Search Antibody Database

Found 1 matching record:

Displaying record number 603

Download this epitope record as JSON.

Notes

Showing 29 of 29 notes.

• 654-D: The authors mutated two conserved tyrosine (Y) residues within the V2 loop of gp120 Y177 and Y173, individually or in combination, by replacing them with either phenylalanine (F) or alanine (A) in a clade B, tier 1B HIV-1 Env protein (BaL), and in a number of tier 2 HIV-1 Envs from different clades, namely, BG505 (clade A), JR-FL and JR-CSF (clade B), and CM244 (clade E). A consistent hierarchy of neutralization sensitivity was seen among the mutants, with a greater impact of Y177 over Y173 single mutations, of double over single mutations, and of A over F substitutions. The double-alanine mutation in mutant HIV-1 BaL, Y173A Y177A, increased sensitivity to all the weakly neutralizing MAbs tested and even rendered the virus sensitive to non-neutralizing antibodies against the CD4 binding site, such as F105, 654-30D, and b13. When tested against bNAbs instead, there was a trend to decrease neutralization sensitivity compared to WT, with the exception of N6, PGT151, 10E8, and 2G12, for which there was no change, and of 2F5 and 4E10, which were more effective against the mutant compared to the WT. Guzzo2018 (antibody binding site, binding affinity)
• 654-30D: 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)
• 654-D: The use of mutated HIV-1 gp120 to elicit higher tilters of ant-gp120 Ab response was investigated. Immune complex vaccine with the anti-CD4bs MAb 654 and N448Q or N448E mutants (site specific N-glycan removal), but not mutants alone, stimulated comparably high levels of serum Abs to gp120 and V3 as the wild type complex; but Abs against the C1 and C2 regions in the gp120 core were more elevated. The mutant complex also elicited higher titers of neutralizing Ab activity than its wild type counterpart. Kumar2011 (glycosylation, neutralization)
• 654-D: This MAb was highly reactive against 6 gp120 from subtype B viruses and one subtype C. Subtype B AN1 and a subtype D gp120 were recognized weakly while a subtype E was not recognized. Six of the highly reactive gp120 in complex with 654-D had higher reactivity with 694/98-D MAb compared to uncomplexed gp120. Mice immunized with LAI gp120/654-D complex in NPL/DDA adjuvant generated sera with Abs specific for gp120 and V3, but these Abs were only reactive to the homologous peptide. Sera from these mice neutralized the homologous virus better than sera from mice immunized with uncomplexed gp120. In contrast, sera from mice immunized with JRFL gp120/654-D were reactive with the homologous virus and also SF162, MN, and LAI. These sera also showed cross-neutralizing activity, but only against highly sensitive viruses, and were ineffective in neutralizing resistant viruses including the homologous JRFL. Hioe2009 (neutralization, variant cross-reactivity, vaccine-induced immune responses)
• 654-D: A mouse CD4 T cell clone proliferated well in response to gp120 alone but this response was inhibited by more than 80% when gp120 was complexed with MAb 654. Mice immunized with gp120-654 complex showed lower levels of lymphoproliferation than mice immunized with gp120-670 complex, indicating that anti-CD4bs Abs suppress the induction of CD4 T cell responses in vivo. However, mice immunized with gp120/654 Ab displayed faster kinetics and higher levels of gp120-specific serum IgG and IgA, but not IgM, indicating that immunization with gp120 in the presence of anti-CD4 Ab alters the immunogenicity of gp120 such that the immune response is dominated by anti-gp120 IgG. Visciano2008a (vaccine-induced immune responses, kinetics)
• 654-D: A significantly higher level of anti-V3 Abs (694/98D and 447-52D) and anti-C1 MAb (EH21) bound to gp120 complexed with 654D MAb than to gp120 alone or in complex with other non-CD4bs Abs, indicating that binding of 654D to gp120 increases exposure of specific V3 and C1 MAb epitopes. Immunization of mice with gp120-654D complex elicited higher and faster V3-specific Ab responses than immunization with gp120 alone or gp120 in complex with other mAbs, while responses to other gp120 regions was comparable. Abs elicited by immunization with gp120-654D complex reacted preferentially with the homologous V3 peptide, and the sera from immunized mice neutralized homologous, but not heterologous, HIV-1 isolates. Visciano2008 (vaccine antigen design)
• 654-D: 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. 654-D was found to compete for binding to recombinant gp120 with the three neutralizing VHH Abs, indicating overlapping epitopes or steric hinderance. Forsman2008 (antibody interactions)
• 654-D: 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 and neutralization by certain MAbs and human sera. 654-30D exhibited similar levels of binding to both the LLP-2 mutant and wildtype viruses, indicating that its epitope was not altered by the mutation. Kalia2005 (antibody binding site, binding affinity)
• 654-D (650-D): 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 interactions, vaccine antigen design, review)
• 654-D: This Ab bound with a high affinity to gp120IIIb and it strongly suppressed gp120 antigen presentation by MHC class II. Binding of 654D to gp120 did not prevent uptake of gp120 by APCs nor did it inhibit transport of gp120 into the endolysosomes of the APCs. 654D did not, however, disassociate from gp120 at acidic pH, suggesting that gp120-654D complexes remain stable in the APC endolysosomes. Lysosomal enzyme digestion of gp120 in complex with 654D was slow and yielded limited fragmentation of gp120 with distinct patterns. It is thus concluded that poorly neutralizing high-affinity CD4bs Abs produced by chronically infected patients prevent the stimulation of gp120-specific CD4 T-cell responses by producing gp120-Ab complexes resistant to the proteolytic processing by lysosomal enzymes. Tuen2005 (antibody interactions, binding affinity, rate of progression)
• 654-D: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
• 654-D: 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)
• 654-D: Called 654-30D. 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)
• 654-D: Called 654: Conformation-dependent anti-V3 loop Abs may be more cross-reactive, so six new V3 MAbs were generated -- the six new MAbs all bind to the tip of the V3 loop and cross-compete with the MAb 447-52D and are conformationally sensitive -- MAbs showed cross-clade binding to native, intact virions and the strength binding was highly correlated with percent neutralization using the ghost cell or PHA blast assay -- five well-characterized MAbs were used as controls: anti-V3 447-52D (anti-V3 MAb for competition and neutralization studies), 654 (anti-CD4BS used as a conformation-sensitive MAb control), 1331A (anti-C5 used as a linear binding site MAb control), and MAb 246 (anti-gp41 MAb that bound to primary isolates of all clades) Gorny2002
• 654-D: 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, while 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)
• 654-D: CD4BS MAbs when complexed with gp120, inhibit proliferation of gp120-specific CD4 T-cells and IFN gamma production -- anti-CD4BS MAbs inhibit gp120 presentation by altering the uptake and/or processing of gp120 by the APCs, not by blocking of gp120 attachment to CD4 on the surface of APCs. Hioe2001
• 654-D: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 6 CD4BS MAbs -- CD4BS MAbs bound consistently to most isolates of clade D, but poorly to isolates of other clades with the exception of broadly reactive MAb IgG1b12 -- 654-D had the weakest binding among CD4BS MAbs, binding to only 4/26 isolates. Nyambi2000 (variant cross-reactivity, subtype comparisons)
• 654-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 -- MAb 654-D strongly diminished proliferation -- there is a discrepancy in isotyping this antibody, previous reports indicated IgG1kappa, while Hioe suggests it is IgG1lambda. Hioe2000
• 654-D: Binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- CD4BS MAbs 559/64-D, 654-D, 729-D, 9CL and 1331E bound with a 5-13 fold preference for the oligomer. Gorny2000b (antibody binding site, variant cross-reactivity)
• 654-D: The presence of leukocyte function-associated molecule 1 (LFA-1) promotes virus infectivity and hinders neutralization, and anti-LFA-1 MAbs can enhance the neutralizing effect of anti-HIV V3 MAb 447-52D and anti-HIV CD4BS MAb IgG1b12 -- non-neutralizing anti-HIV CD4BS MAb 654-D did not become neutralizing in the presence of anti-LFA-1 MAbs. Hioe1999
• 654-D: Called 654.30D -- deleting the V2 loop of neutralization-resistant HIV-1 isolate SF162 does not abrogate its replication in PBMC or macrophages, but it enhances its neutralization sensitivity to sera from patients with B clade infection up to 170-fold, and also enhances sensitivity to sera from clades A through F -- deletion of V2 but not V1 slightly allowed neutralization by CD4BS MAb 654.30D. Stamatatos1998 (antibody binding site, subtype comparisons)
• 654-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- CD4-BS Abs tended to bind very weakly without clade specificity to virions, but bound well to soluble gp120 -- 654-D bound only to JRFL. Nyambi1998 (variant cross-reactivity, subtype comparisons)
• 654-D: Called 654-D100 -- 654-D100 and IgG1b12 neutralized viruses HIV-BRU and a mutated virus that lacks the V3 loop glycan equally effectively -- in contrast, sera from guinea pigs immunized with BRU gp120 neutralize viruses more effectively that lack the V3 glycan. Schonning1998 (variant cross-reactivity)
• 654-D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-reactivity)
• 654-D: Anti-CD4 BS MAb 654-30D and IgG1b12 have comparable binding affinities, neither mediates gp120-virion dissociation, but IgG1b12 can neutralize SF128A and SF162 and 654-D cannot -- 654-D actually enhances infection by both viruses in primary macrophages. Stamatatos1997 (enhancing activity, binding affinity)
• 654-D: Called 654-30D -- One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env. Li1997 (variant cross-reactivity)
• 654-D: Called 654-30D -- 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 -- CD4BS loop epitopes are somewhat occluded in the oligomeric gp120 epitopes on the virion surface relative to the gp120 monomer as indicated by an increase in the half-maximal binding values to macrophage-tropic isolates SF162 and SF128a and to T-cell tropic SF2 -- binding of anti-CD4BS MAbs to SF2 resulted in a significant amount of dissociation of gp120 from virion surface. Stamatatos1995 (antibody binding site)
• 654-D: Mild oxidation of carbohydrate moieties inhibits binding. Gorny1994 (antibody binding site)
• 654-D: Dissociation constant gp120 IIIB 0.008 -- neutralizes IIIB, acts synergistically with anti-V3 MAb 447-52D -- reported to be human(IgG1lambda) Laal1994 (antibody interactions, kinetics)

References

Showing 32 of 32 references.

Isolation Paper
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. Show all entries for this paper.

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. Show all entries for this paper.

Gorny1994 M. K. Gorny, J. P. Moore, A. J. Conley, S. Karwowska, J. Sodroski, C. Williams, S. Burda, L. J. Boots, and S. Zolla-Pazner. Human Anti-V2 Monoclonal Antibody That Neutralizes Primary but Not Laboratory Isolates of Human Immunodeficiency Virus Type 1. J. Virol., 68:8312-8320, 1994. Detailed characterization of the MAb 697-D. PubMed ID: 7525987. Show all entries for this paper.

Gorny1997 Miroslaw K. Gorny, Thomas C. VanCott, Catarina Hioe, Zimra R. Israel, Nelson L. Michael, Anthony J. Conley, Constance Williams, Joseph A. Kessler II, Padmasree Chigurupati, Sherri Burda, and Susan Zolla-Pazner. Human Monoclonal Antibodies to the V3 Loop of HIV-1 With Intra- and Interclade Cross-Reactivity. J. Immunol., 159:5114-5122, 1997. PubMed ID: 9366441. Show all entries for this paper.

Gorny1998 M. K. Gorny, J. R. Mascola, Z. R. Israel, T. C. VanCott, C. Williams, P. Balfe, C. Hioe, S. Brodine, S. Burda, and S. Zolla-Pazner. A Human Monoclonal Antibody Specific for the V3 Loop of HIV Type 1 Clade E Cross-Reacts with Other HIV Type 1 Clades. AIDS Res. Hum. Retroviruses, 14:213-221, 1998. PubMed ID: 9491911. Show all entries for this paper.

Gorny2000b M. K. Gorny, T. C. VanCott, C. Williams, K. Revesz, and S. Zolla-Pazner. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology, 267:220-8, 2000. PubMed ID: 10662617. Show all entries for this paper.

Gorny2002 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Sandra Cohen, Victoria R. Polonis, William J. Honnen, Samuel C. Kayman, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Human Monoclonal Antibodies Specific for Conformation-Sensitive Epitopes of V3 Neutralize Human Immunodeficiency Virus Type 1 Primary Isolates from Various Clades. J. Virol., 76(18):9035-9045, Sep 2002. PubMed ID: 12186887. 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. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

Hioe1999 C. E. Hioe, J. E. Hildreth, and S. Zolla-Pazner. Enhanced HIV Type 1 Neutralization by Human Anti-Glycoprotein 120 Monoclonal Antibodies in the Presence of Monoclonal Antibodies to Lymphocyte Function-Associated Molecule 1. AIDS Res. Hum. Retroviruses, 15:523-531, 1999. PubMed ID: 10221529. Show all entries for this paper.

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. Show all entries for this paper.

Hioe2001 C. E. Hioe, M. Tuen, P. C. Chien, Jr., G. Jones, S. Ratto-Kim, P. J. Norris, W. J. Moretto, D. F. Nixon, M. K. Gorny, and S. Zolla-Pazner. Inhibition of human immunodeficiency virus type 1 gp120 presentation to CD4 T cells by antibodies specific for the CD4 binding domain of gp120. J. Virol., 75(22):10950--7, Nov 2001. URL: http://jvi.asm.org/cgi/content/full/75/22/10950. PubMed ID: 11602735. Show all entries for this paper.

Hioe2009 Catarina E. Hioe, Maria Luisa Visciano, Rajnish Kumar, Jianping Liu, Ethan A. Mack, Rachel E. Simon, David N. Levy, and Michael Tuen. The Use of Immune Complex Vaccines to Enhance Antibody Responses against Neutralizing Epitopes on HIV-1 Envelope gp120. Vaccine, 28(2):352-360, 11 Dec 2009. PubMed ID: 19879224. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

Karwowska1993 Show all entries for this paper.

Kumar2011 Rajnish Kumar, Michael Tuen, Hualin Li, Doris B. Tse, and Catarina E. Hioe. Improving Immunogenicity of HIV-1 Envelope gp120 by Glycan Removal and Immune Complex Formation. Vaccine, 29(48):9064-9074, 8 Nov 2011. PubMed ID: 21945958. Show all entries for this paper.

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. Show all entries for this paper.

Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of Epitopes Exposed on Intact Human Immunodeficiency Virus Type 1 (HIV-1) Virions: A New Strategy for Studying the Immunologic Relatedness of HIV-1. J. Virol., 72:9384-9391, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.

Stamatatos1998 L. Stamatatos and C. Cheng-Mayer. An Envelope Modification That Renders a Primary, Neutralization-Resistant Clade B Human Immunodeficiency Virus Type 1 Isolate Highly Susceptible to Neutralization by Sera from Other Clades. J. Virol., 72:7840-7845, 1998. PubMed ID: 9733820. Show all entries for this paper.

Tuen2005 Michael Tuen, Maria Luisa Visciano, Peter C. Chien, Jr., Sandra Cohen, Pei-de Chen, James Robinson, Yuxian He, Abraham Pinter, Miroslaw K Gorny, and Catarina E Hioe. Characterization of Antibodies that Inhibit HIV gp120 Antigen Processing and Presentation. Eur. J. Immunol., 35(9):2541-2551, Sep 2005. PubMed ID: 16106369. Show all entries for this paper.

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. Show all entries for this paper.

Visciano2008 Maria Luisa Visciano, Michael Tuen, Miroslaw K. Gorny, and Catarina E. Hioe. In Vivo Alteration of Humoral Responses to HIV-1 Envelope Glycoprotein gp120 by Antibodies to the CD4-Binding Site of gp120. Virology, 372(2):409-420, 15 Mar 2008. PubMed ID: 18054978. Show all entries for this paper.

Visciano2008a Maria Luisa Visciano, Michael Tuen, Pei-de Chen, and Catarina E. Hioe. Antibodies to the CD4-Binding Site of HIV-1 gp120 Suppress gp120-Specific CD4 T Cell Response while Enhancing Antibody Response. Infect. Agent. Cancer., 3:11, 2008. PubMed ID: 18638381. Show all entries for this paper.

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. Show all entries for this paper.

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. Show all entries for this paper.