Reitz, Jr., C. A. Wilson, K. Aldrich, A. E. Davis, and M. Robert-Guroff. Immune escape by human immunodeficiency virus type 1 from neutralizing antibodies: evidence for multiple pathways. J. Virol., 67:7493-7500, 1993. A neutralization resistance point mutation (HXB2 A281V) was studied using a variety of MAbs, and it was shown that this substitution affects a different epitope than a previously characterized neutralization escape mutant (A582T) (Reitz 1988, Wilson 1990). PubMed ID: 7693973.
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Wisnewski1996
A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730.
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Wu2009a
Lan Wu, Tongqing Zhou, Zhi-yong Yang, Krisha Svehla, Sijy O'Dell, Mark K. Louder, Ling Xu, John R. Mascola, Dennis R. Burton, James A. Hoxie, Robert W. Doms, Peter D. Kwong, and Gary J. Nabel. Enhanced Exposure of the CD4-Binding Site to Neutralizing Antibodies by Structural Design of a Membrane-Anchored Human Immunodeficiency Virus Type 1 gp120 Domain. J. Virol., 83(10):5077-5086, May 2009. PubMed ID: 19264769.
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Wu2010
Xueling Wu, Zhi-Yong Yang, Yuxing Li, Carl-Magnus Hogerkorp, William R. Schief, Michael S. Seaman, Tongqing Zhou, Stephen D. Schmidt, Lan Wu, Ling Xu, Nancy S. Longo, Krisha McKee, Sijy O'Dell, Mark K. Louder, Diane L. Wycuff, Yu Feng, Martha Nason, Nicole Doria-Rose, Mark Connors, Peter D. Kwong, Mario Roederer, Richard T. Wyatt, Gary J. Nabel, and John R. Mascola. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1. Science, 329(5993):856-861, 13 Aug 2010. PubMed ID: 20616233.
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Wyatt1992
R. Wyatt, M. Thali, S. Tilley, A. Pinter, M. Posner, D. Ho, J. Robinson, and J. Sodroski. Relationship of the Human Immunodeficiency Virus Type 1 gp120 Third Variable Loop to Elements of the CD4 Binding Site. J. Virol., 66:6997-7004, 1992. This paper examines mutations which alter MAb binding and neutralization. Anti-V3 MAb 9284 has enhanced binding due to a mutation in the C4 region that is also important for CD4 binding, and anti-CD4 binding MAbs F105, 1.5e and 1125H show increased precipitation of a gp120 from which the V3 loop was deleted, relative to wild type, in RIPA buffer containing non-ionic detergents. PubMed ID: 1279195.
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Wyatt1993
R. Wyatt, N. Sullivan, M. Thali, H. Repke, D. Ho, J. Robinson, M. Posner, and J. Sodroski. Functional and Immunologic Characterization of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Containing Deletions of the Major Variable Regions. J. Virol., 67:4557-4565, 1993. Affinity of neutralizing MAbs directed against the CD4 binding site was increased dramatically by deletion mutants across the V1/V2 and V3 structures, suggesting that these domains mask these conserved discontinuous epitopes. PubMed ID: 8331723.
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Wyatt1997
R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638.
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Wyatt1998
R. Wyatt, P. D. Kwong, E. Desjardins, R. W. Sweet, J. Robinson, W. A. Hendrickson, and J. G. Sodroski. The Antigenic Structure of the HIV gp120 Envelope Glycoprotein. Nature, 393:705-711, 1998. Comment in Nature 1998 Jun 18;393(6686):630-1. The spatial organization of the neutralizing epitopes of gp120 is described, based on epitope maps interpreted in the context of the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody. PubMed ID: 9641684.
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Xiang2002
Shi-Hua. Xiang, Peter D. Kwong, Rishi Gupta, Carlo D. Rizzuto, David J. Casper, Richard Wyatt, Liping Wang, Wayne A. Hendrickson, Michael L. Doyle, and Joseph Sodroski. Mutagenic Stabilization and/or Disruption of a CD4-Bound State Reveals Distinct Conformations of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. J. Virol., 76(19):9888-9899, Oct 2002. PubMed ID: 12208966.
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Yang2005b
Xinzhen Yang, Svetla Kurteva, Sandra Lee, and Joseph Sodroski. Stoichiometry of Antibody Neutralization of Human Immunodeficiency Virus Type 1. J. Virol., 79(6):3500-3508, Mar 2005. PubMed ID: 15731244.
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Yuan2006
Wen Yuan, Jessica Bazick, and Joseph Sodroski. Characterization of the Multiple Conformational States of Free Monomeric and Trimeric Human Immunodeficiency Virus Envelope Glycoproteins after Fixation by Cross-Linker. J. Virol., 80(14):6725-6737, Jul 2006. PubMed ID: 16809278.
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Zhang2002
Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155.
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Zhou2007
Tongqing Zhou, Ling Xu, Barna Dey, Ann J. Hessell, Donald Van Ryk, Shi-Hua Xiang, Xinzhen Yang, Mei-Yun Zhang, Michael B. Zwick, James Arthos, Dennis R. Burton, Dimiter S. Dimitrov, Joseph Sodroski, Richard Wyatt, Gary J. Nabel, and Peter D. Kwong. Structural Definition of a Conserved Neutralization Epitope on HIV-1 gp120. Nature, 445(7129):732-737, 15 Feb 2007. PubMed ID: 17301785.
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Zwick2003a
Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015.
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Schiffner2018
Torben Schiffner, Jesper Pallesen, Rebecca A. Russell, Jonathan Dodd, Natalia de Val, Celia C. LaBranche, David Montefiori, Georgia D. Tomaras, Xiaoying Shen, Scarlett L. Harris, Amin E. Moghaddam, Oleksandr Kalyuzhniy, Rogier W. Sanders, Laura E. McCoy, John P. Moore, Andrew B. Ward, and Quentin J. Sattentau. Structural and Immunologic Correlates of Chemically Stabilized HIV-1 Envelope Glycoproteins. PLoS Pathog., 14(5):e1006986, May 2018. PubMed ID: 29746590.
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Displaying record number 630
Download this epitope
record as JSON.
MAb ID |
21h (2.1H) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
James Robinson, Tulane University, LA |
Epitope |
|
Ab Type |
gp120 CD4bs |
Neutralizing |
L |
Species
(Isotype)
|
human(IgG1) |
Patient |
N70 |
Immunogen |
HIV-1 infection |
Keywords |
acute/early infection, antibody binding site, antibody interactions, antibody sequence, binding affinity, review, structure, subtype comparisons, vaccine antigen design, variant cross-reactivity |
Notes
Showing 26 of
26 notes.
-
Lists 7 mAbs derived from patient N70: 15E, 1.9B, 2.3A, 2.3B, 2.1H, F91, 1.7B.
Robinson1992
-
21h: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:3-11*03, IGHD:4-17, D-RF:3, IGHJ:5. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner.
Gorny2009
(antibody sequence)
-
21h: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed.
Srivastava2005
(vaccine antigen design, review)
-
21h: This review summarizes MAbs directed to HIV-1 Env. There are 51 CD4BS MAbs and Fabs in the database; most, like this MAb, neutralize TCLA strains only.
Gorny2003
(review)
-
21h: UK Medical Research Council AIDS reagent: ARP3017.
-
21h: A series of mutational changes were introduced into the YU2 gp120 that favored different conformations---375 S/W seems to favor a conformation of gp120 closer to the CD4-bound state, and is readily bound by sCD4 and CD4i MAbs (17b, 48d, 49e, 21c and 23e) but binding of anti-CD4BS MAbs (F105, 15e, IgG1b12, 21h and F91) was markedly reduced---IgG1b12 failed to neutralize this mutant, while neutralization by 2G12 was enhanced---2F5 did not neutralize either WT or mutant, probably due to polymorphism in the YU2 epitope---another mutant, 423 I/P, disrupted the gp120 bridging sheet, favored a different conformation and did not bind CD4, CCR5, or CD4i antibodies, but did bind to CD4BS MAbs.
Xiang2002
(antibody binding site)
-
21h: CD4BS MAbs 15e, 21h, and F91 bind with even lower affinity than 205-43-1 and 205-42-15 to JRFL oligomer -- conclusions of this paper contrast with Parren1998 Fouts1998.
Fouts1998,Parren1998
(binding affinity)
-
21h: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope.
Parren1998
(antibody binding site)
-
21h: Summary of the implications of the crystal structure of the core of gp120 bound to CD4 and 17b with what is known about mutations that reduce NAb binding -- probable mechanism of neutralization by CD4BS Ab is direct interference with CD4 binding.
Wyatt1998
(antibody binding site, structure)
-
21h: Neutralizes TCLA strains, but not primary isolates.
Parren1997
(variant cross-reactivity)
-
21h: Binds both gp120 and soluble gp120+gp41 complex efficiently, suggesting its gp120 epitope is not blocked by gp41 binding -- major deletions in C1 and C5 and deletions of the V1V2 and V3 loops do not diminish binding.
Wyatt1997
(antibody binding site)
-
21h: Viral binding inhibition by 21h strongly correlated with neutralization (all other neutralizing MAbs tested showed some correlation except 2F5).
Ugolini1997
(antibody binding site)
-
21h: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env -- 50% neutralization could not be achieved at a maximal concentration of 67 mug/ml.
Li1997
(variant cross-reactivity)
-
21h: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 21h bound monomer, did not bind oligomer or neutralize JRFL.
Fouts1997
(antibody binding site)
-
21h: Called 2.1H -- Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background.
McKeating1996b
(variant cross-reactivity)
-
21h: 21h is V H3 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals.
Wisnewski1996
(antibody sequence)
-
21h: Anti-CD4BS MAbs 15e, 21h, and IgG1b12 did not cause gp120 dissociation from virus, or exposure of the gp41 epitope of MAb 50-69, in contrast to CD4i MAb 48d and anti-V3 neutralizing MAbs.
Poignard1996b
(antibody binding site, antibody interactions)
-
21h: Anti-CD4 binding site MAb -- reciprocal inhibition by anti-C1, -C4 and other anti-CD4 binding site antibodies -- enhanced by some anti-V2 MAbs and anti-V3 MAb 5G11 -- enhances binding of some anti-V3 and -V2 MAbs.
Moore1996
(antibody interactions)
-
21h: Binds with higher affinity to monomer than to oligomer, moderate association rate.
Sattentau1995a
(antibody binding site)
-
21h: A mutation in gp41, 582 A/T, confers resistance to neutralization (also confers resistance to MAbs F105, 48d, 15e and 17b).
Thali1994
(variant cross-reactivity)
-
21h: Heavy chain is V HIII, VDP-35 -- light chain is V_lambdaIIIa, Hum318. Compared to 15e and F105.
Bagley1994
(antibody sequence)
-
21h: Competition studies with human sera from seroconverting individuals showed that anti-CD4 BS antibodies can arise very early in infection, comparable or prior to anti-V3 antibodies.
Moore1994d
(acute/early infection)
-
21h: Has strong cross-reactivity with gp120 monomers from most subtypes, A-F, with the least reactivity to clade E.
Moore1994b
(subtype comparisons)
-
21h: Conformational, does not bind denatured gp120 -- neutralizes IIIB -- reactive with SF-2 gp120 -- strong inhibition of HIV+ human sera binding to IIIB gp120.
Moore1993a
(antibody binding site)
-
21h: Binding to Delta V1/2 and Delta V1/2/3 mutant glycoproteins is greater than binding to wildtype gp120.
Wyatt1993
(antibody binding site)
-
21h: Amino acid substitutions in HXB2 that inhibit binding, some shared with CD4 binding inhibition, 88, 113, 257, 368, 370, 421, 470, 480.
Thali1992a
(antibody binding site)
References
Showing 28 of
28 references.
Bagley1994
J. Bagley, P. J. Dillon, C. Rosen, J. Robinson, J. Sodroski, and W. A. Marasco. Structural Characterization of Broadly Neutralizing Human Monoclonal Antibodies Against the CD4 Binding Site of HIV-1 gp120. Mol. Immunol., 31(15):1149-1160, 1994. This paper is a detailed study of the V-D-J heavy chain usage and V-J light chain usage for the three monoclonals that bind to the HIV-1 envelope CD4 binding site: F105, 15e and 21h. Different germline genes were used, and there was evidence for antigen-drive clonal selection of somatic mutations. Eight positions in the heavy chain and two in the light chain complementarity determining positions were identical in the three Mabs. PubMed ID: 7935503.
Show all entries for this paper.
Binley1997
J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287.
Show all entries for this paper.
Fouts1997
T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632.
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Fouts1998
T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713.
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Gorny2003
Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162.
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Ho1991a
D. D. Ho, J. A. McKeating, X. L. Li, T. Moudgil, E. S. Daar, N.-C. Sun, and J. E. Robinson. Conformational Epitope of gp120 Important in CD4 Binding and Human Immunodeficiency Virus Type 1 Neutralization Identified by a Human Monoclonal Antibody. J. Virol., 65:489-493, 1991. A description of the neutralizing human MAb 15e. It binds to HIV-1 with a broad specificity, and blocks gp120 binding to CD4, and is a discontinuous epitope; DTT reduction of env abrogates binding. PubMed ID: 1702163.
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Ho1992
D. D. Ho, M. S. C. Fung, H. Yoshiyama, Y. Cao, and J. E. Robinson. Discontinuous Epitopes on gp120 Important in HIV-1 Neutralization. AIDS Res. Hum. Retroviruses, 8:1337-1339, 1992. Further description of the human MAb 15e and the murine MAb G3-4. gp120 mutants that affect 15e epitope binding: 113, 257, 368, 370, 421, 427, 475; four of these coincide with amino acids important for the CD4 binding domain. G3-4 is neutralizing and behaves like a discontinuous epitope, and partially blocks sCD4 binding. PubMed ID: 1281654.
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Li1997
A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic Neutralization of a Chimeric SIV/HIV Type 1 Virus with Combinations of Human Anti-HIV Type 1 Envelope Monoclonal Antibodies or Hyperimmune Globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233.
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McKeating1996b
J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395.
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Moore1993a
J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308.
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Moore1994b
J. P. Moore, F. E. McCutchan, S.-W. Poon, J. Mascola, J. Liu, Y. Cao, and D. D. Ho. Exploration of Antigenic Variation in gp120 from Clades A through F of Human Immunodeficiency Virus Type 1 by Using Monoclonal Antibodies. J. Virol., 68:8350-8364, 1994. Four of five anti-V3 MAbs were slightly cross-reactive within clade B, but not very reactive outside clade B. Two discontinuous CD4 binding site Mabs appear to be pan-reactive. Anti-V2 MAbs were only sporadically reactive inside and outside of clade B. PubMed ID: 7525988.
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Moore1994d
J. P. Moore, Y. Cao, D. D. Ho, and R. A. Koup. Development of the anti-gp120 antibody response during seroconversion to human immunodeficiency virus type 1. J. Virol., 68:5142-5155, 1994. Three seroconverting individuals were studied. The earliest detectable anti-gp120 antibodies were both conformational and anti-V3 loop, and could be detected only after the peak viremia has passed. No uniform pattern of autologous neutralizing anti-CD4BS or anti-V3 MAbs was observed. PubMed ID: 8035514.
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Moore1996
J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711.
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Parren1997
P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324.
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Parren1998
P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629.
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Poignard1996b
P. Poignard, T. Fouts, D. Naniche, J. P. Moore, and Q. J. Sattentau. Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J. Exp. Med., 183:473-484, 1996. Binding of Anti-V3 and the CD4I neutralizing MAbs induces shedding of gp120 on cells infected with the T-cell line-adapted HIV-1 molecular clone Hx10. This was shown by significant increases of gp120 in the supernatant, and exposure of a gp41 epitope that is masked in the oligomer. MAbs binding either to the V2 loop or to CD4BS discontinuous epitopes do not induce gp120 dissociation. This suggests HIV neutralization probably is caused by several mechanisms, and one of the mechanisms may involve gp120 dissociation. PubMed ID: 8627160.
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Sattentau1995a
Q. J. Sattentau and J. P. Moore. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med., 182:185-196, 1995. This study suggests that antibodies specific for one of five different binding regions on gp120 are associated with viral neutralization: V2, V3, C4, the CD4 binding site, and a complex discontinuous epitope that does not interfere with CD4 binding. Kinetic binding properties of a set of MAbs that bind to these regions were studied, analyzing binding to both functional oligomeric LAI gp120 and soluble monomeric LAI BH10 gp120; neutralization ID$_50$s were also evaluated. It was found that the neutralization ID$_50$s was related to the ability to bind oligomeric, not monomeric, gp120, and concluded that with the exception of the V3 loop, regions of gp120 that are immunogenic will be poorly presented on cell-line-adapted virions. Further, the association rate, estimated as the t$_1/2$ to reach equilibrium binding to multimeric, virion associated, gp120, appears to be a major factor relating to affinity and potency of the neutralization response to cell-line-adapted virus. PubMed ID: 7540648.
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Srivastava2005
Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830.
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Thali1992a
M. Thali, C. Furman, D. D. Ho, J. Robinson, S. Tilley, A. Pinter, and J. Sodroski. Discontinuous, Conserved Neutralization Epitopes Overlapping the CD4-Binding Region of Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. J. Virol., 66:5635-5641, 1992. Maps the relationship between amino acid substitutions that reduce CD4-gp120 interaction, and amino acid substitutions that reduce the binding of discontinuous epitope MAbs that inhibit CD4 binding. PubMed ID: 1380099.
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Thali1994
M. Thali, M. Charles, C. Furman, L. Cavacini, M. Posner, J. Robinson, and J. Sodroski. Resistance to Neutralization by Broadly Reactive Antibodies to the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein Conferred by a gp41 Amino Acid Change. J. Virol., 68:674-680, 1994. A T->A amino acid substitution at position 582 of gp41 conferred resistance to neutralization to 30\% of HIV positive sera (Wilson et al. J Virol 64:3240-48 (1990)). Monoclonal antibodies that bound to the CD4 binding site were unable to neutralize this virus, but the mutation did not reduce the neutralizing capacity of a V2 region MAb G3-4, V3 region MAbs, or gp41 neutralizing MAb 2F5. PubMed ID: 7507184.
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Ugolini1997
S. Ugolini, I. Mondor, P. W. H. I Parren, D. R. Burton, S. A. Tilley, P. J. Klasse, and Q. J. Sattentau. Inhibition of Virus Attachment to CD4+ Target Cells Is a Major Mechanism of T Cell Line-Adapted HIV-1 Neutralization. J. Exp. Med., 186:1287-1298, 1997. PubMed ID: 9334368.
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Wisnewski1996
A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730.
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Wyatt1993
R. Wyatt, N. Sullivan, M. Thali, H. Repke, D. Ho, J. Robinson, M. Posner, and J. Sodroski. Functional and Immunologic Characterization of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Containing Deletions of the Major Variable Regions. J. Virol., 67:4557-4565, 1993. Affinity of neutralizing MAbs directed against the CD4 binding site was increased dramatically by deletion mutants across the V1/V2 and V3 structures, suggesting that these domains mask these conserved discontinuous epitopes. PubMed ID: 8331723.
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Wyatt1997
R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638.
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Wyatt1998
R. Wyatt, P. D. Kwong, E. Desjardins, R. W. Sweet, J. Robinson, W. A. Hendrickson, and J. G. Sodroski. The Antigenic Structure of the HIV gp120 Envelope Glycoprotein. Nature, 393:705-711, 1998. Comment in Nature 1998 Jun 18;393(6686):630-1. The spatial organization of the neutralizing epitopes of gp120 is described, based on epitope maps interpreted in the context of the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody. PubMed ID: 9641684.
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Xiang2002
Shi-Hua. Xiang, Peter D. Kwong, Rishi Gupta, Carlo D. Rizzuto, David J. Casper, Richard Wyatt, Liping Wang, Wayne A. Hendrickson, Michael L. Doyle, and Joseph Sodroski. Mutagenic Stabilization and/or Disruption of a CD4-Bound State Reveals Distinct Conformations of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. J. Virol., 76(19):9888-9899, Oct 2002. PubMed ID: 12208966.
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Gorny2009
Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295.
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Robinson1992
J. Robinson, H. Yoshiyama, D. Holton, S. Elliot, and D.D. Ho. Distinct Antigenic Sites on HIV gp120 Identified by a Panel of Human Monoclonal Antibodies. J. Cell Biochem., Suppl 16E:71, 1992.
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