Found 4 matching records:
Displaying record number 593
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record as JSON.
MAb ID |
D7324 |
HXB2 Location |
Env(497-511) DNA(7713..7757) |
Env Epitope Map
|
Author Location |
gp120(497-511) |
Research Contact |
Aalto BioReagents Ltd, Dublin, Ireland or Cliniqa Inc., Fallbrook, CA, USA |
Epitope |
APTKAKRRVVQREKR
|
Epitope Alignment
|
Subtype |
B |
Ab Type |
gp120 C5 |
Neutralizing |
no |
Species
(Isotype)
|
sheep |
Patient |
|
Immunogen |
vaccine |
Keywords |
antibody binding site, antibody generation, antibody interactions, assay or method development, binding affinity, mimics, structure, subtype comparisons, vaccine antigen design, variant cross-reactivity |
Vaccine Details
Notes
Showing 19 of
19 notes.
-
D7324: D7324 was used as a C5-binding antibody in a competition ELISA that was used to define the binding sites of newly-isolated mAbs.
Li2012
-
D7324: used to purify gp120.
Ho1991a
-
Database note: D7324: This antibody product is produced by first immunising sheep with a single synthetic peptide which has the amino acid sequence: APTKAKRRVVQREKR. This amino acid sequence corresponds to amino acid numbers 497-511 in the envelope gene gp120 protein of the BH-10 strain of HIV-1 (see Ratner, L. et al., Nature, 313, 277-284 (1985)). The antibodies are isolated from the sheep hyperimmune serum by affinity chromatography using the above specified synthetic peptide coupled to Sepharose.
(antibody generation)
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D7324: 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 D7324 was used to visualize binding op gp120 to CCR5 by flow cytometry. The association of gp120 and CCR5 was increased in the presence of sCD4 or miniCD4.
Martin2011
(mimics, binding affinity)
-
D7324: The antigenic structure of Gag-Env pseudovirions was characterized and it was shown that these particles can recapitulate native HIV virion epitope structures. D7324 did not bind Gag-Env pseudovirions, indicating maintenance of surface heterodimers, as the epitope for this Ab is not available on intact heterodimers. 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)
-
D7324: Unlike the MPER MAbs tested, D7324 did not show any Env-independent virus capture in the conventional or in the modified version of the virus capture assay.
Leaman2010
-
D7324: Binding of HLA peptide HA307-319 to gp120 was not influenced by pre-incubation of gp120 with D7324, indicating that this Ab does not completely occlude sequences/structures of the C5 gp120 region relevant for the C5 mimicry of the HLA activation domain.
Cadogan2008
(mimics)
-
D7324: Binding of gp120 in the presence or absence of CD4, or in the presence of synthetic miniproteins with HIV-1 gp120 binding surface of the CD4 receptor incorporated, were evaluated using D7324 Ab. Phenylalanine derivatives of the miniproteins were more capable of inducing a CCR5-binding conformation of gp120.
Stricher2008
-
D7324: 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. The identity of gp120SF162 purified by miniCD4 method was confirmed by D7324-binding. D7324 was also used to normalize the concentration of gp120SF162 envelopes for comparison between the miniCD4 affinity chromatography and a reference method. Binding of D7324 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 D7324 epitope.
Martin2008
(assay or method development, binding affinity)
-
D7324: This Ab was shown not to bind to clade C gp140 (97CN54).
Sheppard2007a
(variant cross-reactivity)
-
D7324: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication 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 F105, IgG1b12, 17b and 48d, 2G12 and 447-52D. Association rates of sCD4 and 17b were not changed, but dissociation rates were 3-fold slower for sCD4 and 14-fold slower for 17b. The kinetics of D7324 binding were tested as a control, and were unchanged.
Martin-Garcia2005
(antibody binding site)
-
D7324: IgG antibody phage display libraries were created from HIV-1+ individuals after pre-selection of PBMC with gp120, as an alternative to using bone marrow for generating libraries. D7324 was among a set of Abs used for competition studies to define the binding sites of the newly isolated MAbs, representing a MAb with a C5 epitope.
Koefoed2005
(antibody binding site)
-
D7324: 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. D7324 bound to clade A, B, C, D and F HIV-1 primary isolates, but not to the group O protein. 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)
-
D7324: 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. This is a C5-binding polyclonal Ab that had no impact on 4KG5 binding.
Zwick2003a
(antibody interactions)
-
D7324: Used to capture gp120 onto solid phase for epitope mapping.
Moore1993b,Moore1993c,Ditzel1997,Binley1998,Basmaciogullar2002,Sanders2002,Xiang2002b,Herrera2003,Poignard2003
-
D7324: Gp120 capture ELISAs with MAbs D7324 (anti-C-term) or 9205 (anti-V3) were compared in a study of orientation of glycosylation sites -- CD4 binding could only inhibit deglycosylation when gp120 was bound to the plate by D7324, not by 9205, while Abs from HIV-1 infected people inhibited deglycosylation most effectively when gp120 was caught by 9205.
Gram2002
-
D7324: Epitope in C5 -- Does not neutralize JR-FL nor block gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study.
Trkola1996b
-
D7324: Binds to the last 15 amino acids in gp120 -- used for antigen capture ELISA.
Wyatt1995
-
D7324: Binding unaltered by gp120 binding to sCD4, in contrast to 110.5, 9284, 50-69 and 98-6.
Sattentau1991
References
Showing 29 of
29 references.
Basmaciogullar2002
Stéphane Basmaciogullari, Gregory J. Babcock, Donald Van Ryk, Woj Wojtowicz, and Joseph Sodroski. Identification of Conserved and Variable Structures in the Human Immunodeficiency Virus gp120 Glycoprotein of Importance for CXCR4 Binding. J. Virol., 76(21):10791-800, Nov 2002. PubMed ID: 12368322.
Show all entries for this paper.
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.
Show all entries for this paper.
Cadogan2008
Martin Cadogan, Brian Austen, Jonathan L. Heeney, and Angus G. Dalgleish. HLA Homology within the C5 Domain Promotes Peptide Binding by HIV Type 1 gp120. AIDS Res. Hum. Retroviruses, 24(6):845-855, Jun 2008. PubMed ID: 18544021.
Show all entries for this paper.
Ditzel1997
H. J. Ditzel, P. W. Parren, J. M. Binley, J. Sodroski, J. P. Moore, C. F. Barbas, III, and D. R. Burton. Mapping the Protein Surface of Human Immunodeficiency Virus Type 1 gp120 Using Human Monoclonal Antibodies from Phage Display Libraries. J. Mol. Biol., 267:684-695, 1997. (Genbank: U82767 U82768 U82769 U82770 U82771 U82772 U82942 U82943 U82944 U82945 U82946 U82947 U82948 U82949 U82950 U82951 U82952 U82961 U82962) Recombinant monoclonal antibodies from phage display libraries provide a method for Env surface epitope mapping. Diverse epitopes are accessed by presenting gp120 to the library in different forms, such as sequential masking of epitopes with existing MAbs or sCD4 prior to selection or by selection on peptides. Fabs identified by these methods have specificities associated with epitopes presented poorly on native multimeric envelope. PubMed ID: 9126846.
Show all entries for this paper.
Gram2002
G. J. Gram, A. Bolmstedt, K. Schonning, M. Biller, J.-E. S. Hansen, and S. Olofsson. Detection of Orientation-Specific Anti-gp120 Antibodies by a New N-Glycanase Protection Assay. APMIS, 110(2):123-131, Feb 2002. PubMed ID: 12064867.
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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.
Show all entries for this paper.
Hicar2010
Mark D. Hicar, Xuemin Chen, Bryan Briney, Jason Hammonds, Jaang-Jiun Wang, Spyros Kalams, Paul W. Spearman, and James E. Crowe, Jr. Pseudovirion Particles Bearing Native HIV Envelope Trimers Facilitate a Novel Method for Generating Human Neutralizing Monoclonal Antibodies Against HIV. J. Acquir. Immune Defic. Syndr., 54(3):223-235, Jul 2010. PubMed ID: 20531016.
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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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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.
Show all entries for this paper.
Koefoed2005
Klaus Koefoed, Lauge Farnaes, Meng Wang, Arne Svejgaard, Dennis R. Burton, and Henrik J. Ditzel. Molecular Characterization of the Circulating Anti-HIV-1 gp120-Specific B Cell Repertoire using Antibody Phage Display Libraries Generated from Pre-Selected HIV-1 gp120 Binding PBLs. J. Immunol. Methods, 297(1-2):187-201, Feb 2005. PubMed ID: 15777942.
Show all entries for this paper.
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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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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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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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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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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Moore1990b
J. P. Moore. Simple Methods for Monitoring HIV-1 and HIV-2 gp120 Binding to Soluble CD4 by Enzyme-Linked Immunosorbent Assay: HIV-2 Has a 25-Fold Lower Affinity Than HIV-1 for Soluble CD4. AIDS NY, 4:297, 1990. PubMed ID: 2190604.
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Moore1993b
J. P. Moore, Q. J. Sattentau, H. Yoshiyama, M. Thali, M. Charles, N. Sullivan, S.-W. Poon, M. S. Fung, F. Traincard, M. Pinkus, G. Robey, J. E. Robinson, D. D. Ho, and J. Sodroski. Probing the Structure of the V2 Domain of Human Immunodeficiency Virus Type 1 Surface Glycoprotein gp120 with a Panel of Eight Monoclonal Antibodies: Human Immune Response to the V1 and V2 domains. J. Virol., 67:6136-6151, 1993. PubMed ID: 7690418.
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Moore1993c
J. P. Moore, M. Thali, B. A. Jameson, F. Vignaux, G. K. Lewis, S.-W. Poon, M. S. Fung, P. J. Durda, L. Akerblom, B. Wahren, D. D. Ho, Q. J. Sattentau, and J. Sodroski. Immunochemical Analysis of the gp120 Surface Glycoprotein of Human Immunodeficiency Virus Type 1: Probing the Structure of the C4 and V4 Domains and the Interaction of the C4 Domain with the V3 Loop. J. Virol., 73:4785-4796, 1993. General observations: C4 and V3 MAbs are sensitive to the way the epitopes are presented, and this sensitivity cannot be correlated to peptide binding. Some V3-C4 domain interaction was indicated based on mutation and interference studies. PubMed ID: 7687303.
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Poignard2003
Pascal Poignard, Maxime Moulard, Edwin Golez, Veronique Vivona, Michael Franti, Sara Venturini, Meng Wang, Paul W. H. I. Parren, and Dennis R. Burton. Heterogeneity of Envelope Molecules Expressed on Primary Human Immunodeficiency Virus Type 1 Particles as Probed by the Binding of Neutralizing and Nonneutralizing Antibodies. J. Virol., 77(1):353-365, Jan 2003. PubMed ID: 12477840.
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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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Sattentau1991
Q. J. Sattentau and J. P. Moore. Conformational Changes Induced in the Human Immunodeficiency Virus Envelope Glycoprotein by Soluble CD4 Binding. J. Exp. Med., 174:407-415, 1991. sCD4 binding to gp120 induces conformational changes within envelope oligomers. This was measured on HIV-1-infected cells by the increased binding of gp120/V3 loop specific MAbs, and on the surface of virions by increased cleavage of the V3 loop by an exogenous proteinase. PubMed ID: 1713252.
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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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Stricher2008
François Stricher, Chih-chin Huang, Anne Descours, Sophie Duquesnoy, Olivier Combes, Julie M. Decker, Young Do Kwon, Paolo Lusso, George M. Shaw, Claudio Vita, Peter D. Kwong, and Loïc Martin. Combinatorial Optimization of a CD4-Mimetic Miniprotein and Cocrystal Structures with HIV-1 gp120 Envelope Glycoprotein. J. Mol. Biol., 382(2):510-524, 3 Oct 2008. PubMed ID: 18619974.
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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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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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Wyatt1995
R. Wyatt, J. Moore, M. Accola, E. Desjardin, J. Robinson, and J. Sodroski. Involvement of the V1/V2 Variable Loop Structure in the Exposure of Human Immunodeficiency Virus Type 1 gp120 Epitopes Induced by Receptor Binding. J. Virol., 69:5723-5733, 1995. Deletions in the V1/V2 loops of gp120 resulted in the loss of the ability of sCD4 to induce binding of the MAbs 17b, 48d, and A32. A32 can induce binding of 17b and 48d; this induction does not appear to involve the V1/V2 regions. PubMed ID: 7543586.
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Xiang2002b
Shi-Hua Xiang, Najah Doka, Rabeéea K. Choudhary, Joseph Sodroski, and James E. Robinson. Characterization of CD4-Induced Epitopes on the HIV Type 1 gp120 Envelope Glycoprotein Recognized by Neutralizing Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 18(16):1207-1217, 1 Nov 2002. PubMed ID: 12487827.
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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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Displaying record number 631
Download this epitope
record as JSON.
MAb ID |
F105 (F-105) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
Marshall Posner, Boston MA |
Epitope |
(Discontinuous epitope)
|
Ab Type |
gp120 CD4bs |
Neutralizing |
L View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human(IgG1κ) |
Patient |
|
Immunogen |
HIV-1 infection |
Keywords |
adjuvant comparison, antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody polyreactivity, antibody sequence, assay or method development, autologous responses, binding affinity, brain/CSF, chimeric antibody, co-receptor, complement, computational prediction, dendritic cells, effector function, enhancing activity, escape, genital and mucosal immunity, glycosylation, HAART, ART, immunoprophylaxis, immunotherapy, immunotoxin, isotype switch, kinetics, mimics, mother-to-infant transmission, neutralization, polyclonal antibodies, rate of progression, review, SIV, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity |
Notes
Showing 181 of
181 notes.
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F105: 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)
-
F105: Membrane-bound mRNA-encoded BG505-based Apex GT Env trimer vaccine candidates, which bind to inferred germline variants of bnAbs PCT64 and PG9, were developed through directed evolution and characterized. All assessed ApexGT constructs, as well as BG505 SOSIP.MD39 (background for Apex constructs), in soluble or membrane-bound forms (encoded by DNA or RNA), had generally similar antigenic profiles and had absent to low binding to mAb F105.
Willis2022
(antibody binding site)
-
F105: 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)
-
F105: Reduction in exposure of non-neutralizing Ab (nnAb) epitopes on native-like Env trimer immunogens results in bnAbs being elicited that have autologous tier 2 neutralization instead of tier 1. The design of trimer modifications to silence nnAb reactivity were directed towards (1) the V3 loop (2) epitopes exposed through CD4-induced conformational changes (CD4i epitopes) and (3) the exposed SOSIP trimer base that is usually buried within virus membrane. (1) In Steichen2016 2 Env variants of BG505 SOSIP.664 with reduced V3 nnAb-generating activity were created, one using mammalian display screens, BG505 MD39, and the other with an engineered disulfide bond, BG505 SOSIP.DS21. MD39's trimer design was improved by using the Rosetta Design platform and inserting 6 buried mutations to form BG505 Olio6, and both this trimer as well as the DS21 were shown to have reduced antigenicity for nnAb generation in a rabbit vaccine model. (2) To reduce CD4i epitope elicitation of nnAbs, saturation mutagenesis of Olio6 was performed, in search of the trimer that binds VRC01-class bnAbs but not CD4. BG505 Olio6.CD4KO containing the G473T mutation was identified. In addition, for the purposes of nucleic acid-based vaccine platform designs, the natural furin cleavage site between gp120 and gp41 was removed to abolish protease cleavage, by swapping the order of gp14 and gp120 in the gp160 gene, giving the trimer BG505 MD39.CP (circular permutation). (3) The exposed trimer base was masked with glycan in 3 under-glycosylated regions in order to direct bnAb responses to the distal regions (CD4bs, V2 apex, N332 superset) of the trimer instead, generating the GRSF (glycan resurfaced) MD39 and GRSF MD39.CP variants. Furthermore, variants with improved thermostability over MD39 were created, MD37 and MD64. All of these stabilizing mutations were transferred to diverse HIV isolates from different subtypes. Finally 3 subtype C (isolate 327c) trimers were assessed for binding to bnAbs, VRC01, PGT121, PGT151, PGT145, PG9 and to nnAbs, F105 and 17b - F105 did not bind to any of these. nnAb F105 discriminates between non-native and native trimers by binding non-native subtype B Env immunogens like AD8 SOSIP and not native AD8 MD64.
Kulp2017
(antibody binding site, antibody generation, antibody interactions, assay or method development, autologous responses, vaccine antigen design, structure)
-
F105: 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. Before V3-negative selection, mAb F105 recognized DS-SOSIP and BG505 SOSIP.664 but failed to recognize 4mut or the other 3 designed trimers (DS-SOSIP.6mut containing 4mut mutations, Y177W and I420M, DS-SOSIP.I423F and DS-SOSIP.A316W). After V3-negative selection, F105 also failed to recognize DS-SOSIP and BG505 SOSIP.664. 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)
-
F105: Using subtype A BG505 Env structural information, improved variants of subtype B JRFL and subtype C 16055 Env native flexibly linked (NFL) trimers were generated. The trimer-derived (TD) residues that increased well-ordered, homogeneous, stable, and soluble trimers did not require positive or negative selection as previously needed [Guenaga2015, PLoS Pathos. 11(1):e1004570]. ELISA binding to the two CD4bs-targeting nnAbs, F105 and b6 was inefficient as desired, for the NFL TD as well as NFL TD CC (disulfide link stabilized) trimers, indicating that these trimers were probably in the desired, closed conformation.
Guenaga2015a
(antibody interactions, assay or method development, vaccine antigen design, structure)
-
F105: 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 only bound a single CD4 and remained in a prefusion closed conformation. CD4bs-targeting mAb F105 was author-defined as ineffective due to its neutralization breadth of 7.65% on a panel of 170 diverse HIV-1 pseudoviruses. This was consistent with structural modeling which suggested that F105 was incompatible with BG505 SOSIP.664 when considering antibody-antigen-volume overlap yet compatible when considering epitope r.m.s deviation. Some mutations that stabilized the closed prefusion state of BG505 SOSIP.664 increased F105 binding modestly to moderately, compared to the lack of binding seen with wildtype SOSIP.664. Soluble CD4 did not have an effect on F105 binding of Env trimers.
Kwon2015
(neutralization, vaccine antigen design, structure)
-
F105: Cryo-electron microscopy (EM) of the cleaved, soluble SOSIP gp140 trimer complexed with CD4bs-binding bnAb PGV04 was studied at 5.8Å, facilitating study of Env V1/V2, V3, HR1 and HR2 domains and some shielding glycans. This provides further information on trimer assembly, gp120-gp41 interactions and the three-dimensional CD4bs epitope cluster. For instance, bnAb F105, like b13, does not neutralize the BG505 virus or bind trimer BG505 SOSIP.664 - it has extensive clashes with V1/V2 (same protomer), glycans, and V3 from the adjacent protomer, which differs from another CD4bs bnAbs that also does not neutralize BG505, b12, but which has minimal clashing with these regions of the Env trimer.
Lyumkis2013
(vaccine antigen design, structure)
-
F105: 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. CD4bs-binding, non-nAb F105 inefficiently recognized the negatively selected trimers.
Guenaga2015
(vaccine antigen design, subtype comparisons, structure)
-
F105: 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)
-
F105: 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)
-
F105: To understand early bnAb responses, 51 HIV-1 clade C infected infants were assayed for neutralization of a 12-virus multi-clade panel. Plasma bnAbs targeting V2-apex on Env were predominant in infant elite and broad neutralizers. In infant elite neutralizers, multi-variant infection was associated with plasma bnAbs targeting diverse autologous viruses. A panel of mAbs (PG9, PG16, PGT145, PGDM1400, VRC26.25, 10-1074, BG18, AIIMS-P01, PGT121, PGT128, PGT135, VRC01, N6, 3BNC117, PGT151, 35O22, 10E8, 4E10, F105, 17b, A32, 48d, b6, 447-52d) was assayed for their ability to neutralize Env clones from infant elite neutralizers; circulating viral variants in infant elite neutralizers were most susceptible to V2-apex bnAbs.
Mishra2020a
(neutralization, polyclonal antibodies)
-
F105: 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. The CD4bs Ab F105 exhibited poor neutralization against HIV-1AD8 full-length and cytoplasmic tail-deleted Envs.
Castillo-Menendez2019
(vaccine antigen design, structure)
-
F105: 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)
-
F105: 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. State 2/3 preferring ligand F105 recognized L193A variants of CH58 and CH77 IMCs with a significant increase compared to the WT.
Prevost2018
(effector function)
-
F105: 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)
-
F105: 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 F105 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)
-
F105: This study reports host tolerance mechanisms that limit the development of CD4bs and HCDR3-binder bNAbs via sequential HIV-1 Env vaccination. Vaccine-induced macaque CD4bs bNAbs recognize open Env trimers, and accumulate relatively modest somatic mutations. In naive CD4bs, unmutated common ancestor knock-in mice Env + B cell clones develop anergy and partial deletion at the transitional to mature B cell stage, but become Env- upon receptor editing. Stepwise immunization initiates CD4bs-bNAb responses, but immune tolerance mechanisms restrict their development. The Val-Phe-Tyr hydrophobic tip of the F105 HCDR3 was reported to interact with the same hydrophobic pocket on gp120 (PDB: 3HI1).
Williams2017a
(glycosylation, structure, antibody lineage, chimeric antibody)
-
F105: 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)
-
F105: This study performed cyclical permutation of the V1 loop of JRFL in order to develop better gp120 trimers to elicit neutralizing antibodies. Some mutated trimers showed improved binding to several mAbs, including VRC01, VRC03, VRC-PG04, PGT128, PGT145, PGDM1400, b6, and F105. Guinea pigs immunized with prospective trimers showed improved neutralization of a panel of HIV-1 pseudoviruses.
Kesavardhana2017
(vaccine antigen design, vaccine-induced immune responses)
-
F105: 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. N197 glycan mutants were tested against F105 showing a loss of tier 2 phenotype. The results are in Table S5.
Crooks2015
(glycosylation, neutralization)
-
F105: 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)
-
F105: PGT145 was used to positively isolate a subtype B Env trimer immunogen, B41 SOSIP.664, 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. Among non-nAbs to CD4bs (b6, F91, F105); to CD4i (17b); to gp41ECTO (F240); and to V3 (447-52D, 39F, CO11, 19b and 14e), none neutralized B41 (IC50 >50µg/ml).
Pugach2015
-
F105: Two clade C recombinant Env glycoprotein trimers, DU422 and ZM197M, with native-like structural and antigenic properties involving epitopes against 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 have no affinity for the CD4bs non-nAb, F105, and F105 was unable to neutralize the equivalent pseudotyped viruses for either trimer.
Julien2015
(assay or method development, structure)
-
F105: 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. Anti-CD4bs epitope, non-nAb F105 showed reduced binding to cross-linked trimers.
Schiffner2016
(assay or method development, binding affinity, structure)
-
F105: 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 F105 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)
-
F105: This study examined the development and co-evolution of autologous antibodies and viruses in two patients. Antibodies with limited heterologous breadth were able to potently neutralize autologous viruses, and such antibodies could select for neutralization-resistant autologous viruses implicated in transmission. Viruses from subject CH0457 were largely susceptible to neutralization by CD4bs-binding heterologous nAbs CH31 and CH106. The CD4bs CH27 lineage mAbs from subject CH0457 were similar to HJ16, which neutralizes multiple tier 2 but not tier 1 viruses. Narrow neutralizing CD4bs mAb F105 weakly neturalized 2.8% of an 84-psuedoviral panel amplified from CH0457.
Moody2015
(neutralization)
-
F105: CD4-binding site Abs are reviewed. New insights from donor-serum responses, atomic-level structures of antibody-Env complexes, and next-generation sequencing of B-cell transcripts are invigorating vaccine-design efforts to elicit effective CD4-binding site Abs. Analysis of the epitopes recognized by CD4-binding Abs reveals substantial similarity in the recognized region of gp120. The non-potent F105 induces conformations of the bridging sheet which is incompatible with the functional viral spike.
Georgiev2013a
(review)
-
F105: 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-Abs, including F105, against 181 diverse HIV-1 strains with available Ab-Ag complex structures
Chuang2013
(computational prediction)
-
F105: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. F105 is discussed as the CD4bs-targeting, neutralizing anti-gp120 mAb exhibiting ADCC activity and having a discontinuous epitope.
Pollara2013
(effector function, review)
-
F105: Systematic computational analyses of gp120 plasticity and conformational transition in complexes with CD4 binding fragments, mimetic proteins and Ab fragments are described to explain the molecular mechanisms by which gp120 interacts with the CD4bs at local and subdomain levels. An isotopic elastic network analysis, a full atomic normal mode analysis and simulation of conformational transitions were used to compare the gp120 structures in CD4 bound and F105 Ab-bound states.
Korkut2012
(structure)
-
F105: 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. F105 was used as a CD4bs mAb to compare neutralizing specificity of VRC06.
Li2012
-
F105: 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. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on F105.
Klein2013
(neutralization, structure, antibody lineage)
-
F105: 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. HIV-1 has developed steric constraints on the Abs binding to CD4BS. Role of F105 has been discussed as a CD4BS binding Ab. The sensitivity of HIV-1 to F105 was enhanced by the altered gp41, J1Hx(66, 197).
Haim2011
(antibody interactions)
-
F105: 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. F105 was used as a Non-bNAb which was similar in function to non human primates mAbs.
Sundling2012
(vaccine-induced immune responses)
-
F105: Crystal structures of unliganded core gp120 from HIV-1 clade B, C, and E were determined to understand the mechanism of CD4 binding capacity of unliganded HIV-1. The results suggest that the CD4 bound conformation represents "a ground state" for the gp120 core with variable loop. F105 was used as a control to prove whether the purified and crystallized gp120 is in the CD4 bound conformational state or not.
Kwon2012
(structure)
-
F105: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. F105 has been mentioned to describe the sites of HIV-1 vulnerability to neutralizing antibody.
Kwong2011
(antibody binding site, neutralization, vaccine antigen design, review)
-
F105: 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. F105 was used as a control to compare the neutralizing activity of patients' sera.
Lavine2012
(neutralization)
-
F105: 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)
-
F105: 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. F105 bound very strongly to the gp120 core but did not bind to the gp120 core D368R, RSC3, RSC3/G367R, RSC3 Δ3711, and RSC3 Δ3711/P363N.
Lynch2012
(binding affinity)
-
F105: The strategy of incorporating extra glycans onto gp120 was explored, with the goal to occlude the epitopes of non-neutralizing mAbs while maintaining exposure of the b12 site. The focus was on the head-to-head comparison of the ability of 2 adjuvants, monophosphoryl lipid A (MPL) and Quil A, to promote CD4-specific Ab responses in mice immunized with the engineered mutant Q105N compared to gp120wt. Neutralizing and non-neutralizing antibodies targeting three areas on gp120 – the CD4bs (F105, b6, b12, b13, VRC01, VRC03 and CD4- IgG2), the glycosylated ‘silent face’ (2G12) and the V3 loop (B4e8) – were assessed for binding. The antibodies b6, b12, b13, VRC01 and 2G12 bound best to mutant Q105N, albeit with lower affinities than to gp120wt. Retention of b6 and b13 binding was not expected, but can be explained by their very similar mode of interaction with the CD4bs compared to b12. Abs F105 and VRC03 did not bind Q105N at all. The V3-specific antibody B4e8 did not bind to Q105N.
Ahmed2012
(adjuvant comparison, antibody binding site, glycosylation, neutralization, escape)
-
F105: gp120 was cyclically permuted and new N- and C-termini were created within the V1, V3, and V4 loop regions to reduce the length of the linker joining gp120 and M9. The cyclic permutant V1cyc were used to incorporate the trimerization domains. In contrast to monomeric gp120, h-CMP-V1cyc (a covalently linked trimer) interacted with similar affinities to both b12 and F105. SUMO2a-V1cyc (a mixture of a trimer, a dimer, and a monomer) binds approximately 5-10-fold weaker than gp120 to b12 and F105. Monomeric and both trimeric versions of V1cyc bound less well to F105 than wt-gp120. It has been shown that V1 cyclic permutants of gp120 with an appropriate trimerization domain can fold into a conformation that shows poorer affinity for F105 relative to gp120.
Saha2012
(binding affinity)
-
F105: Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies was studied by isolation of VRC01-like neutralizers with CD4bs probe; structural definition of gp120 recognition by RSC3-identified antibodies from different donors; functional complementation of heavy and light chains among VRC01-like antibodies; identification of VRC01 antibodies by 454 pyrosequencing; and cross-donor phylogenetic analysis of sequences derived from the same precursor germline gene. F105 had 37-69% sequence identity of its heavy and light chains to respective chains of VRC-PG04 and VRC-CH31.
Wu2011
(structure)
-
F105: A strategy is described for eliciting antibodies in mice against selected cryptic, conformationally dependent conserved epitopes of gp120 by immunizing with multiple identical copies of covalently linked multiple copy peptides (MCPs) representing 3 different domains of gp120. MAb F105 bound to oligomeric gp120 on cells infected with viruses from clade B with similar affinity as mAb 11A8 but with a very low affinity from clade A and D.
Kelker2010
(binding affinity)
-
F105: 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)
-
F105: 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. F105 was classified into CD4BS group as it interferes with CD4 binding site. The number of F105 Abs needed to neutralize a single trimer was determined to equal 1.
Magnus2010
-
F105: Unlike the MPER mAbs tested, F105 did not show any Env-independent virus capture. MAb competition assays revealed that F105 did not compete with b12 or b6 for virion capture.
Leaman2010
-
F105: Impact of in vivo Env-CD4 interactions was studied during vaccinations of Rhesus macaques with two Env trimer variants rendered CD4 binding defective (368D/R and 423/425/431 trimers) and wild-type (WT) trimers. Ab binding profiles of the three trimer variants were assessed by binding analyses to different MAbs. CD4bs-directed mAb F105 bound similarly to WT and 423/425/431 trimers but did not bind to 368D/R trimers.
Douagi2010
(binding affinity)
-
F105: Expression of gp120 was shown to lead to the accumulation of both monomeric gp120 and aberrant dimeric gp120 forms. Dimeric forms of gp120 were recognized by CD4BS mAbs, such as F105, but were not recognized by CD4i MAbs or MAbs to the gp120 inner domain. It is suggested that gp120 dimerization occludes or disrupts the inner domain and/or the co-receptor binding site. Formation of gp120 dimers was reduced by removal of the V1/V2 loops or the N and C termini.
Finzi2010
(antibody binding site)
-
F105: Crystal structure of the D7 llama heavy chain antibody fragment V(HH) was resolved and compared to other CD4bs Abs (b12, b13, F105 and m18). Unlike for F105, CDR2 of D7 did not have aromatic residues at the tip and does not play a prominent role in gp120 interactions. As F105 and the other CD4bs Abs, D7 had aromatic residues at the tip of its CDR3. Other than that, there was no significant structural homology between D7 and other CD4bs Ab loops, underlining the differences in mode of gp120 interaction.
Hinz2010
(structure)
-
F105: 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. F105 bound better to the ΔV1V2 variants than to the full-length trimer, indicating better exposure of F105 epitope when the V1V2 domain is removed.
Bontjer2010
(binding affinity)
-
F105: An outer domain (ODec) based immunogen including the whole outer domain and most of the CD4 binding residues was designed and expressed in E-coli bacterial cells. The ODec lacked V1V2 and V3, incorporated 11 designed mutations at the interface of the inner and outer domains of gp120, and was unglycosylated. F105 bound to monomeric gp120 but did not bind to ODec. Structural analyses showed that 5/10 residues required for F105 binding were absent in the ODec construct. Sera from rabbits immunized with ODec neutralized 4/5 clade B and 1/2 clade C viruses.
Bhattacharyya2010
(kinetics, binding affinity)
-
F105: 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. F105 bound with high affinity to non-CD4-bound gp120 but not to CD4-bound conformation. F105 covered 79% of the contact site for CD4 receptor on gp120, its heavy chain contacting CDR1, CDR2 and CDR3 regions. The number of mutations from the germline and the number of mutated contact residues for F105 were smaller than those for VRC01. Unlike VRC01, variation of V5 conformation of gp120 with F105 spanned over the whole range of V5.
Zhou2010
(antibody binding site, neutralization, binding affinity, structure)
-
F105: 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 F105. Memory B cells were selected that bound to RSC3 and full IgG mAbs were expressed. Three newly detected mAbs (VRC1, VRC2 and VRC3) competed with F105 for binding to gp120. Addition of RSC3 had no effect on F105 neutralization of HXB2.
Wu2010
(antibody interactions, neutralization, binding affinity)
-
F105: 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 F105.
Wu2009a
(binding affinity)
-
F105: A panel of clade B and C viruses from early infections was used to analyze F105 neutralization resistance. Removal of a glycan at position 301 at the base of the V3 loop rendered PVO.4 strain sensitive to neutralization by F105. In addition, point mutations T569A and I675V in the gp41 region increased viral neutralization sensitivity to F105, indicating their effect on viral spike accessibility.
Wu2009
(glycosylation, neutralization)
-
F105: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:4-59*01, IGHD:4-17, D-RF:2, 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)
-
F105: The Fab' fragment of F105 was linked to sterically stabilized pegylated liposomes containing a protease inhibitor. The complex was specifically taken up by HIV-1 infected cells, indicating preservation of F105 specific binding after conjugation and incorporation into liposomes. The inhibitor that was derived intracellularly by F105-liposome complex showed greater and longer antiviral activity than the free drug, indicating that F105 can be used in targeted delivery of antiretroviral compounds.
Clayton2009
(HAART, ART)
-
F105: IgG and Fab F105 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 compared to CD4, 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 F105, suggesting that F105 relies on access to the hydrophobic surface for binding. Structure analyses revealed that F105, and other CD4BS Abs that access this hydrophobic region, induce conformation changes in gp120 that are poorly compatible with functional viral spike. F105 was not able to bind to cleavage-defective envelope glycoproteins.
Chen2009
(antibody binding site, neutralization, kinetics, binding affinity, structure)
-
F105: F105 neutralized infection of PBLs with various HIV-1 strains. However, F105 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells, in contrast, it somewhat increased the passage of cell-free HIV-1 through the epithelial cells. A mixture of 13 mAbs directed to well-defined epitopes of the HIV-1 envelope, including F105, 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
(enhancing activity, neutralization)
-
F105: 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. F105 MAb bound gp120 of the IIIB wild type virus 8- to 16-fold better than gp120 of the 89.6 wild type. Deletion of loop C resulted in greater than 100-fold increase in F105 binding to 89.6 gp120. Deletions of loops A, D or three amino acids in loop E resulted in gp120 mutants that failed to bind F105.
Berkower2008
(antibody binding site, binding affinity)
-
F105: 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 F105-gp120 interaction, but the CNV alone did not, indicating that the chimera has the high affinity binding property of the CNV molecule and the inhibitory property of the 12p1 peptide.
McFadden2007
-
F105: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. F105 neutralization properties 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, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed.
Phogat2007
(review)
-
F105: F105 structure, binding and neutralization are reviewed in detail. Molecules designed to eliminate binding by F105 while preserving epitopes of other neutralizing Abs are discussed.
Lin2007
(review, structure)
-
F105: This review summarizes F105 Ab epitope, properties and neutralization activity. F105 use in passive immunization studies in primates and possible mechanisms explaining protection against infection are discussed.
Kramer2007
(immunotherapy, review)
-
F105: gp120 proteins with double mutation T257S+S375W, which alters the cavity at the epicenter of the CD4 binding region, decreased F105 recognition to an undetectable level. The S375W single mutation also disrupted the binding surface of the F105 Ab.
Dey2007a
(binding affinity)
-
F105: A significantly higher level of anti-V3 Ab (694/98D) and anti-C1 mAb (EH21) bound to gp120 complexed with F105 mAb than to gp120 alone or in complex with other non-CD4bs Abs, indicating that binding of F105 to gp120 increases exposure of specific V3 and C1 mAb epitopes.
Visciano2008
-
F105: 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. All high affinity peptides inhibited the interactions of YU2 gp120 with F105 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
-
F105: F105 was tested for its ability to induce conformational changes similar to those induced by CD4. Although presence of sCD4 increased neutralization of JRFL by 447-52D and immune sera rich in V3-Abs from guinea pigs, the presence of F105 did not, indicating that F105 does not induce a conformation alternation in Env that exposes the V3 loop to neutralizing Abs.
Wu2008
-
F105: Neutralization of HIV-1 IIIB LAV isolate by F105 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)
-
F105: 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 generally more sensitive to neutralization by F105 than the adapted KB9 variants. All of the NL4-3 exhibited similar sensitivity to neutralization by F105 except for the viruses containing the V242I change, which exhibited a slight increase in neutralization sensitivity to F105. Wildtype KB9 is resistant to neutralization by F105 but the changes associated with adaptation to marmoset receptors resulted in variants with increased sensitivity to neutralization by F105. Thus, adaptation to marmoset receptors resulted in an increase in sensitivity to neutralization by F105 for KB9 but not for NL4-3.
Pacheco2008
(neutralization)
-
F105: 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 F105 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 an intact F105 epitope. gp140DF162ΔV2 was purified by the miniCD4 method to assess its ability to capture gp140 trimers. Binding of F105 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)
-
F105: 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. IgG eluted from gp120 wildtype and core protein from the sera were reabsorbed with the gp120-D368R mutant protein to remove non-CD4-binding site Abs. Binding of the resulting flow-through core eluate/368ft IgG to gp120 was completely blocked by Fab F105. Fab F105 also blocked most of the binding of the gp120WT eluate/368ft IgG, indicating that these Ab fractions were highly enriched with CD4-binding site Abs.
Li2007a
(neutralization)
-
F105: A recombinant gp120-Fc, used in an assay to determine 2G12 epitope contribution to DC-SIGN binding to gp120, bound to F105, indicating it was conformationally intact.
Hong2007
(binding affinity)
-
F105: 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 F105 compared to wildtype. Also, there was no association between increased sensitivity to F105 neutralization and enhanced macrophage tropism.
Dunfee2007
(neutralization)
-
F105: The crystal structure of this Ab was compared to the high resolution crystal structure of Fab m18. Although the variable domains of m18 and F105 showed sequence similarity, the H3s of these Abs showed distinct conformations. Similarly, the H2s conformations of these Abs differed.
Prabakaran2006
(antibody binding site, mimics, antibody sequence, structure)
-
F105: This Ab was used to determine the degree to which fixation of gp120 in its CD4-bound conformation restricts antigenic recognition. F105 was not able to bind well to the stabilized gp120.
Zhou2007
-
F105: F105 bound exclusively to cells expressing gp120 in a co-receptor-independent manner. Although binding and uptake of F105 was increased with increased expression of gp120 on the cell surface, efficient internalization in short amount of time was possible even in cells expressing low levels of gp120. Internalized F105 was localized to the Golgi compartment. Kinetic analyses of F105 binding to gp120 demonstrated a heterogeneous mode of binding that did not trigger a conformational change in the formed complex. Compared to sCD4, F105 had a higher gp120 affinity, due to slower dissociation.
Clayton2007
(co-receptor, kinetics, binding affinity)
-
F105: Compared to the full-length Con-S gp160, chimeric VLPs containing Con-S ΔCFI gp145 with transmembrane (TM) and cytoplasmic tail (CT) sequences derived from the mouse mammary tumor virus (MMTV), showed higher binding capacity to F105. Chimeric VLPs with only CT derived from MMTV also showed higher binding capacity to F105 than the full-length Con-S gp160, however, not as high as the chimeric CT-TM VLPs.
Wang2007a
(binding affinity)
-
F105: This Ab was used to select phages from two different peptide libraries. Synthetic peptides corresponding to the selected phage sequences showed slight inhibition of F105 binding to gp120. F105 did not bind to synthetic peptides to 5145A MAb fused to phage pIII protein. Sera from rabbits immunized with 5145A peptide-phage pIII protein did not inhibit binding of F105 to gp120.
Wilkinson2007
(antibody polyreactivity)
-
F105: 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 more neutralization sensitive to F105 than Ch2, which did not contain any of these mutations. Neutralization sensitivity to F105 by Env-pseudotyped viruses containing D457G mutation alone, or in combination with E440G or H564N, was unaffected compared to mutants lacking this mutation. Binding of F105 to gp120 derived from Env-pseudotyped viruses was unaffected by any of these mutations.
Beddows2005a
(neutralization, binding affinity)
-
F105: All clones derived from biopanning using IgG1b12 bound to this Ab but not to the control Ab F105.
Dorgham2005
(antibody binding site)
-
F105: 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. F105 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)
-
F105: 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 F105, modified protein 3G (mutations in 3 glycosylation sites) showed the highest binding to this Ab compared to the other Env proteins.
Kang2005
(antibody binding site, binding affinity)
-
F105: A stable trimerization motif, GCN4, was appended to the C terminus of YU2gp120 to obtain stable gp120 trimers (gp120-GCN4). Each trimer subunit was capable of binding IgG1b12, indicating that they were at least 85% active. D457V mutation in the CD4 binding site resulted in a decreased affinity of the gp120-GCN4 for CD4, but the mutation did not affect binding of F105. F105 was able to bind to both wildtype gp120, gp120-GCN4, and to the respective corresponding mutant molecules D457Vgp120 and D457Vgp120-GCN4.
Pancera2005a
(binding affinity)
-
F105: JR-FL and YU2 HIV-1 strains were not neutralized by F105. F105 and other non-neutralizing Abs only recognized JR-FL cleavage-defective glycoproteins, while the neutralizing Abs (2G12 and IgG1b12) recognized both cleavage competent and 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. F105, along with other Abs able to neutralize lab-adapted isolates, displayed enhanced viral entry at higher Ab concentrations, whereas the Abs that cannot neutralize any virus did not display such enhancement.
Pancera2005
(antibody binding site, enhancing activity, neutralization, binding affinity)
-
F105: 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, immunotherapy, mother-to-infant transmission, review)
-
F105: 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)
-
F105: 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 F105 to the glycoprotein indicating that the inter-S-S bonds had no impact on the exposure of F105 epitope.
Yuan2005
(antibody binding site)
-
F105: 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, variant cross-reactivity, immunotherapy, review)
-
F105: A chimeric cell surface receptor (105TCR) was designed consisting of the single chain Fv domain of F105, CD8α hinge and the transmembrane, and the cytoplasmic domains of TCRζ. 105TCR was successfully expressed on the surface of T-cells. It mediated full activation of T-cells leading to cytokine production when bound to gp120 on the surface of an infected cell. It did not bind to soluble gp120. Retrovirally transduced CD8+ cells expressed high levels of 105TCR and were able to lyse HIV-1 envelope expressing cells specifically in an MHC-unrestricted manner.
Masiero2005
(immunotherapy)
-
F105: A T-cell line adapted strain (TCLA) of CRF01_AE primary isolate DA5 (PI) was more neutralization sensitive to F105 than the primary isolate. Mutant virus derived from the CRF01_AE PI strain, that lacked N-linked glycosylation at position 197 in the C2 region of gp120, was significantly more sensitive to neutralization by F105 then the PI strain. Deglycosylated subtype B mutants at positions 197 and 234 were significantly more neutralizable by F105 than the parental strain.
Teeraputon2005
(antibody binding site, neutralization, subtype comparisons)
-
F105: 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). F105 bound to SF162gp140 but a deletion of V2 or V3 loops from the gp140 construct reduced the binding.
Derby2006
(antibody binding site)
-
F105: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs.
Holl2006
(neutralization, dendritic cells)
-
F105: The ability of F105 to neutralize R5, R5X4 and X4 primary isolates was compared to that of mAbs 17b, E51 and 412d. F105 neutralized the R5 ADA virus more efficiently than 17b, comparable to 412d, however, it neutralized R5X4 isolate 89.6 less efficiently than 412d and E51. F105 was, on the other hand, more efficient in neutralizing the X4 isolate HXBc2 than the other mAbs.
Choe2003
(neutralization)
-
F105: The crystal structure of the Fab fragment from F105 was solved. It has an extended CDR H3 loop, with a Phe at the apex that may recognize the binding pocket of gp120 used by the Phe-42 residue of CD4. The potent nAb IgG1b12 recognizes an overlapping binding site, the main difference is that F105 extends across the interface of the inner and outer domains of gp120 while b12 does not. IgG1b12 also has undergone extensive affinity maturation (45 mutations) while F105 has not (13 mutations) -- an average for gp120 mAbs is 22 mutations.
Wilkinson2005
(antibody sequence, structure)
-
F105: 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. CD4BS mAbs except Fab b12 (b6, b3, F105) did not bind to either GDMR or mCHO.
Selvarajah2005
(vaccine antigen design, vaccine-induced immune responses)
-
F105: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication 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)
-
F105: 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 F105.
Pantophlet2004
(vaccine antigen design)
-
F105: NAbs against HIV-1 M group isolates were tested for their ability to neutralize 6 randomly selected HIV-1 O group strains. F105 was not particularly effective at neutralizing HIV-1 group O strains.
Ferrantelli2004a
(variant cross-reactivity)
-
F105: 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 CD4BS mAb F105 was decreased by trypsin, but increased by thrombin. Thrombin may increase HIV-induced cell fusion in blood by causing a conformational activating shift in gp120.
Ling2004
(antibody binding site)
-
F105: A pseudotyping assay showed that an X4 V3 loop peptide could enhance infectivity of X4 virus, R5 and R5X4 V3 loops peptides could enhance infectivity of an R5 virus, and R5X4 peptides could enhance infectivity of an R5X4 virus. Neither R5 nor R5X4 peptides influenced binding of CD4BS mAbs F105 and Ig1Gb12, but did increase binding of CD4i mAb 17b.
Ling2002
(antibody binding site, co-receptor)
-
F105: 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 12p1 a promising lead for therapeutic design.
Biorn2004
-
F105: 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)
-
F105: 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)
-
F105: 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)
-
F105: 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. F105 recognized most variants, some from each of the four individuals by gp120 immunoprecipitation.
Ohagen2003
(brain/CSF, variant cross-reactivity)
-
F105: 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 and 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)
-
F105: 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 JR-FL and to CCR5 in a concentration dependent manner. 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.
Raja2003
(antibody binding site, co-receptor)
-
F105: 17b: This paper describes the generation of CD4i MAb E51, that like CD4i mAb 17b, blocks CCR5 binding to sCD4-bound gp120. The substitutions E381R, F383S, R419D I420R, K421D, Q422L, I423S, and Y435S (HXB2 numbering) all severely reduce 17b and E51 binding. All but I423S also diminish CCR5 binding by more than 50%. The mutation F383S also inhibits sCD4 binding and F105 binding, and K421D inhibits F105 binding, but not sCD4.
Xiang2003
(antibody binding site)
-
F105: 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 enhanced the binding of CD4BS MAbs IgG1b12 and F105 to both R5X4 and R5 isolates, but had no effect on neutralization. Anti-V3 MAb B4a1 increased CD4BS MAbs IgG1b12 and F105 to R5X4 virions, but only IgG1b12 binding was increased by B4a1 to the R5 isolate, and neutralization was not impacted.
Cavacini2002
(co-receptor)
-
F105: NIH AIDS Research and Reference Reagent Program: 857.
-
F105: 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)
-
F105: Virion capture assays are not a good predictor of neutralization, and the presentation of epitopes using this assay seems to be different from that of functional Envelope spikes on primary isolates -- F105 and b6 could efficiently block the b12-mediated capture of infectious virions in a virus capture, but did not inhibit b12 neutralization -- while b12 was potent at neutralizing the three primary virions JR-CSF, ADA, and 89.6, the Abs F105, 19b, and Fab b6 were overall very poor neutralizers.
Poignard2003
(antibody interactions)
-
F105: Review of nAbs that discusses mechanisms of neutralization, passive transfer of nAbs and protection in animal studies, and vaccine strategies.
Liu2002
(immunoprophylaxis, review)
-
F105: Review of nAbs that notes that F105 binds the CD4BS, in combination with other mAbs it can protect some macaques against SHIV infection, and that it has strong ADCC activity.
Ferrantelli2002
(antibody interactions, effector function, immunoprophylaxis, review)
-
F105: 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)
-
F105: gp120 mutants were used to define the CXCR4 binding site using CXCR4 displayed on paramagnetic proteoliposomes (PMPLs) to reduce non-specific gp120 binding---basic residues in the V3 loop and the β19 strand (RIKQ, positions 419-422) were involved, and deletion of the V1-V2 loops allowed CD4-independent CXCR4 binding---mAbs 17b (CD4i) and F105 (CD4BS) were used to study conformational changes in the mutants---the affinity of ΔV1 and ΔV1-V2 mutants for F105 was comparable to the wildtype---V3 mutants did not affect F105 binding---the K421A mutation in the β19 strand dramatically reduced F105 affinity, consistent with what is known about the F105 epitope.
Basmaciogullar2002
(antibody binding site)
-
F105: 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, 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 gp160δCT PLs indistinguishably from gp160δCT expressed on the cell surface.
Grundner2002
(antibody binding site)
-
F105: 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)
-
F105: 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)
-
F105: 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
(immunoprophylaxis, mother-to-infant transmission)
-
F105: 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 gp140δ683(-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 C11, A32, and 30D which did not bind the stabilized oligomer.
Yang2002
(vaccine antigen design)
-
F105: 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
(antibody binding site)
-
F105: 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 F105.
Kolchinsky2001
(antibody binding site)
-
F105: SHIV-HXBc2 is a neutralization sensitive non-pathogenic virus, and several in vivo passages through monkeys 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
(antibody binding site)
-
F105: 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) that preserve and expose some neutralizing epitopes while occluding some non-neutralizing epitopes -- CD4BS MAbs (F105 and F91) and CD4i (17b and 48d) recognized gp140-GNC4 as well as gp120 or gp140 -- non-neutralizing mAbs C11, A32, 522-149, M90, and #45 bound to the gp140-GNC4 glycoprotein at reduced levels compared to gp120 -- mAbs directed at the extreme termini of gp120 C1 (135/9 and 133/290) and C5 (CRA-1 and M91) bound efficiently to gp140-GNC4.
Yang2000
(vaccine antigen design)
-
F105: 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, although F105 was an exception and cannot neutralize either form of MN -- the mutation L544P reduced binding of all mAbs against gp120 by causing conformational changes.
Park2000
-
F105: Host encoded intercellular adhesion molecule (ICAM-1) is incorporated by the HIV-1 virion and enhances viral infectivity -- ICAM-1 does not modify virus sensitivity to antibodies 0.5beta or 4.8D or sCD4, but neutralizing ability of F105 was diminished in ICAM bearing virions in the presence of lymphocyte function-association antigen-1 (LFA-1) Ab.
Fortin2000
-
F105: 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 7.2 +/- 2.2 days.
Baba2000
(immunoprophylaxis, mother-to-infant transmission)
-
F105: 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)
-
F105: Anti-C1 region mAb 87-135/9 blocks gp120 interaction with CD4+ cells -- blocking activity is additive when combined with antibodies which bind in the C4 region of gp120 (F105, 388/389, and b12).
Kropelin1998
(antibody interactions)
-
F105: F105 enhances viral entry of viruses carrying the YU2 envelope glycoproteins, but neutralizes HXBc2.
Sullivan1998b
(enhancing activity)
-
F105: A comparison of 25 gp120 specific, conformation dependent mAbs was done and F105 was used for competition studies -- F105 did cross-compete with multiple CD4BS specific MAbs, however most could not neutralize even the autologous NL4-3 strains.
Sugiura1999
(antibody interactions)
-
F105: Immunoprecipitation of gp120 and gp160 expressed from a rec Semliki Forest virus by F105 and IgG1b12 indicated that the SFV expressed HIV-1 Env was folded appropriately -- and SVF-HIV-1 Env vaccine gave the strongest anti-HIV-1 Env response in mice, when compared to an HIV-1 Env DNA vaccine and a rgp160 protein.
Brand1998
(vaccine antigen design)
-
F105: The mAb F240 binds to the immunodominant region of gp41 and enhances infection in the presence of complement -- reactivity of F240 is enhanced by preincubation of cells with sCD4 or anti-CD4BS MAb F105.
Cavacini1998a
(antibody interactions)
-
F105: 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)
-
F105: Phase I dose escalation study, single dose of 100 or 500 mg/m2 was given to 4 HIV+ patients -- sustained levels, no immune response against F105, no toxicity, infused Ab retained function -- there was no evidence of anti-HIV-1 activity and virus was not diminished at day 1 or 7, by culture or plasma RNA.
Cavacini1998
(kinetics, immunotherapy)
-
F105: 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)
-
F105: Binds both gp120 and soluble gp120+gp41 complex efficiently, suggesting its gp120 epitope is not blocked by gp41 binding -- 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)
-
F105: Virus with the V1-V2 loop deleted was viable and more susceptible to neutralization by CD4i MAb 17b, and anti-V3 mAbs 1121, 9284, and 110.4, but not to a CD4BS mAb, F105 or sCD4.
Cao1997
(antibody binding site)
-
F105: One of 14 human mAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env -- F105 could only achieve 50% neutralization alone -- all Ab combinations tested showed synergistic neutralization -- F105 has synergistic response with mAbs 694/98-D (anti-V3), 48d, 2F5, and 2G12, and also with HIVIG.
Li1997
(antibody interactions, variant cross-reactivity)
-
F105: In a multilaboratory blinded study, failed to neutralize any of nine B clade primary isolates.
DSouza1997
(variant cross-reactivity)
-
F105: Neutralizes TCLA strains, but not primary isolates.
Parren1997
(variant cross-reactivity)
-
F105: Intracellular co-expression of heavy and light chains of the Fab105 fragment MAb F105 was enhanced by inclusion of an internal ribosome entry site (IRES) sequence -- the Fab105 IRES expression cassette was cloned into an adeno-associated virus (AAV) shuttle vector, and transduced into human lymphocytes which were able to produce and secrete the Fab105 fragments while maintaining normal growth -- several primary HIV-1 patient isolates were effectively blocked.
Chen1996
(immunotherapy)
-
F105: Binding of F105 to oligomeric gp120 occurs despite the fact it cannot neutralize primary isolates.
Litwin1996
-
F105: 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)
-
F105: F105 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)
-
F105: Neutralizes HIV-1 LAI less potently than V3 specific mAbs.
McDougal1996
-
F105: Phase I study -- mAb clearance in plasma has a 13 day half-life.
Wolfe1996
(kinetics, immunotherapy)
-
F105: The sulfated polysaccharide curdlan sulfate (CRDS) binds to the Envelope of T-tropic viruses and neutralizes virus -- deletion of the V3 loop results in less potent inhibition of F105 binding by CRDS -- binding site of F105 described as 256-257 ST, 368-370 DPE, 421 K, and 470-484 PGGGDMRDNWRSELY.
Jagodzinski1996
(antibody binding site)
-
F105: Changing heavy chain from IgG1 to IgG3 increased neutralization efficiency.
Cavacini1995
-
F105: Biotinylated F105 was used for competition studies with Ab derived from pregnant HIV-1+ women -- a correlation between maternal anti-CD4 BS Abs overlapping the F105 binding site and lack of HIV-1 transmission to infants was noted.
Khouri1995
(mother-to-infant transmission)
-
F105: Efficient neutralization of T-cell adapted lines HXBc2 and MN, no neutralization of primary isolates 89.6, ADA and YU2 -- even some enhancement of infection of ADA and YU2 was observed.
Sullivan1995
(enhancing activity, variant cross-reactivity)
-
F105: Eight patient phase Ia trial for use as an immunotherapeutic -- no clinical or biochemical side effects observed, plasma levels of 10 ug/ml maintained for 21 days.
Posner1995
(immunotherapy)
-
F105: An immunoassay for titrating CD4BS serum antibody was developed using a gp120-coated solid phase and competition with mAb F105 -- 109/110 French HIV-1+ sera and 51/56 HIV-1+ African sera had detectable CD4BS Abs using this assay, demonstrating CD4 binding site conservation among diverse subtypes -- CD4BS Abs were detected soon after seroconversion and persisted -- 0/21 HIV-2+ sera reacted, indicating that the HIV-1 and HIV-2 CD4BS Abs are not cross-reactive.
Turbica1995
(assay or method development, subtype comparisons)
-
F105: A human CD4+ T lymphocyte line was transduced to express Fab fragments of F105 -- heavy and light chains are joined by an inter-chain linker -- in the transduced cells infected with HIV-1, the Fab binds intracellularly to the envelope protein and inhibits HIV-1 production -- secreted Fab fragments neutralize cell-free HIV-1 -- combined intra- and extracellular binding activities of the expressed Fab make transduced cells resistant to HIV-1 infection and also can protect surrounding lymphocytes by secreting neutralizing antibodies.
Marasco1993,Chen1994a
(variant cross-reactivity)
-
F105: Used as a positive control for CD4 BS antibodies in a study of the influence of oligomeric structure of Env in determining the repertoire of the Ab response.
Earl1994
(antibody binding site)
-
F105: Fab fragments show reduced capacity to neutralize IIIB, MN, and RF compared to intact IgG1, suggesting bivalent interaction may be important in binding and neutralization.
Cavacini1994a
(variant cross-reactivity)
-
F105: Administered intravenously to four cynomologus monkeys, plasma pharmacokinetics and biological activity tested.
Cavacini1994
(kinetics)
-
F105: 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 F105 binding.
Cook1994
(brain/CSF)
-
F105: A mutation in gp41, 582 A/T, confers resistance to neutralization (also confers resistance to mAbs 48d, 21h, 15e and 17b).
Thali1994
(antibody binding site)
-
F105: Comparison of mAb F105 sequences with those of mAbs 21h and 15e.
Bagley1994
(antibody sequence)
-
F105: A neutralization escape mutant (HXB2 A281V) was selected by growth of HXB2 in the presence of broadly neutralizing sera -- F105 neutralization was not affected by this mutation.
Watkins1993
(escape)
-
F105: Ab response in IIIB lab workers was compared to gp160 LAI vaccine recipients -- F105 was used as a control -- infected lab workers and some of the gp160 vaccinees had a mAb response that could inhibit gp120-CD4 binding, at lower titers than the infected lab workers.
Pincus1993a
(vaccine-induced immune responses)
-
F105: 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 -- required >81 fold higher concentrations to neutralize the mutant than wild type.
Klasse1993b
(antibody interactions)
-
F105: Study of synergy of neutralization and binding comparing F105 and sCD4 with the V3 mAbs: 50.1, 59.1, 83.1, and 58.2 -- synergy was observed, and the data suggest that binding of one ligand (F105) can increase the binding of the second (e. g. V3 loop mAbs) due to conformational changes.
Potts1993
(antibody interactions)
-
F105: Study of synergy between F105 and sera from vaccinated volunteers with V3-loop specific neutralization activity -- 2/3 sera demonstrated neutralization synergy, and 3/3 binding/fusion-inhibition synergy.
Montefiori1993
(antibody interactions)
-
F105: Binding to Delta V1/2 and Delta V1/2/3 mutant glycoproteins is 2.4- and 13-fold greater, respectively, than binding to wildtype gp120.
Wyatt1993
(antibody binding site)
-
F105: Serum from all asymptomatic HIV-1 positive people tested block F105 binding, but only from 27% of symptomatic individuals.
Cavacini1993a
(rate of progression)
-
F105: Additive MN or SF2 neutralization when combined with anti-V3 mAbs 447-52D and 257-D.
Cavacini1993
(antibody interactions)
-
F105: No neutralization of primary isolates observed (John Moore, pers comm), laboratory strains could be neutralized though.
-
F105: F105 binds to and neutralizes selected lab strains and 3/9 HIV-1 primary isolates -- synergistic enhancement of neutralization by seropositive sera.
Posner1993
(antibody interactions, variant cross-reactivity)
-
F105: Called F-105 -- neutralizes IIIB -- strong inhibition of HIV+ human sera binding to IIIB gp120.
Moore1993a
-
F105: Significant enhancement of F105 binding to RF infected cells preincubated with V3-specific mAbs V3-2 and V3-1.
Posner1992a
(antibody interactions)
-
F105: F105 mediates ADCC against SF2 through the CD16+ population of PBMC -- does not mediate complement-dependent cytotoxicity.
Posner1992
(complement, effector function)
-
F105: Precipitation of Delta 297-329 env glycoprotein, which has a deleted V3 loop, is much more efficient than precipitation of wild type.
Wyatt1992
(antibody binding site)
-
F105: MAb cDNA sequence -- V H4 V71-4 rearranged with a D H D-D fusion product of dlr4 and da4, and with J H5 -- V kappa is from the Humvk325 germline gene joined with Jkappa 2.
Marasco1992
(antibody sequence)
-
F105: Amino acid substitutions that impair F105 neutralization inhibit gp120-CD4 interaction.
Thali1992a
(antibody binding site)
-
F105: F105 neutralization escape mutants result from changes in amino acids in discontinuous regions: C2, 256-262 and C3, 386-370.
Thali1991
(antibody binding site)
-
F105: First description of F105, binds topographically near the CD4-binding site -- inhibits binding of free, infectious virions to uninfected HT-H9 cells, but does not react with virus adsorbed to uninfected HT-H9 cells -- soluble rCD4 pre-bound to infected cells inhibits F105 binding -- F105 inhibits infection of HT-H9 cells in standard neutralization assays with HIV-1 and MN strains.
Posner1991
(antibody binding site, antibody generation)
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Cao1997
J. Cao, N. Sullivan, E. Desjardin, C. Parolin, J. Robinson, R. Wyatt, and J. Sodroski. Replication and Neutralization of Human Immunodeficiency Virus Type 1 Lacking the V1 and V2 Variable Loops of the gp120 Envelope Glycoprotein. J. Virol., :9808-9812, 1997. An HIV-1 mutant lacking the V1-V2 loops can replicate in Jurkat cells and revertants that replicate with wild-type efficiency rapidly evolve in culture. These viruses exhibited increased neutralization susceptibility to V3 loop or CD4i MAbs, but not to sCD4 or anti-CD4BS MAbs. Thus the gp120 V1 and V2 loops protect HIV-1 from some subsets of neutralizing antibodies. PubMed ID: 9371651.
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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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Cavacini1993
L. A. Cavacini, C. L. Emes, J. Power, A. Buchbinder, S. Zolla-Pazner, and M. R. Posner. Human Monoclonal Antibodies to the V3 Loop of HIV-1 gp120 Mediate Variable and Distinct Effects on Binding and Viral Neutralization by a Human Monoclonal Antibody to the CD4 Binding Site. J. Acquir. Immune Defic. Syndr., 6:353-358, 1993. PubMed ID: 8455141.
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Cavacini1993a
L. A. Cavacini, C. L. Emes, J. Power, J. Underdalh, R. Goldstein, K. Mayer, and M. R. Posner. Loss of Serum Antibodies to a Conformational Epitope of HIV-1/gp120 Identified by a Human Monoclonal Antibody Is Associated with Disease Progression. J. Acquir. Immune Defic. Syndr., 6:1093-1102, 1993. Serum from 100\% of asymptomatic HIV-positive people blocked F105 binding, while serum samples from 27\% of ARC/AIDS patients blocked F105 binding. PubMed ID: 7692037.
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Cavacini1994
L. A. Cavacini, J. Power, C. L. Emes, K. Mace, G. Treacy, and M. R. Posner. Plasma Pharmacokinetics and Biological Activity of a Human Immunodeficiency Virus Type 1 Neutralizing Human Monoclonal Antibody, F105, in Cynomolgus Monkeys. Tumor Immunol., 15:251-256, 1994. MAb F105 was administered intravenously to four cynomolgus monkeys. At 15 days post-dose, total serum F105 was 230 +/- 79 $\mu$g/ml and F105 was immunoreactive with cells infected with the MN and IIIB strains of HIV-1 as determined by flow cytometry. PubMed ID: 8061897.
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Cavacini1994a
L. A. Cavacini, C. L. Emes, J. Power, M. Duval, and M. R. Posner. Effect of Antibody Valency on Interaction with Cell-Surface Expressed HIV-1 and Viral Neutralization. J. Immunol., 152:2538-2545, 1994. PubMed ID: 7510748.
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Cavacini1995
L. A. Cavacini, C. L. Emes, J. Power, F. D. Desharnais, M. Duval, D. Montefiori, and M. R. Posner. Influence of Heavy Chain Constant Regions on Antigen Binding and HIV-1 Neutralization by a Human Monoclonal Antibody. J. Immunol., 155:3638-3644, 1995. By changing the IgG1 constant region of MAb F105 from IgG$_1\kappa$ to IgG$_3\kappa$, dramatic strain specific increases in neutralization efficiency were obtained. PubMed ID: 7561063.
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Cavacini1998
L. A. Cavacini, M. H. Samore, J. Gambertoglio, B. Jackson, M. Duval, A. Wisnewski, S. Hammer, C. Koziel, C. Trapnell, and M. R. Posner. Phase I Study of a Human Monoclonal Antibody Directed against the CD4-Binding Site of HIV Type 1 Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:545-550, 1998. In an immunotherapeutic study, administration of a single dose of F105 was non-toxic and the Ab persisted, yet no benefit was observed in 4 individuals. The authors suggest it may be more helpful in other settings, for example, patients with no pre-existing anti-CD4 BS Abs, or in combination with other MAbs. PubMed ID: 9591708.
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Cavacini1998a
L. A. Cavacini, C. L. Emes, A. V. Wisnewski, J. Power, G. Lewis, D. Montefiori, and M. R. Posner. Functional and molecular characterization of human monoclonal antibody. AIDS Res. Hum. Retroviruses, 14:1271-80, 1998. PubMed ID: 9764911.
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Cavacini1999
L. A. Cavacini, A. Wisnewski, J. E. Peterson, D. Montefiori, C. Emes, M. Duval, G. Kingsbury, A. Wang, D. Scadden, and M. R. Posner. A Human Anti-HIV Autoantibody Enhances EBV Transformation and HIV infection. Clin. Immunol., 93:263-273, 1999. PubMed ID: 10600338.
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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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Chen1994a
S. Y. Chen, Y. Khouri, J. Bagley, and W. A. Marasco. Combined intra- and extracellular immunization against human immunodeficiency virus type 1 infection with a human anti-gp120 antibody. Proc. Natl. Acad. Sci. U.S.A., 91:5932-5936, 1994. PubMed ID: 8016092.
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Chen1996
J. D. Chen, Q. Yang, W. A. Marasco, and S. Y. Chen. Intra- and Extra-Cellular Immunization against HIV-1 Infection with Lymphocytes Transduced with an AAV Vector Expressing a Human Anti-gp120 Antibody. Hum. Gene Ther., 7:1515-1525, 1996. PubMed ID: 8864752.
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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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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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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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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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Clayton2007
Reginald Clayton, Asa Ohagen, Olivia Goethals, Alexandra Smets, Marnix Van Loock, Lieve Michiels, Erin Kennedy-Johnston, Mark Cunningham, Haiyan Jiang, Sharon Bola, Lester Gutshall, George Gunn, Alfred Del Vecchio, Robert Sarisky, Sabine Hallenberger, and Kurt Hertogs. Binding Kinetics, Uptake and Intracellular Accumulation of F105, an Anti-gp120 Human IgG1kappa Monoclonal Antibody, in HIV-1 Infected Cells. J. Virol. Methods, 139(1):17-23, Jan 2007. PubMed ID: 17034868.
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Clayton2009
Reginald Clayton, Asa Ohagen, Francois Nicol, Alfred M. Del Vecchio, Tim H. M. Jonckers, Olivia Goethals, Marnix Van Loock, Lieve Michiels, John Grigsby, Zheng Xu, Yuan Peng Zhang, Lester L. Gutshall, Mark Cunningham, Haiyan Jiang, Sharon Bola, Robert T. Sarisky, and Kurt Hertogs. Sustained and Specific In Vitro Inhibition of HIV-1 Replication by a Protease Inhibitor Encapsulated in gp120-Targeted Liposomes. Antiviral Res., 84(2):142-149, Nov 2009. PubMed ID: 19699239.
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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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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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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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Dorgham2005
Karim Dorgham, Ismaïl Dogan, Natacha Bitton, Christophe Parizot, Valerie Cardona, Patrice Debré, Oliver Hartley, and Guy Gorochov. Immunogenicity of HIV Type 1 gp120 CD4 Binding Site Phage Mimotopes. AIDS Res. Hum. Retroviruses, 21(1):82-92, Jan 2005. PubMed ID: 15665647.
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Douagi2010
Iyadh Douagi, Mattias N. E. Forsell, Christopher Sundling, Sijy O'Dell, Yu Feng, Pia Dosenovic, Yuxing Li, Robert Seder, Karin Loré, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. Influence of Novel CD4 Binding-Defective HIV-1 Envelope Glycoprotein Immunogens on Neutralizing Antibody and T-Cell Responses in Nonhuman Primates. J. Virol., 84(4):1683-1695, Feb 2010. PubMed ID: 19955308.
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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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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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Earl1994
P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157.
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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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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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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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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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Finzi2010
Andrés Finzi, Beatriz Pacheco, Xin Zeng, Young Do Kwon, Peter D. Kwong, and Joseph Sodroski. Conformational Characterization of Aberrant Disulfide-Linked HIV-1 gp120 Dimers Secreted from Overexpressing Cells. J Virol Methods, 168(1-2):155-161, Sep 2010. PubMed ID: 20471426.
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Fortin2000
J. F. Fortin, R. Cantin, M. G. Bergeron, and M. J. Tremblay. Interaction between Virion-Bound Host Intercellular Adhesion Molecule-1 and the High-Affinity State of Lymphocyte Function-Associated Antigen-1 on Target Cells Renders R5 and X4 Isolates of Human Immunodeficiency Virus Type 1 More Refractory to Neutralization. Virology, 268:493-503, 2000. PubMed ID: 10704357.
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Georgiev2013a
Ivelin S. Georgiev, M. Gordon Joyce, Tongqing Zhou, and Peter D. Kwong. Elicitation of HIV-1-Neutralizing Antibodies against the CD4-Binding Site. Curr. Opin. HIV AIDS, 8(5):382-392, Sep 2013. PubMed ID: 23924998.
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Giraud1999
A. Giraud, Y. Ataman-Onal, N. Battail, N. Piga, D. Brand, B. Mandrand, and B. Verrier. Generation of Monoclonal Antibodies to Native Human Immunodeficiency Virus Type 1 Envelope Glycoprotein by Immunization of Mice with Naked RNA. J. Virol. Methods, 79:75-84, 1999. PubMed ID: 10328537.
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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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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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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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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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Guenaga2015a
Javier Guenaga, Viktoriya Dubrovskaya, Natalia de Val, Shailendra K. Sharma, Barbara Carrette, Andrew B. Ward, and Richard T. Wyatt. Structure-Guided Redesign Increases the Propensity of HIV Env To Generate Highly Stable Soluble Trimers. J. Virol., 90(6):2806-2817, 30 Dec 2015. PubMed ID: 26719252.
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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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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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Hinz2010
Andreas Hinz, David Lutje Hulsik, Anna Forsman, Willie Wee-Lee Koh, Hassan Belrhali, Andrea Gorlani, Hans de Haard, Robin A. Weiss, Theo Verrips, and Winfried Weissenhorn. Crystal Structure of the Neutralizing Llama V(HH) D7 and Its Mode of HIV-1 gp120 Interaction. PLoS One, 5(5):e10482, 2010. PubMed ID: 20463957.
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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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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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Jagodzinski1996
P. P. Jagodzinski, J. Wustner, D. Kmieciak, T. J. Wasik, A. Fertala, A. L. Sieron, M. Takahashi, T. Tsuji, T. Mimura, M. S. Fung, M. K. Gorny, M. Kloczewiak, Y. Kaneko, and D. Kozbor. Role of the V2, V3, and CD4-Binding Domains of GP120 in Curdlan Sulfate Neutralization Sensitivity of HIV-1 during Infection of T Lymphocytes. Virology, 226:217-227, 1996. PubMed ID: 8955041.
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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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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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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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Kelker2010
Hanna C. Kelker, Vincenza R. Itri, and Fred T. Valentine. A Strategy for Eliciting Antibodies against Cryptic, Conserved, Conformationally Dependent Epitopes of HIV Envelope Glycoprotein. PLoS One, 5(1):e8555, 2010. PubMed ID: 20052405.
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Kesavardhana2017
Sannula Kesavardhana, Raksha Das, Michael Citron, Rohini Datta, Linda Ecto, Nonavinakere Seetharam Srilatha, Daniel DiStefano, Ryan Swoyer, Joseph G. Joyce, Somnath Dutta, Celia C. LaBranche, David C. Montefiori, Jessica A. Flynn, and Raghavan Varadarajan. Structure-Based Design of Cyclically Permuted HIV-1 gp120 Trimers That Elicit Neutralizing Antibodies. J. Biol. Chem., 292(1):278-291, 6 Jan 2017. PubMed ID: 27879316.
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Khouri1995
Y. F. Khouri, K. McIntosh, L. Cavacini, M. Posner, M. Pagano, R. Tuomala, and W. A. Marasco. Vertical Transmission of HIV-1. Correlation with Maternal Viral Load and Plasma Levels of CD4 Binding Site Anti-gp120 Antibodies. J. Clin. Invest., 95:732-737, 1995. Differences in levels of Abs directed against the monomeric gp120 and against the V3 loop region of gp120 were not significantly different between transmitting and non-transmitting mothers. Differences were observed in the levels of CD4 binding site antibodies, as determined by the ability of diluted maternal plasma to inhibit binding of the CD4 binding site monoclonal antibody F105 (MAb F105) to monomeric gp120. PubMed ID: 7860754.
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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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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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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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Anil Korkut and Wayne A. Hendrickson. Structural Plasticity and Conformational Transitions of HIV Envelope Glycoprotein gp120. PLoS One, 7(12):e52170, 2012. PubMed ID: 23300605.
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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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M. Kropelin, C. Susal, V. Daniel, and G. Opelz. Inhibition of HIV-1 rgp120 Binding to CD4+ T Cells by Monoclonal Antibodies Directed against the gp120 C1 or C4 Region. Immunol. Lett., 63:19-25, 1998. PubMed ID: 9719434.
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Kulp2017
Daniel W. Kulp, Jon M. Steichen, Matthias Pauthner, Xiaozhen Hu, Torben Schiffner, Alessia Liguori, Christopher A. Cottrell, Colin Havenar-Daughton, Gabriel Ozorowski, Erik Georgeson, Oleksandr Kalyuzhniy, Jordan R. Willis, Michael Kubitz, Yumiko Adachi, Samantha M. Reiss, Mia Shin, Natalia de Val, Andrew B. Ward, Shane Crotty, Dennis R. Burton, and William R. Schief. Structure-Based Design of Native-Like HIV-1 Envelope Trimers to Silence Non-Neutralizing Epitopes and Eliminate CD4 Binding. Nat. Commun., 8(1):1655, 21 Nov 2017. PubMed ID: 29162799.
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Kwon2012
Young Do Kwon, Andrés Finzi, Xueling Wu, Cajetan Dogo-Isonagie, Lawrence K. Lee, Lucas R. Moore, Stephen D. Schmidt, Jonathan Stuckey, Yongping Yang, Tongqing Zhou, Jiang Zhu, David A. Vicic, Asim K. Debnath, Lawrence Shapiro, Carole A. Bewley, John R. Mascola, Joseph G. Sodroski, and Peter D. Kwong. Unliganded HIV-1 gp120 Core Structures Assume the CD4-Bound Conformation with Regulation by Quaternary Interactions and Variable Loops. Proc. Natl. Acad. Sci. U.S.A., 109(15):5663-5668, 10 Apr 2012. PubMed ID: 22451932.
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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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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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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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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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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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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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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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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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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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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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Hong Ling, Xiao-Yan Zhang, Osamu Usami, and Toshio Hattori. Activation of gp120 of Human Immunodeficiency Virus by Their V3 Loop-Derived Peptides. Biochem. Biophys. Res. Commun., 297(3):625-631, 27 Sep 2002. PubMed ID: 12270140.
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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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V. Litwin, K. A. Nagashima, A. M. Ryder, C. H. Chang, J. M. Carver, W. C. Olson, M. Alizon, K. W. Hasel, P. J. Maddon, and G. P. Allaway. Human immunodeficiency virus type 1 membrane fusion mediated by a laboratory-adapted strain and a primary isolate analyzed by resonance energy transfer. J. Virol., 70:6437-6441, 1996. Fusion of primary (JRFL) and TCLA (LAI) strains of the virus were studied. The degree, kinetics, neutral pH and divalent cations requirements were similar for membrane fusion for both viruses. However, the inhibition of fusion by sCD4 and CD4-IgG2 occurred at virus neutralization concentrations for JRFL, but higher concentrations were required to inhibit LAI fusion than to neutralize LAI, suggesting that viral neutralization and fusion-inhibition are distinct. PubMed ID: 8709277.
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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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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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Lyumkis2013
Dmitry Lyumkis, Jean-Philippe Julien, Natalia de Val, Albert Cupo, Clinton S. Potter, Per-Johan Klasse, Dennis R. Burton, Rogier W. Sanders, John P. Moore, Bridget Carragher, Ian A. Wilson, and Andrew B. Ward. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer. Science, 342(6165):1484-1490, 20 Dec 2013. PubMed ID: 24179160.
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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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W. A. Marasco, J. Bagley, C. Zani, M. Posner, L. Cavacini, W. A. Haseltine, and J. Sodroski. Characterization of the cDNA of a Broadly Reactive Neutralizing Human anti-gp120 Monoclonal Antibody. J. Clin. Invest., 90:1467-1478, 1992. PubMed ID: 1401079.
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W. A. Marasco, W. A. Haseltine, and S. Y. Chen SY. Design, intracellular expression, and activity of a human anti-human immunodeficiency virus type 1 gp120 single-chain antibody. Proc. Natl. Acad. Sci. U.S.A., 90:7889-7893, 1993. Comment in Proc Natl Acad Sci USA 1993 90:7427-8. PubMed ID: 8356098.
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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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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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Masiero2005
S. Masiero, C. Del Vecchio, R. Gavioli, G. Mattiuzzo, M. G. Cusi, L. Micheli, F. Gennari, A. Siccardi, W. A. Marasco, G. Palu, and C. Parolin. T-Cell Engineering by a Chimeric T-Cell Receptor with Antibody-Type Specificity for the HIV-1 gp120. Gene Ther., 12(4):299-310, Feb 2005. PubMed ID: 15496956.
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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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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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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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Mishra2020a
Nitesh Mishra, Shaifali Sharma, Ayushman Dobhal, Sanjeev Kumar, Himanshi Chawla, Ravinder Singh, Muzamil Ashraf Makhdoomi, Bimal Kumar Das, Rakesh Lodha, Sushil Kumar Kabra, and Kalpana Luthra. Broadly Neutralizing Plasma Antibodies Effective against Autologous Circulating Viruses in Infants with Multivariant HIV-1 Infection. Nat. Commun., 11(1):4409, 2 Sep 2020. PubMed ID: 32879304.
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Montefiori1993
D. C. Montefiori, B. S. Graham, J. Zhou, J. Zhou, R. A. Bucco, D. H. Schwartz, L. A. Cavacini, M. R. Posner, and the NIH-NIAID AIDS Vaccine Clinical Trials Network. V3-Specific Neutralizing Antibodies in Sera From HIV-1 gp160-Immunized Volunteers Block Virus Fusion and Act Synergistically with Human Monoclonal Antibody to the Conformation-dependent CD4 Binding Site of gp120. J. Clin. Invest., 92:840-847, 1993. PubMed ID: 8349820.
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Moody2015
M. Anthony Moody, Feng Gao, Thaddeus C. Gurley, Joshua D. Amos, Amit Kumar, Bhavna Hora, Dawn J. Marshall, John F. Whitesides, Shi-Mao Xia, Robert Parks, Krissey E. Lloyd, Kwan-Ki Hwang, Xiaozhi Lu, Mattia Bonsignori, Andrés Finzi, Nathan A. Vandergrift, S. Munir Alam, Guido Ferrari, Xiaoying Shen, Georgia D. Tomaras, Gift Kamanga, Myron S. Cohen, Noel E. Sam, Saidi Kapiga, Elin S. Gray, Nancy L. Tumba, Lynn Morris, Susan Zolla-Pazner, Miroslaw K. Gorny, John R. Mascola, Beatrice H. Hahn, George M. Shaw, Joseph G. Sodroski, Hua-Xin Liao, David C. Montefiori, Peter T. Hraber, Bette T. Korber, and Barton F. Haynes. Strain-Specific V3 and CD4 Binding Site Autologous HIV-1 Neutralizing Antibodies Select Neutralization-Resistant Viruses. Cell Host Microbe., 18(3):354-362, 9 Sep 2015. PubMed ID: 26355218.
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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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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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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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Oscherwitz1999
J. Oscherwitz, F. M. Gotch, K. B. Cease, and J. A. Berzofsky. New Insights and Approaches Regarding B- and T-Cell Epitopes in HIV Vaccine Design. AIDS, 13(Suppl A):S163-174, 1999. PubMed ID: 10885773.
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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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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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Pancera2005a
Marie Pancera, Jacob Lebowitz, Arne Schön, Ping Zhu, Ernesto Freire, Peter D. Kwong, Kenneth H. Roux, Joseph Sodroski, and Richard Wyatt. Soluble Mimetics of Human Immunodeficiency Virus Type 1 Viral Spikes Produced by Replacement of the Native Trimerization Domain with a Heterologous Trimerization Motif: Characterization and Ligand Binding Analysis. J. Virol., 79(15):9954-9969, Aug 2005. PubMed ID: 16014956.
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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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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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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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S. H. Pincus, K. G. Messer, D. H. Schwartz, G. K. Lewis, B. S. Graham, W. A. Blattner, and G. Fisher. Differences in the Antibody Response to Human Immunodeficiency Virus-1 Envelope Glycoprotein (gp160) in Infected Laboratory Workers and Vaccinees. J. Clin. Invest., 91:1987-1996, 1993. PubMed ID: 7683694.
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Pincus1996
S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220.
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Poignard2003
Pascal Poignard, Maxime Moulard, Edwin Golez, Veronique Vivona, Michael Franti, Sara Venturini, Meng Wang, Paul W. H. I. Parren, and Dennis R. Burton. Heterogeneity of Envelope Molecules Expressed on Primary Human Immunodeficiency Virus Type 1 Particles as Probed by the Binding of Neutralizing and Nonneutralizing Antibodies. J. Virol., 77(1):353-365, Jan 2003. PubMed ID: 12477840.
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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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Posner1992
M. R. Posner, H. S. Elboim, T. Cannon, L. Cavicini, and T. Hideshima. Functional Activity of an HIV-1 Neutralizing IgG Human Monoclonal Antibody: ADCC and Complement-Mediated Lysis. AIDS Res. Hum. Retroviruses, 8:553-558, 1992. PubMed ID: 1381201.
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Posner1992a
M. Posner, L. Cavacini, C. Emes, J. Power, M. Gorny, and S. Zolla-Pazner. Human Monoclonal Antibodies to the V3 Loop of gp120 Mediate Variable and Distinct Effects on Binding and Viral Neutralization by a Human Monoclonal Antibody to the CD4 Binding Site. J. Cell Biochem., Suppl O(16 part E):69, 1992.
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Posner1993
M. R. Posner, L. A. Cavacini, C. L. Emes, J. Power, and R. Byrn. Neutralization of HIV-1 by F105, a Human Monoclonal Antibody to the CD4 Binding Site of gp120. J. Acquir. Immune Defic. Syndr., 6:7-14, 1993. PubMed ID: 8417177.
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Posner1995
M. R. Posner, L. A. Cavacini, J. Gambertoglio, C. Spino, E. Wolfe, C. Trapnell, N. Ketter, S. Hammer, and M. Samore. An ACTG Phase Ia Safety and Pharmacokinetic Trial of Immunotherapy with the Anti-CD4 Binding Site Human Monoclonal Antibody F105. Natl. Conf. Hum. Retroviruses Relat. Infect. (2nd), 1995:150, 1995. Aidsline: 95920546 Abstract: Eight HIV-positive asymptomatic individuals were given F105 by intravenous infusion. There were no clinical side effects or changes in biochemical tests among the eight volunteers. The plasma half life of F105 had a range of 8.7-18.6 days.
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Potts1993
B. J. Potts, K. G. Field, Y. Wu, M. Posner, L. Cavacini, and M. White-Scharf. Synergistic Inhibition of HIV-1 by CD4 Binding Domain Reagents and V3-Directed Monoclonal Antibodies. Virology, 197:415-419, 1993. Four anti-V3 loop MAbs, (59.1, 83.1, 50.1, and 58.2), were evaluated for their affinity, neutralization potencies, and their ability to synergize F105 or sCD4 neutralization. The most important parameter for synergy was the capacity to neutralize a given virus independently. PubMed ID: 8212576.
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Prabakaran2006
Ponraj Prabakaran, Jianhua Gan, You-Qiang Wu, Mei-Yun Zhang, Dimiter S. Dimitrov, and Xinhua Ji. Structural Mimicry of CD4 by a Cross-Reactive HIV-1 Neutralizing Antibody with CDR-H2 and H3 Containing Unique Motifs. J. Mol. Biol., 357(1):82-99, 17 Mar 2006. PubMed ID: 16426633.
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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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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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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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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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Saha2012
Piyali Saha, Sanchari Bhattacharyya, Sannula Kesavardhana, Edward Roshan Miranda, P. Shaik Syed Ali, Deepak Sharma, and Raghavan Varadarajan. Designed Cyclic Permutants of HIV-1 gp120: Implications for Envelope Trimer Structure and Immunogen Design. Biochemistry, 51(9):1836-1847, 6 Mar 2012. PubMed ID: 22329717.
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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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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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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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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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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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Sugiura1999
W. Sugiura, C. C. Broder, B. Moss, and P. L. Earl. Characterization of conformation-dependent anti-gp120 murine monoclonal antibodies produced by immunization with monomeric and oligomeric human immunodeficiency virus type 1 envelope proteins. Virology, 254:257-67, 1999. PubMed ID: 9986792.
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Sullivan1995
N. Sullivan, Y. Sun, J. Li, W. Hofmann, and J. Sodroski. Replicative Function and Neutralization Sensitivity of Envelope Glycoproteins from Primary and T-Cell Line-Passaged Human Immunodeficiency Virus Type 1 Isolates. J. Virol., 69:4413-4422, 1995. Three gp120 molecules derived from primary isolates were compared to T-cell adapted lines HXBc2 and MN. Complementation experiments showed viral entry into peripheral blood mononuclear cell targets was five-fold less efficient for primary isolates. Anti-CD4 binding site neutralizing MAbs were far less potent against primary isolates, and the single anti-V3 MAb tested was 3-fold less potent. The differences in neutralization efficiency could not be attributed to differences in affinity for monomeric gp120, but were related to binding to the oligomeric complex. Enhanced infectivity of primary isolates was observed using sCD4 and MAb F105, which can neutralize T-cell adapted strains. PubMed ID: 7769703.
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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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Teeraputon2005
Sirilak Teeraputon, Suda Louisirirojchanakul, and Prasert Auewarakul. N-Linked Glycosylation in C2 Region of HIV-1 Envelope Reduces Sensitivity to Neutralizing Antibodies. Viral Immunol., 18(2):343-353, Summer 2005. PubMed ID: 16035946.
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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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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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Turbica1995
I. Turbica, M. Posner, C. Bruck, and F. Barin. Simple Enzyme Immunoassay for Titration of Antibodies to the CD4-Binding Site of Human Immunodeficiency Virus Type 1 gp120. J. Clin. Microbiol., 33:3319-3323, 1995. PubMed ID: 8586727.
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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.
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Wang2007a
Bao-Zhong Wang, Weimin Liu, Sang-Moo Kang, Munir Alam, Chunzi Huang, Ling Ye, Yuliang Sun, Yingying Li, Denise L. Kothe, Peter Pushko, Terje Dokland, Barton F. Haynes, Gale Smith, Beatrice H. Hahn, and Richard W. Compans. Incorporation of High Levels of Chimeric Human Immunodeficiency Virus Envelope Glycoproteins into Virus-Like Particles. J. Virol., 81(20):10869-10878, Oct 2007. PubMed ID: 17670815.
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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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Wilkinson2005
Royce A. Wilkinson, Chayne Piscitelli, Martin Teintze, Lisa A. Cavacini, Marshall R. Posner, and C. Martin Lawrence. Structure of the Fab Fragment of F105, a Broadly Reactive Anti-Human Immunodeficiency Virus (HIV) Antibody That Recognizes the CD4 Binding Site of HIV Type 1 gp120. J. Virol., 79(20):13060-13069, Oct 2005. PubMed ID: 16189008.
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Wilkinson2007
Royce A. Wilkinson, Jody R. Evans, Jon M. Jacobs, Dustin Slunaker, Seth H. Pincus, Abraham Pinter, Charles A. Parkos, James B. Burritt, and Martin Teintze. Peptides Selected from a Phage Display Library with an HIV-Neutralizing Antibody Elicit Antibodies to HIV gp120 in Rabbits, But Not to The Same Epitope. AIDS Res. Hum. Retroviruses, 23(11):1416-1427, Nov 2007. PubMed ID: 18184085.
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Williams2017a
Wilton B. Williams, Jinsong Zhang, Chuancang Jiang, Nathan I. Nicely, Daniela Fera, Kan Luo, M. Anthony Moody, Hua-Xin Liao, S. Munir Alam, Thomas B. Kepler, Akshaya Ramesh, Kevin Wiehe, James A. Holland, Todd Bradley, Nathan Vandergrift, Kevin O. Saunders, Robert Parks, Andrew Foulger, Shi-Mao Xia, Mattia Bonsignori, David C. Montefiori, Mark Louder, Amanda Eaton, Sampa Santra, Richard Scearce, Laura Sutherland, Amanda Newman, Hilary Bouton-Verville, Cindy Bowman, Howard Bomze, Feng Gao, Dawn J. Marshall, John F. Whitesides, Xiaoyan Nie, Garnett Kelsoe, Steven G. Reed, Christopher B. Fox, Kim Clary, Marguerite Koutsoukos, David Franco, John R. Mascola, Stephen C. Harrison, Barton F. Haynes, and Laurent Verkoczy. Initiation of HIV Neutralizing B Cell Lineages with Sequential Envelope Immunizations. Nat. Commun., 8(1):1732, 23 Nov 2017. PubMed ID: 29170366.
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Willis2022
Jordan R. Willis, Zachary T. Berndsen, Krystal M. Ma, Jon M. Steichen, Torben Schiffner, Elise Landais, Alessia Liguori, Oleksandr Kalyuzhniy, Joel D. Allen, Sabyasachi Baboo, Oluwarotimi Omorodion, Jolene K. Diedrich, Xiaozhen Hu, Erik Georgeson, Nicole Phelps, Saman Eskandarzadeh, Bettina Groschel, Michael Kubitz, Yumiko Adachi, Tina-Marie Mullin, Nushin B. Alavi, Samantha Falcone, Sunny Himansu, Andrea Carfi, Ian A. Wilson, John R. Yates III, James C. Paulson, Max Crispin, Andrew B. Ward, and William R. Schief. Human immunoglobulin repertoire analysis guides design of vaccine priming immunogens targeting HIV V2-apex broadly neutralizing antibody precursors. Immunity, 55(11):2149-2167e9 doi, Nov 2022. PubMed ID: 36179689
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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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Wolfe1996
E. J. Wolfe, L. A. Cavacini, M. H. Samore, M. R. Posner, C. Kozial, C. Spino, C. B. Trapnell, N. Ketter, S. Hammer, and J. G. Gambertoglio. Pharmacokinetics of F105, a Human Monoclonal Antibody, in Persons Infected with Human Immunodeficiency Virus Type 1. Clin. Pharmacol. Ther., 59:662-667, 1996. PubMed ID: 8681491.
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Wu2008
Xueling Wu, Anna Sambor, Martha C. Nason, Zhi-Yong Yang, Lan Wu, Susan Zolla-Pazner, Gary J. Nabel, and John R. Mascola. Soluble CD4 Broadens Neutralization of V3-Directed Monoclonal Antibodies and Guinea Pig Vaccine Sera against HIV-1 Subtype B and C Reference Viruses. Virology, 380(2):285-295, 25 Oct 2008. PubMed ID: 18804254.
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Wu2009
Xueling Wu, Tongqing Zhou, Sijy O'Dell, Richard T. Wyatt, Peter D. Kwong, and John R. Mascola. Mechanism of Human Immunodeficiency Virus Type 1 Resistance to Monoclonal Antibody b12 That Effectively Targets the Site of CD4 Attachment. J. Virol., 83(21):10892-10907, Nov 2009. PubMed ID: 19692465.
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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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Wu2011
Xueling Wu, Tongqing Zhou, Jiang Zhu, Baoshan Zhang, Ivelin Georgiev, Charlene Wang, Xuejun Chen, Nancy S. Longo, Mark Louder, Krisha McKee, Sijy O'Dell, Stephen Perfetto, Stephen D. Schmidt, Wei Shi, Lan Wu, Yongping Yang, Zhi-Yong Yang, Zhongjia Yang, Zhenhai Zhang, Mattia Bonsignori, John A. Crump, Saidi H. Kapiga, Noel E. Sam, Barton F. Haynes, Melissa Simek, Dennis R. Burton, Wayne C. Koff, Nicole A. Doria-Rose, Mark Connors, NISC Comparative Sequencing Program, James C. Mullikin, Gary J. Nabel, Mario Roederer, Lawrence Shapiro, Peter D. Kwong, and John R. Mascola. Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing. Science, 333(6049):1593-1602, 16 Sep 2011. PubMed ID: 21835983.
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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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Xiang2003
Shi-Hua Xiang, Liping Wang, Mariam Abreu, Chih-Chin Huang, Peter D. Kwong, Eric Rosenberg, James E. Robinson, and Joseph Sodroski. Epitope Mapping and Characterization of a Novel CD4-Induced Human Monoclonal Antibody Capable of Neutralizing Primary HIV-1 Strains. Virology, 315(1):124-134, 10 Oct 2003. PubMed ID: 14592765.
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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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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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Yang2002
Xinzhen Yang, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt, and Joseph Sodroski. Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin. J. Virol., 76(9):4634-4642, 1 May 2002. PubMed ID: 11932429.
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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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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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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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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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Zhou2010
Tongqing Zhou, Ivelin Georgiev, Xueling Wu, Zhi-Yong Yang, Kaifan Dai, Andrés Finzi, Young Do Kwon, Johannes F. Scheid, Wei Shi, Ling Xu, Yongping Yang, Jiang Zhu, Michel C. Nussenzweig, Joseph Sodroski, Lawrence Shapiro, Gary J. Nabel, John R. Mascola, and Peter D. Kwong. Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01. Science, 329(5993):811-817, 13 Aug 2010. PubMed ID: 20616231.
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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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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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Displaying record number 658
Download this epitope
record as JSON.
MAb ID |
17b (1.7b, sCD4-17b, 1.7B) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
James Robinson, Tulane University, New Orleans, LA, USA |
Epitope |
(Discontinuous epitope)
|
Ab Type |
gp120 CD4i CoRbs (Cluster C) |
Neutralizing |
L P (weak) View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human |
Patient |
N70 |
Immunogen |
HIV-1 infection |
Keywords |
acute/early infection, adjuvant comparison, antibody binding site, 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, computational prediction, dendritic cells, drug resistance, dynamics, effector function, enhancing activity, escape, glycosylation, HAART, ART, immunoprophylaxis, immunotherapy, kinetics, mimics, mimotopes, mutation acquisition, neutralization, polyclonal antibodies, review, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity, viral fitness and/or reversion |
Notes
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286 notes.
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17b: 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)
-
17b: 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)
-
17b: 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)
-
17b: 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, vaccine antigen design, binding affinity)
-
17b: CD4-mimetic compounds (CD4mc) can inhibit the interaction of gp120 with CD4 by inhibiting viral entry and inducing structural changes in Env through insertion within the Phe43 cavity of gp120. YIR-821 is a novel CD4mc that has potent antiviral activity and lower toxicity than its prototype, NBD-556. In an assay of its antiviral activity on a multi-clade panel of HIV-1 pseudoviruses, YIR-821 displayed entry inhibitor activity against 53.5% (21/40) of the pseudoviruses tested. YIR-821 enhanced neutralization mediated by coreceptor binding site antibodies 4E9C and 916B2, and by plasma IgG samples in approximately 50% of tested pseudoviruses. The direct antiviral activity of YIR-821 as an entry inhibitor was observed in 53% of both subtype B (27/51) and non-B subtype (40/75) pseudoviruses. The ADCC activity of YIR-821 was compared with CoRBS mAbs (17b and 4E9C) and cluster A region mAb A32. YIR-821 enhanced ADCC activity mediated by 4E9C or by plasma IgG. YIR-821 enhanced the binding activity of 4E9C, 17b and plasma IgG. Sequence diversity in the CD4 binding site as well as other regions, such as the gp120 inner domain layers or gp41, may be involved in the multiple mechanisms related to the sensitive/resistant phenotype of the virus to YIR-821.
Matsumoto2023
(effector function, mimics, binding affinity)
-
17b: Reduction in exposure of non-neutralizing Ab (nnAb) epitopes on native-like Env trimer immunogens results in bnAbs being elicited that have autologous tier 2 neutralization instead of tier 1. The design of trimer modifications to silence nnAb reactivity were directed towards (1) the V3 loop (2) epitopes exposed through CD4-induced conformational changes (CD4i epitopes) and (3) the exposed SOSIP trimer base that is usually buried within virus membrane. (1) In Steichen2016 2 Env variants of BG505 SOSIP.664 with reduced V3 nnAb-generating activity were created, one using mammalian display screens, BG505 MD39, and the other with an engineered disulfide bond, BG505 SOSIP.DS21. MD39's trimer design was improved by using the Rosetta Design platform and inserting 6 buried mutations to form BG505 Olio6, and both this trimer as well as the DS21 were shown to have reduced antigenicity for nnAb generation in a rabbit vaccine model. (2) To reduce CD4i epitope elicitation of nnAbs, saturation mutagenesis of Olio6 was performed, in search of the trimer that binds VRC01-class bnAbs but not CD4. BG505 Olio6.CD4KO containing the G473T mutation was identified. In addition, for the purposes of nucleic acid-based vaccine platform designs, the natural furin cleavage site between gp120 and gp41 was removed to abolish protease cleavage, by swapping the order of gp14 and gp120 in the gp160 gene, giving the trimer BG505 MD39.CP (circular permutation). (3) The exposed trimer base was masked with glycan in 3 under-glycosylated regions in order to direct bnAb responses to the distal regions (CD4bs, V2 apex, N332 superset) of the trimer instead, generating the GRSF (glycan resurfaced) MD39 and GRSF MD39.CP variants. Furthermore, variants with improved thermostability over MD39 were created, MD37 and MD64. All of these stabilizing mutations were transferred to diverse HIV isolates from different subtypes. Finally 3 subtype C (isolate 327c) trimers were assessed for binding to bnAbs, VRC01, PGT121, PGT151, PGT145, PG9 and to nnAbs, F105 and 17b. nnAb 17b interacts with non-native subtype C Env immunogens like c27c SOSIP and not native-like c27c MD37, it also binds BG505 foldon but not other BG505 trimers like SOSIP.664, MD39 and Olio6.
Kulp2017
(antibody binding site, antibody generation, antibody interactions, assay or method development, autologous responses, vaccine antigen design, structure)
-
17b: 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 and only with sCD4, CD4-induced mAb 17b recognized BG505 SOSIP.664 but failed to recognize 4mut, the other 3 designed trimers (DS-SOSIP.6mut containing 4mut mutations, Y177W and I420M, DS-SOSIP.I423F and DS-SOSIP.A316W), and DS-SOSIP. 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)
-
17b: Using subtype A BG505 Env structural information, improved variants of subtype B JRFL and subtype C 16055 Env native flexibly linked (NFL) trimers were generated. The trimer-derived (TD) residues that increased well-ordered, homogeneous, stable, and soluble trimers did not require positive or negative selection as previously needed [Guenaga2015, PLoS Pathos. 11(1):e1004570]. Non-nAbs like 17b and Vc813 target the receptor-bridging sheet epitope of the co-receptor when Env is in its open conformation, after CD4 on the host cell is engaged by the CD4bs of Env. Therefore 17b is not able to bind NFL TD CC trimers that are incapable of exposing the coreceptor due to the CC disulfide bond, but it does recognize 16055 NFL TD8 and JRFL NFL TD15. Disulfide-stablilized CC trimers keep Env in its closed conformation which is preferable for nAb generation.
Guenaga2015a
(antibody interactions, assay or method development, vaccine antigen design, structure)
-
17b: 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 only bound a single CD4 and remained in a prefusion closed conformation. CD4i-targeting mAb 17b was author-defined as ineffective due to its neutralization breadth of 8% on a panel of 170 diverse HIV-1 pseudoviruses. This was consistent with structural modeling which suggested that 17b was incompatible with BG505 SOSIP.664. Soluble CD4 strongly induced 17b binding of wildtype BG505 SOSIP.664, JR-FL SOS E168K, or BG505 SOS T332N trimers, but not mutant trimers containing the DS mutations. Some mutations that stabilized the closed prefusion state of BG505 SOSIP.664 affected 17b binding modestly to moderately.
Kwon2015
(neutralization, vaccine antigen design, structure)
-
17b: The chemokine coreceptor-binding Ab, 17b, was studied in complex with trimeric gp140 immunogens or native HIV-1 Env and they were found to have the same quaternary structure in both the closed and open phases. Thus soluble gp140 trimers from subtypes A (KNH1144) and B (JR-FL) have been designed as mimetics that go through the same structure transitions as the native trimeric Env on BaL virions.
Harris2011
(antibody interactions, assay or method development, vaccine antigen design, structure)
-
17b: 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. Non-CD4bs-binding, non-nAb 17b did not recognize negatively-selected JRFL or 16055 SOSIP trimers.
Guenaga2015
(vaccine antigen design, subtype comparisons, structure)
-
17b: 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. Soluble CD4 induction of 17b binding was efficient for both SOS and SOSIP gp140 proteins indicating that the overlapping CD4-induced coreceptor binding site on gp120 was preserved.
Sanders2002a
(vaccine antigen design)
-
17b: HIV-1 and its SIV precursors share a bnAb epitope in Env V2 at the trimer apex. This study tested the immunogenicity of a chimpanzee SIV (SIVcpz) Env trimer. In mice expressing a human V2-apex bnAb heavy-chain precursor, trimer immunization induced V2-directed nAbs. Infection of macaques with chimeric simian-chimpanzee immunodeficiency viruses (SCIVs) elicited high-titer viremia, potent autologous neutralizing antibodies, rapid sequence escape in the canonical V2-apex epitope, and in some cases, low-titer heterologous plasma breadth mapping to the V2-apex. Antibody cloning from 2 macaques (T925 and T927) identified 7 lineages (53 mAbs) with long CDRH3 regions that cross-neutralize some primary HIV-1 strains with low potency. Electron microscopy of members of the two most cross-reactive lineages confirmed V2 targeting with an angle of approach distinct from prototypical V2-apex bNAbs; antibody binding either required or induced an occluded-open trimer. Probing with conformation-sensitive, nonneutralizing antibodies revealed that SCIV-expressed, but not wild-type SIVcpz Envs, as well as a subset of primary HIV-1 Envs, preferentially adopted a more open trimeric state. These results reveal the existence of a cryptic V2 epitope that is exposed in occluded-open SIVcpz and HIV-1 Env trimers and elicits cross-neutralizing responses of limited breadth and potency. This cryptic epitope, which in some Env backgrounds is immunodominant, needs to be considered in immunogen design. As part of the study, binding and neutralization assays used panels of nAbs (PG9, PG16, PGT145, PGDM1400, VRC26.25, CH01, BG1, VRC38.01), non-nAbs (697-D, 1393A, CH58, CAP228-3D, 3074, 447-52D, 17b, A32), and unmutated ancestors (PG9-RUA, PG16-RUA, VRC26-UCA, CH01-RUA).
Bibollet-Ruche2023
(neutralization, vaccine antigen design, vaccine-induced immune responses)
-
17b: Extensive analysis of new and existing structural models identifies conformation of soluble B41 SOSIP Env trimer intermediates induced by binding with CD4 alone or CD4 and mAb 17b or mAb b12 alone. CD4 or b12 binding induces large conformational rearrangements of gp41 subunits and concomitant inaccessibility of the fusion peptide. A 3.7 Å cryo-EM structure of glycosylated B41 SOSIP.664 in complex with soluble CD4 (sCD4) and mAb 17b, which targets a CD4 binding-induced epitope, and a 5.6 Å cryo-EM structure of ligand-free B41 SOSIP.664 were generated and compared. This revealed extensive Env rearrangements including movement of V1V2 loops, exposure of V3 loop, formation of bridging sheet and α0 structures, conformational changes of HR1 and C3 domains, rearrangement of N262 glycan, and subtle changes in a network of conserved residues. In addition, the fusion peptide becomes embedded and stabilized in a newly formed pocket distant from the host membrane. Further analysis with a generated cryo-EM structure of subtype B B41 SOSIP.664 complexed with sCD4 alone revealed only slight differences whether or not 17b was also present or if the soluble trimer was subtype A BG505 SOSIP.664. This suggests that 17b does not induce further conformational changes beyond those that are induced by sCD4 alone.
Ozorowski2017
(structure)
-
17b: To understand early bnAb responses, 51 HIV-1 clade C infected infants were assayed for neutralization of a 12-virus multi-clade panel. Plasma bnAbs targeting V2-apex on Env were predominant in infant elite and broad neutralizers. In infant elite neutralizers, multi-variant infection was associated with plasma bnAbs targeting diverse autologous viruses. A panel of mAbs (PG9, PG16, PGT145, PGDM1400, VRC26.25, 10-1074, BG18, AIIMS-P01, PGT121, PGT128, PGT135, VRC01, N6, 3BNC117, PGT151, 35O22, 10E8, 4E10, F105, 17b, A32, 48d, b6, 447-52d) was assayed for their ability to neutralize Env clones from infant elite neutralizers; circulating viral variants in infant elite neutralizers were most susceptible to V2-apex bnAbs.
Mishra2020a
(neutralization, polyclonal antibodies)
-
17b: 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)
-
17b: Single chain variable fragments (scFvs) were constructed for mAbs 916B2, 4E9C, and 25C4b. Coverage of neutralization by the scFvs against a panel of 66 multiclade pseudoviruses was 89% for 4E9C, 95% for 25C4b, and 100% for 916B2. 25C4b bound the region spanning multiple domains of hairpin 1 (H1) and H2 of the bridging sheet and V3 base, similar to mAb 17b. For 4E9C, V3-base dependent binding was apparent based on lack of binding to mutants containing a V3 truncation. In contrast, binding of 916B2 was dependent on the H1 region. The study also assayed the binding of additional mAbs (17b, 12G10, 917B11, 5D6S, A32) to gp120 mutants in the CD4i region.
Tanaka2017
(antibody binding site)
-
17b: 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)
-
17b: 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)
-
17b: 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. The CD4i Ab 17b exhibited poor neutralization against HIV-1AD8 full-length and cytoplasmic tail-deleted Envs.
Castillo-Menendez2019
(vaccine antigen design, structure)
-
17b: 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)
-
17b: 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. State 2/3 preferring ligand 17b recognized L193A variants of CH58 and CH77 IMCs with a significant increase compared to the WT.
Prevost2018
(effector function)
-
17b: 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. ISOSIP 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 17b 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)
-
17b: 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 17b in ELISA EC50 and Surface Plasmon Resonance (SPR) assays. 6240.B gp120 exhibited binding to 17b.
Wen2018
(glycosylation, vaccine antigen design)
-
17b: Assays of poly- and autoreactivity demonstrated that broadly neutralizing NAbs are significantly more poly- and autoreactive than non-neutralizing NAbs. 17b is neither autoreactive nor polyreactive.
Liu2015a
(autoantibody or autoimmunity, antibody polyreactivity)
-
17B: The study identified a HIV-1–neutralizing protein in breast milk, Tenascin-C (TNC). TNC is an extracellular matrix protein important in fetal development and wound healing. TNC bound the HIV-1 Envelope protein at a site that is induced upon engagement of its primary receptor, CD4, and is blocked by monoclonal antibodies that bind to the V3 loop (19B and F39F) and chemokine coreceptor binding site (17B).
Fouda2013
(antibody binding site)
-
17b: 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 co-receptor binding site for 17b.
Hogan2018
(vaccine antigen design)
-
17b: 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.
deTaeye2018
(broad neutralizer)
-
17b: 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 non-NAb 17b, binds at a fraction of the binding of 2G12 to Env-ND, and this binding is slightly sensitive to glutaraldehyde treatment .
Witt2017
(vaccine antigen design, binding affinity)
-
17b: 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)
-
17b: 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 (including 17b), 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)
-
17b: 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. The 17b antibody was shown to have a steric clash with two other CD4bs Abs, GE136 and GE148, but not with VRC01.
Chen2016b
(antibody binding site, vaccine antigen design, vaccine-induced immune responses, structure)
-
17b: 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)
-
17b: 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. Mabs 17b and LF17 were used as anti-CoRBS Abs.
Ding2015
(effector function)
-
17b: 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)
-
17b: 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. N197 glycan mutants were tested against 17b showing a loss of tier 2 phenotype. The results are in Table S5.
Crooks2015
(glycosylation, neutralization)
-
17b: 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
-
17b: 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)
-
17b: 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. Non-neutralizing CD4i Ab, 17b did not bind cell surface or neutralize 92UG037.8 HIV-1 isolate, but it did bind well in the presence of sCD4.
Chen2015
(neutralization, binding affinity)
-
17b: PGT145 was used to positively isolate a subtype B Env trimer immunogen, B41 SOSIP.664, 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. Among non-NAbs to CD4bs (b6, F91, F105); to CD4i (17b); to gp41ECTO (F240); and to V3 (447-52D, 39F, CO11, 19b and 14e), none neutralized B41 (IC50 >50µg/ml).
Pugach2015
-
17b: 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. CD4i non-NAb, 17b binding was modestly increased by the initial binding of CD4bs bNAbs, VRC01, 3BNC60, NIH45-46.
Derking2015
(antibody interactions, neutralization, binding affinity, structure)
-
17b: Two clade C recombinant Env glycoprotein trimers, DU422 and ZM197M, with native-like structural and antigenic properties involving epitopes against 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 have almost no affinity for the CD4induced non-NAb, 17b, and 17b was unable to neutralize the equivalent pseudotyped viruses for either trimer.
Julien2015
(assay or method development, structure)
-
17b: 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. Binding of CD4i-epitope-recognizing non-NAb, 19b, to trimers was almost completely eliminated by trimer cross-linking.
Schiffner2016
(assay or method development, binding affinity, structure)
-
17b: 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-CDi non-NAb 17b 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)
-
17b: A panel of Env-specific mAbs was isolated from 6 HIV1-infected lactating women. Antibodies in colostrum may help prevent mucosal infection of the infant, so this study aimed to define milk IgGs for future vaccination strategies to reduce HIV transmission during lactation. Despite the high rate of VH 1-69 usage among colostrum Env specific B cells, it did not correlate with distinct gp120 epitope specificity or function. 17b was compared to the newly-derived mAbs; it didn't cross-react with gut bacteria, and tested negative in 2 tests of autoreactivity.
Jeffries2016
(antibody polyreactivity)
-
17b: A solution-phase ECL assay for ultrasensitive and quantitative analysis of binding affinities of HIV receptor and MAb interactions has been demonstrated. This study of binding of gp120 with anti CD4 mAb Q4120-CD4-tag and 17b-gp120 with CD4-tag shows that Q4120 can completely block the binding of gp120 with CD4-tag, while 17b can only partially block their binding. The results indicate that Q4120 can serve as a more effective neutralizing antibody than 17b to potentially block the HIV infection of T cells.
Xu2013
(antibody interactions, assay or method development)
-
17B: 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. MAb 17B itself did not block Env-Galcer binding, suggesting that the C1 Ab-induced gp120 conformational changes resulted in alteration in a Galcer binding site distant from the CD4i 17B MAb binding site.
Dennison2014
(antibody binding site, antibody interactions, effector function, glycosylation)
-
17b: 17b 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 CCR5BS binding Nab bound well at <10 nM to 3/5 chronic Envs, 3/6 Consensus Envs and 6/7 T/F Envs.
Liao2013c
(antibody interactions, binding affinity)
-
17b: The neutralization profile of 1F7, a human CD4bs mAb, is reported and compared to other bnNAbs. 1F7 competed with 17b for binding with gp120.
Gach2013
(neutralization)
-
17b: 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. 17b was used as a CD4b Ab control.
Gach2014
(neutralization, HAART, ART)
-
17b: 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. 17b was used in co-expression and cryoelectron tomography assays to understand the conformational changes in Env upon CD4 binding.
Veillette2014
(effector function, structure)
-
17b: 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. 17b was used as a control and A32 showed 4-6 fold higher ADCC activity than 17b.
Ferrari2011a
(effector function)
-
17b:X-ray crystallography, surface plasmon resonance and pseudovirus neutralization were used to characterize a heavy chain only llama antibody, named JM4. The full-length IgG2b version of JM4 neutralizes over 95% of circulating HIV-1 isolates. JM4 targets a hybrid epitope on gp120 that combines elements from both the CD4 binding region and the coreceptor binding surface. JM4 epitope overlaps with the CD4i binding site of 17b.
Acharya2013
(neutralization)
-
17b: 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-Abs, including 17b, against 181 diverse HIV-1 strains with available Ab-Ag complex structures.
Chuang2013
(computational prediction)
-
17b: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 17b is discussed as the CD4i CoRBS (Cluster C) region-targeting, neutralizing anti-gp120 mAb exhibiting ADCC activity and having a discontinuous epitope. Co-localization of the gp120HXBc2core CD4/17b complex (PDB:1GC1) was studied by tomogram of the chimera.
Pollara2013
(effector function, review, structure)
-
1.7B: This study mapped the amino acid changes in epitopes that led to escape from the initial autologous neutralizing Ab response in two HIV-1 B infected individuals. Escape occurred by different pathways but the responses appeared to be directed against the same region of gp120. In conclusion, a region just below the base of the V3 loop, near the coreceptor binding domain of gp120, can be a target for autologous neutralization. MAb 1.7B was used as a noncompeting human Ab in cross competition analysis.
Tang2011
(autologous responses, glycosylation, neutralization, escape, HAART, ART, structure)
-
17b: ADCC mediated by CD4i mAbs (or anti-CD4i-epitope mAbs) was studied using a panel of 41 novel mAbs. Three epitope clusters were classified, depending on cross-blocking in ELISA by different mAbs: Cluster A - in the gp120 face, cross-blocking by mAbs A32 and/or C11; Cluster B - in the region proximal to CoRBS (co-receptor binding site) involving V1V2 domain, cross-blocking by E51-M9; Cluster C - CoRBS, cross-blocking by 17b and/or 19e. The ADCC half-maximal effective concentrations of the Cluster A and B mAbs were generally 0.5-1 log lower than those of the Cluster C mAbs, and none of the Cluster A or B mAbs could neutralize HIV-1. Cluster A's A32- and C11-blockable mAbs were suggested to recognize conformational epitopes within the inner domain of gp120 that involve the C1 region. Neutralization potency and breadth were also assessed for these mAbs. No correlation was found between ADCC and neutralization Abs' action or functional responses.17b was used as the classical CoRBS Ab control in different assays, especially competition ELISA assays to determine epitope specificity.
Guan2013
(antibody interactions, effector function)
-
17b: This study uncovered a potentially significant contribution of VH replacement products which are highly enriched in IgH genes for the generation of anti-HIV Abs including anti-gp41, anti-V3 loop, anti-gp120, CD4i and PGT Abs. The VH replacement "footprints" within CD4i Abs preferentially encode negatively charged amino acids within IgH CDR3. The details of 17b VH replacement products in IgH gene and mutations and amino acid sequence analysis are described in Table 1,Table 2 and Fig 3.
Liao2013a
(antibody sequence)
-
17b: Cryoelectron tomography was used to determine structures of A12, m36, or m36/CD4 complexed to trimeric Env displayed on intact HIV-1 BaL virus. The foot print of m36 binding on gp120 is near the base of the V3 loop which resembles a "fully open" conformation similar to the coreceptor targeted CD4i mAb, 17b.
Meyerson2013
(antibody binding site, structure)
-
Lists 7 mAbs derived from patient N70: 15E, 1.9B, 2.3A, 2.3B, 2.1H, F91, 1.7B.
Robinson1992
-
17b: Systematic computational analyses of gp120 plasticity and conformational transition in complexes with CD4 binding fragments, mimetic proteins and Ab fragments is described to explain the molecular mechanisms by which gp120 interacts with the CD4bs at local and subdomain levels. An isotopic elastic network analysis, a full atomic normal mode analysis and simulation of conformational transitions were used to compare the gp120 structures in CD4 bound and 17b Ab-bound states.
Korkut2012
(structure)
-
17b: Design, synthesis, characterization and structures of gp120 in complex with dual hot-spot HIV-1 entry inhibitor small-molecules is reported. 17b was used as a surrogate for the co-receptor and structure of HIV-1 CD4:gp120:17b complex is described.
LaLonde2012
(structure)
-
17b: 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. 17b was used as an anti CD4 binding Ab to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets.
Smalls-Mantey2012
(assay or method development, effector function)
-
17b: 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. 17b was used as a CoRB-specific MAb to compare binding specificity of VRC06.
Li2012
-
17b: This is a comment on Tan2012. It is noted that Tran and colleagues used high-resolution 3D cryoelectron tomography to define the conformation of Env when bound to soluble CD4 and to a series of monoclonal antibodies. It was demonstrated that antibodies binding to the CD4 binding site or coreceptor binding site of Env may lead to significantly different conformations of the trimeric Env complex. VRC01 locks the complex in a closed conformation, while binding to soluble CD4 or the monoclonal antibody 17b fixed the trimer in an open conformation.
Wright2012
(review, structure)
-
17b: Previous cryo-electron tomographic studies were extended. A more complete picture of the HIV entry process was presented by showing that HIV-1 Env binding to either soluble CD4 (sCD4) or the co-receptor mimic 17b leads to the same structural opening, or activation, of the Env spike. Atudy also demonstrated structurally that the broadly neutralizing antibodies VRC01, VRC02, VRC03 are able to block this activation, locking Env in a state that resembles closed, native Env. The cryo-electron microscopic structure of soluble trimeric Env in the 17b-bound state is presented at ˜9 Å resolution, revealing it as a novel, activated intermediate conformation of trimeric Env that could serve as a new template for immunogen design.
Tran2012
(structure)
-
17b: 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)
-
17b: 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 MF59 adjuvant, but there was 3-fold decrease of antigenicity with FIA, C971, C974, C971+MF59 C971+MF59 as compared to the unadjuvanted sample.
Lai2012
(adjuvant comparison)
-
17b: 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. 17b had limited neutralizing activity recognizing the CD4 induced site and carried fewer somatic mutations than bnAbs. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 17b.
Klein2013
(neutralization, structure, antibody lineage)
-
17b: 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. Immobilized 17b Fab could capture gp120 even in the absence of CD4 and CD4 binding greatly increased the strength of interaction. In contrast, gp140 trimer bound to 17b Fab only in the presence of CD4, suggesting that gp120 portions of unligated epitope trimer are tightly confined in a conformation distinct from the CD4-bound state.
Kovacs2012
(antibody binding site, neutralization, binding affinity)
-
17b: 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. CD4 independence of the glycoprotein variants exhibits strong correlation with 17b binding. The viral sensitivity increases with the S375W mutation to 17b.
Haim2011
(antibody interactions)
-
17b: The study used the swarm of quasispecies representing Env protein variants to identify mutants conferring sensitivity and resistance to BnAbs. Libraries of Env proteins were cloned and in vitro mutagenesis was used to identify the specific AA responsible for altered neutralization/resistance, which appeared to be associated with conformational changes and exposed epitopes in different regions of gp160. The result showed that sequences in gp41, the CD4bs, and V2 domain act as global regulator of neutralization sensitivity. 17b was used as BnAb to screen Env clones. N197H mutation caused increase in neutralization by 17b, but failed in highest concentration.
ORourke2012
(neutralization)
-
17b: 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. 17b was used as a positive control Abs in competitive binding assay with non human primates mAbs.
Sundling2012
(vaccine-induced immune responses)
-
17b: 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. 17b was used in immunoprecipitation assay.
Melchers2012
(neutralization)
-
17b: 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. 17b was used to determine and compare the immunogenicity of homo and heterotrimers gp140s and to investigate the relative exposure of the CCR5 co-receptor binding site. The relative binding of 17b to the Q461/SF162 nonlinker heterotrimer was greater than expected.
Sellhorn2012
(vaccine antigen design)
-
17b: Crystal structures of unliganded core gp120 from HIV-1 clade B, C, and E were determined to understand the mechanism of CD4 binding capacity of unliganded HIV-1. The results suggest that the CD4 bound conformation represents "a ground state" for the gp120 core with variable loop. 17b was used as a control to prove whether the purified and crystallized gp120 is in the CD4 bound conformational state or not.
Kwon2012
(structure)
-
17b: 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. 17b was used in binding assays to compare glycosylated or deglycosylated JFRL and didn't exhibit strong binding to deglycosylated JRFL. The authors inferred that glycan interferences control the binding of unmutated ancestor Abs of broad neutralizing mAb to Env gp41.
Ma2011
(glycosylation, neutralization)
-
17b: 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. 17b was used as a control to compare the neutralizing activity of patients' sera. Mutated glycan 241 (N241S) had an increase neutralization sensitivity to 17b.
Lavine2012
(neutralization)
-
17b: 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. In the absence of CD4, the CD4i epitope MAb 17b, 48d, and 412d bound poorly to Env-wild-type and Env-hGM-CSF but efficiently to Env-ΔV1V2. Adding soluble CD4 substantially increased the binding of these MAb to Env-ΔV1V2 and especially to Env-wild-type, but binding to Env-hGM-CSF was improved only modestly, suggesting that the presence of GM-CSF in the V1V2 region either limits the accessibility of the CD4i epitopes or blocks the conformational changes that expose them.
vanMontfort2011
(vaccine antigen design)
-
17b: 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). MAbs 17b and E51, with restricted neutralizing activity, had pIs from 7 to 7.85. Plasma-derived, anti-gp120 IgG fractions in this range also had narrow neutralization breadth.
Sajadi2012
(polyclonal antibodies)
-
17b: 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, including MAb 17b, was used to analyze the antigenic integrity of the covalent complexes using capture ELISA.
Martin2011
(mimics, binding affinity)
-
17b: 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. 17b was largely ineffective in both inducing neutralization and shedding.
Ruprecht2011
(neutralization, kinetics)
-
17b: 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)
-
17b: 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)
-
17b: 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 effect on basal or sCD4-induced interactions between the trimers and the coreceptor binding site-directed MAb 17b.
Depetris2012
(glycosylation, binding affinity)
-
17b: 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. 17b did not bind to gp120 core, gp120 core D368R, RSC3, RSC3/G367R, RSC3 Δ3711, and RSC3 Δ3711/P363N.
Lynch2012
(binding affinity)
-
17b: The study followed the dynamics of alternating viral neutralization phenotype over time in 7 patients monitored for 1-5 years starting from seroconversion. While the development of neutralization resistance, including escape from the autologous antibody response was observed, there was also temporal emergence of viruses exquisitely sensitive to both autologous and heterologous Nabs. All Envs with heightened serum sensitivity were also potently neutralized by sCD4 and/or IgG1b12.Neutralization by 17b in the absence of sCD4 was also observed. In contrast, out of nineteen serum resistant env-chimeras only three were neutralized by 17b in absence of sCD4.
Aasa-Chapman2011
(autologous responses, escape)
-
17b: 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. In the absence of sCD4, binding of MAb 17b to immature particles was approximately 40% less than binding to mature particles. 17b, A1g8, and E51 binding to immature virions was stimulated by sCD4 to a greater or equal extent vs. mature particles, with MAb 17b exhibiting the greatest increase. Truncation of the CT abolished the enhanced sCD4-induced binding of 17b to immature particles. This suggested that CD4 binding triggers exposure of some epitopes to an equal extent on immature and mature virions and other epitopes to a greater extent on immature virions.
Joyner2011
(binding affinity)
-
17b: 17b MAb was used to study mechanism of neutralization by bnMAbs. In contrast to VRC01, PGV04 did not enhance 17b or X5 binding to their epitopes in the co-receptor region on the gp120 monomer, and in contrast to CD4, none of the CD4bs MAbs tested induced the 17b site on trimeric cleaved Env, suggesting that a degree of mimicry of CD4 by anti-CD4bs bnMAbs may be a consequence of binding to the CD4 epitope on monomeric gp120 rather than a neutralization mechanism.
Falkowska2012
(neutralization)
-
17b: Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies was studied by isolation of VRC01-like neutralizers with CD4bs probe; structural definition of gp120 recognition by RSC3-identified antibodies from different donors; functional complementation of heavy and light chains among VRC01-like antibodies; identification of VRC01 antibodies by 454 pyrosequencing; and cross-donor phylogenetic analysis of sequences derived from the same precursor germline gene. 17b was studied among other antibodies that derive from a common IGHV1-69 allele to assess how atypical the VRC01-like antibody convergence was. T The angular difference in heavy-chain orientation between 17b, 412d, and X5 was over 90°, or roughly 10 times as much as among the VRC01-like antibodies. 17b had 41-62% sequence identity of its heavy and light chains to respective chains of VRC-PG04 and VRC-CH31.
Wu2011
(structure)
-
17b: Molecular architectures of the soluble CD4 (sCD4)-bound states of SIV Env trimers for three different strains (SIVmneE11S, SIVmac239, and SIV CP-MAC) have been determined using cryo-electron tomography that showed only minor conformational changes following sCD4 binding in marked contrast to HIV-1 BaL, SIVmneE11S and SIVmac239. Binding of trimeric HIV-1gp120 to either sCD4 alone or to sCD4 in combination with the coreceptor mimic 17b results in an opening of the trimeric Env structure. Due to a dramatic difference between the angle of approach of MAbs 17b and that of SIV MAb 7D3, these Abs target epitopes on gp120 that are on opposites sides of the coreceptor binding site and in the vicinity of the V3 loop.
White2011
(antibody binding site, structure)
-
17b: To address the controversy of significant differences in chosen atomic coordinates of monomeric SIV gp120 in unliganded, and monomeric HIV-1 gp120 in various liganded and antibodybound states, the molecular architectures of trimeric Env from SIVmneE11S, SIVmac239 and HIV-1 R3A strains are shown to be closely comparable to that previously determined for HIV-1 BaL. The gp120 density profiles obtained from the coordinates of the trimeric Env complex with sCD4/17b (1GC1) and b12 (2NY7) are similar even though there are important differences in their atomic resolution structures.
White2010
(structure)
-
17b: 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. This MAb is noted in the review to be CD4i antibody and to have weak neutralizing activity against most HIV-1 isolates, with increased activity when soluble CD4 is added.
Gonzalez2010
(neutralization, variant cross-reactivity, escape, review)
-
17b: 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)
-
17b: 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. One Env clone each from patients IVC2 and IVC3 was neutralized by 17b suggesting spontaneous exposure of CD4i epitopes.
Ringe2010
(neutralization)
-
17b: 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. 17b neutralized wildtype sensitive clone and 6 out of 9 mutants tested (D179N, D179E, D179Q, D179H, D179S and D179A).
ORourke2010
(neutralization, variant cross-reactivity)
-
17b: MAb m9 showed superior neutralization potency compared to scFv 17b in a TZM-bl assay, where it neutralized all 15 isolates compared to 17b that neutralized only 2 isolates. Unlike m9, 17b did not compete with R5Nt for binding to gp120, indicating that the epitope for m9 differs from that of 17b.
Zhang2010
(neutralization)
-
17b: 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. High frequency and titers of 17b-like Abs were detected in all three vaccine trials. 58% of sera from the HVTN 203 trial, 75% of sera from the HVTN 041 trial, and 81% of sera from the DP6-001 trial were able to outcompete binding to 17b MAb.
Vaine2010
(antibody interactions)
-
17b: 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)
-
17b: 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. 17b was classified into CD4i group as it binds CD4. The number of 17b Abs needed to neutralize a single trimer was determined to equal 1 with 99.8% probability.
Magnus2010
-
17b: 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. MAb 17b was able to capture HIV-1 pseudovirions only in the presence of soluble CD4 and not in its absence. 17b did not induce the production of chemokines.
Moody2010
(binding affinity)
-
17b: The antigenic structure of Gag-Env pseudovirions was characterized and it was shown that these particles can recapitulate native HIV virion epitope structures. 17b exhibited low level binding to the Gag-Env pseudovirions that was markedly improved in the presence of sCD4, 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)
-
17b: 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 17b to gp120 was inhibited by B40t77, which is suggested to be due to the overlapping binding sites of the two molecules.
Joubert2010
(binding affinity, structure)
-
17b: Biological effects of mutating I309L in HIV-1 subtype C Envs was examined. 4/11 mutated Envs showed moderate increase in their neutralization sensitivity to 17b after incubation with sCD4, indicating that I309L affects the efficiency with which the coreceptor binding site is formed.
Lynch2010
(antibody binding site, neutralization)
-
17b: Unlike the MPER MAbs tested, 17b did not show any Env-independent virus capture in the conventional or in the modified version of the virus capture assay.
Leaman2010
-
17b: Impact of in vivo Env-CD4 interactions was studied during vaccinations of Rhesus macaques with two Env trimer variants rendered CD4 binding defective (368D/R and 423/425/431 trimers) and wild-type (WT) trimers. Ab binding profiles of the three trimer variants were assessed by binding analyses to different MAbs. coreceptor binding site (CoRbs) directed MAb 17b bound similarly to WT and 368D/R trimers but its binding affinity was completely abrogated for 423/425/431 trimers.
Douagi2010
(binding affinity)
-
17b: Peptide ligands for CD4i epitopes on native dualtropic Env were selected by phage display. The correct exposure of CD4i epitopes was detected with 17b, and incubation with sCD4 greatly enhanced its binding. An optimized synthetic peptide derivative (XD3) bound to all Env proteins analyzed with different coreceptor usage and inhibited binding of MAb 17b to immobilized gp120 in the presence and absence of sCD4 by 30 percent and 50 percent, respectively.
Dervillez2010
(binding affinity)
-
17b: 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)
-
17b: Expression of gp120 was shown to lead to the accumulation of both monomeric gp120 and aberrant dimeric gp120 forms. Dimeric forms of gp120 were not recognized by CD4i MAbs, such as 17b, nor by MAbs against the gp120 inner domain, but were recognized by CD4BS MAbs. It is suggested that gp120 dimerization occludes or disrupts the inner domain and/or the co-receptor binding site. Formation of gp120 dimers was reduced by removal of the V1/V2 loops or the N and C termini.
Finzi2010
(antibody binding site)
-
17b: 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 other MAbs (b12, 2G12, 2F5 and 4E10), neutralizing 100% of HIV-1 primary isolates of subtypes A, B, C, D, F, CRF01_AE and CRF02_AG. Unlike the other MAbs, sCD4-17b was equivalently active against virus particles generated from different producer cell types.
Lagenaur2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
17b: 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. In the absence of sCD4, 17b bound and neutralized ΔV1V2 variants more potently than the full-length trimer. Addition of sCD4 did not enhance 17b binding, as it was close to optimal without sCD4. 17b did not bind to the ΔV1V2 variant with V120K substitution. For the uncleaved variants, 17b bound to the ΔV1V2 but did not bind well to the full-length virus, unaffected by presence of sCD4.
Bontjer2010
(neutralization, binding affinity)
-
17b:The effect of amino acid polymorphisms on the structural stability and cooperative interactions of gp120, from A and B subtype HIV-1, were compared using microcalorimetric techniques. The impact of these polymorphisms on the binding mechanisms of gp120-A and gp120-B to the host cell surface receptors and coreceptors was also studied for development of entry inhibitors. The binding affinity of 17b is increased by CD4 for gp120-B but only minimally increased for gp120-A. Binding of 17b to gp120-A induced smaller enthalpy and entropy changes compared to 17b binding to gp120-B, indicating that binding of this Ab to gp120-A induces smaller conformational changes. The epitope for this Ab is highly conserved between gp120-A and gp120-B proteins, although 17b has 3-fold weaker affinity for gp120-A.
Brower2010
(kinetics, binding affinity, subtype comparisons)
-
17b: Neutralizing activities of 17b 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), with all viruses being resistant to neutralization by this Ab.
Binley2010
(glycosylation, neutralization)
-
17b: Binding of 17b to Env HIV-1 JR-FL increased gradually as the amount of CD4-mimicking small compound NBD-556 increased. Pretreatment by NBD-556 remarkably increased binding of 17b to JR-FL Env, indicating enhancement of 17b epitope accessibility by NBD-556.
Yoshimura2010
(mimics, binding affinity)
-
17b: A panel of 109 HIV-1 pseudoviruses was assessed for neutralization sensitivities to 17b 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. 3 Tier 1A, 6 Tier 1B, 1 Tier 2 but no Tier 3 viruses were found to be sensitive to neutralization by 17b.
Seaman2010
(neutralization)
-
1.7B: gp41 L669S mutant virus was moderately sensitive to neutralization by 1.7B while the L669 wild type virus was resistant. This indicates that conformational changes in the MPER could alter the exposure of neutralization epitopes in other regions of HIV-1 Env.
Shen2010
(neutralization)
-
17b: Fusion of CD4 with 17b scFv resulted in CD4-scFv17b reagent with neutralization potency comparable to other CD4-CD4i complexes. The neutralization potency was improved by inclusion of an IgG Fc region and by linkage of CD4 to the heavy chain of 17b. The resulting CD4hc-IgG17b neutralized a range of clade A, B and C viruses with potency comparable to other broadly neutralizing Abs. The complex, however, had low expression levels.
West2010
(neutralization, variant cross-reactivity, subtype comparisons)
-
17b: 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. 17b neutralized 5/6 chimeric viruses poorly, indicating that the quaternary structure of the spikes was maintained. One virus with the HA-tag inserted in the V2 loop was more sensitive to neutralization by 17b than the wild type, indicating that the HA tag had resulted in localized alternation of gp120.
Pantophlet2009
(neutralization)
-
17b: NAb specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. The integrity of gp120 beads in adsorption assay were validated by binding analysis to 17b. 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 17b. To test for presence of coreceptor binding region MAbs in sera, gp120 I420 mutant was used. This mutant was not recognized by 17b, and it could not adsorb binding activity of 17b 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)
-
17b: 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 is displayed.
Korber2009
(review)
-
17b: 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 V1/V2 deleted viruses were sensitive to neutralization by 17b, while the wild type and the evolved variants were resistant. This indicated that deletion of V1/V2 increases exposure of 17b epitope, and that the compensation mutations in the evolved viruses damage 17b epitope.
Bontjer2009
(antibody binding site, neutralization)
-
17b: 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. 17b bound with high affinity to CD4-bound but not to non-CD4-bound gp120 conformation. The number of mutations from the germline and the number of mutated contact residues for 17b were smaller than those for VRC01.
Zhou2010
(neutralization, binding affinity, structure)
-
17b: 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 17b. Memory B cells were selected that bound to RSC3 and full IgG mAbs were expressed. Binding of 17b to gp120 was enhanced by the addition of two newly detected mAbs VRC01 and VRC02.
Wu2010
(antibody interactions, binding affinity)
-
17b: Flexibility and rigidity of gp120 structures in isolation and in complex with CD4, CD4-mimics, and NAbs was analyzed using Floppy Inclusion and Rigid Substructure Topography program. The mean global flexibility of CD4/17b-bound gp12 was lower than that of b12-bound gp120. A common rigid core including residues 335-352 of gp120 was found, regardless of the strain or binding patterns.
Tan2009
(antibody binding site)
-
17b: 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 significantly increased 17b binding, even in the absence of CD4, and introduction of stabilizing F and D mutations significantly increased the on-rates of 17b interaction. Immunization assays revealed that the truncated core protein induced much higher titer of CD4bs-directed Abs than CD4i Abs, while conformationally stabilized mutant did the opposite.
Dey2009
(kinetics, binding affinity)
-
17b: A review about the in vivo efficacy of MAbs against HIV-1, and about inhibition of HIV-1 infection by MAb fragments (Fab, scFv), including single molecules or fusion proteins of 17b. Also, the efficacy of engineered human Ab variable domains or "domain antibodies" (dAbs) as therapeutic agents is reviewed.
Chen2009b
(neutralization, immunotherapy, review)
-
17b: Affinity and changes in enthalpy and entropy of 17b binding to gp120/sCD4 complex were evaluated. S22 peptide, which is a 22 aa tyrosine-sulfated peptide corresponding to the CCR5 N-terminal region, competitively inhibited 17b.
Brower2009
(kinetics, binding affinity)
-
17b: 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 17b.
Wu2009a
(binding affinity)
-
17b: 17b competed slightly with the broadly neutralizing Ab PG9 for binding to gp120.
Walker2009a
-
17b: Δ9-12a, 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 and to neutralization by 17b. TA1, a mutant with a 15 amino acid deletion of the distal half of V3, was extremely sensitive to neutralization by 17b.
Nolan2009
(neutralization)
-
17b: Binding of 17b 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
-
17b: EpiSearch is an algorithm that predicts the location of conformational epitopes on the surface of an antigen by using peptide sequences from phage display experiments as input and ranking surface exposed patches according to the frequency distribution of similar residues in the peptides and in the patch. When tested for 17b, the conformational epitope was predicted correctly with terminal cysteine residues, but when these were omitted the accuracy of the method was lowered.
Negi2009
(computational prediction)
-
17b: Subtype A gp140 SOSIP trimers were recognized by 17b.
Kang2009
-
17b: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:1-69, IGHD:nd, D-RF:nd, IGHJ:1. 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. Anti-CD4i mAbs exclusively used the VH1 gene family.
Gorny2009
(antibody sequence)
-
17b: Ten new non-neutralizing, cross-reactive mAbs were found in immunized mice. 17b was able to bind free virions, which was increased by addition of sCD4, while the newly detected mAbs could not bind free virions.
Gao2009
-
17b: 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 17b.
Davis2009
(neutralization)
-
17b: Two different but genetically related viruses, CC101.19 and D1/85.16, which are resistant to small molecule CCR5 inhibitors, and two clones from their inhibitor sensitive parental strain CC1/85, were used to analyze interactions of HIV-1 with CCR5. CC101.19 had 4 substitutions in the V3 region and D1/85.16 had 3 changes in gp41. CC101.19 was the most neutralization sensitive to 17b, while this Ab had limited neutralization activity to the two parental clones and to D1/85.16. However, gp120 from CC1/85 and D1/85.16 were the most reactive with 17b, and gp120 from all four viruses was equally reactive with 17b when sCD4 was added. This indicates that at least one major element of the CCR5 binding site has become accessible in the inhibitor-resistant CC101.19 virus.
Berro2009
(neutralization)
-
17b: 17b neutralized Tier 1 but not Tier 2 viruses. Crystal structure of F105 in complex with gp120 revealed that 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 bound by 17b, suggesting that 17b does not rely on access to the hydrophobic surface for binding. Binding affinity and kinetics of 17b binding to several gp120 variants as assessed.
Chen2009
(neutralization, kinetics, binding affinity)
-
17b: 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. 17b 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)
-
17b: An R5X4 HIV-1 strain, R3A, could tolerate partial loss of its V3 loop, but was poorly functional. After passage in tissue culture, the virus (now called TA1) still had a truncated V3 loop, but had acquired five mutations in its env gene and had also regained its function. TA1 was sensitive to neutralization by 17b MAb while the parental R3A was resistant to neutralization by this Ab. Viruses with Envs containing two or three of the five adaptive mutations were less sensitive to neutralization by 17b than TA1. Thus, the V3 truncation played a central role in sensitivity to 17b, but the adaptive mutations substantially increased sensitivity of the virus to 17b.
Agrawal-Gamse2009
(neutralization)
-
17b: 17b neutralized infection of PBLs with R5 HIV-1 strains with higher potency than X4 HIV-1 strains. However, 17b 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 17b, 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)
-
17b: 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 17b-gp120 interaction, but the CNV alone had a limited effect, indicating that the chimera has the high affinity binding property of the CNV molecule and the inhibitory property of the 12p1 peptide.
McFadden2007
-
17b: 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. The neutralizing activity of CD4i Abs, such as 17b, is discussed.
McKnight2007
(review)
-
17b: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 17b neutralization properties 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, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed.
Phogat2007
(review)
-
17b: 17b structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit 17b-like Abs, are reviewed in detail.
Lin2007
(review, structure)
-
17b: This review summarizes 17b Ab epitope, properties and neutralization activity. The effect of differential CCR5 cell surface expression on 17b neutralization activity is discussed.
Kramer2007
(co-receptor, neutralization, review)
-
17b: gp120 proteins with double mutation T257S+S375W, which alters the cavity at the epicenter of the CD4 binding region, showed a weak interaction with 17b in the absence of CD4 and efficient interaction with maximal 17b binding in the presence of 17b. Similar results were observed with unmodified gp120, indicating that although properly folded, the mutant proteins were not completely stabilized in the CD4-bound conformation by the two mutations. The gp120 proteins with double mutation T257S+S375W were 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 enhanced by 17b.
Dey2007a
(binding affinity)
-
17b: 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 17b MAb are described.
Willey2008
(review)
-
17b: 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 resistant to neutralization by 17b, while Envs from three chronically infected patients were unusually sensitive to neutralization by 17b. This indicated that the coreceptor binding surfaces on transmitted/founder Envs are conformationally masked.
Keele2008
(neutralization, acute/early infection)
-
1.7b: Transmission of HIV-1 by immature and mature DCs to CD4+ T lymphocytes was significantly higher for CXCR4- than for CCR5-tropic strains. Preneutralization of R5 virus with 1.7b prior to capture efficiently blocked transmission to 44%, while preineutralization of X4 virus with 1.7b had no effect, indicating that 1.7b treatment results in more efficient transfer of X4 than of R5 HIV-1.
vanMontfort2008
(co-receptor, neutralization, dendritic cells)
-
17b: 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 seven-fold more sensitive to neutralization by 17b than the parental virus, indicating that the CCR5 binding site of gp120 is partially exposed on the mutant virus without prior binding to CD4. These properties of the mutant virus were determined by alternations in gp41.
Taylor2008
(co-receptor, neutralization)
-
17b: Trimeric envelope glycoproteins with a partial deletion of the V2 loop derived from subtype B SF162 and subtype C TV1 were compared. The magnitude of 17b binding to subtype C trimer was lower than to subtype B trimer, either in the presence or absence of CD4. However, the fold increase in binding of 17b in presence of CD4 was similar for both subtypes, indicating similar structural rearrangements. 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)
-
17b: 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 17b, 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. None of the control or resistant viruses were sensitive to neutralization by 17b.
Pugach2008
(co-receptor, neutralization)
-
17b: 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 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. None of the patient envelopes were inhibited by 17b, indicating that 17b epitope is not more exposed on macrophage-tropic envelopes than on non-macrophage tropic ones.
Peters2008a
(neutralization)
-
17b: Crystal structures of CD4M47 (a derivative of a synthetic miniprotein with HIV-1 gp120 binding surface of the CD4 receptor incorporated) and a phenylalanine variant ((Phe23)M47) were determined in ternary complexes with HIV-1 gp120 and 17b Ab. The structures revealed correlation between mimetic affinity of the miniprotein for gp120 and overall mimetic-gp120 interactive surface.
Stricher2008
(structure)
-
17b: 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. All high affinity peptides inhibited the interactions of YU2 gp120 with 17b Ab. Inhibition was found to be concentration-dependent. 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. No inhibition of gp120 binding to 17b was observed for position 7 homoalanine-derived conjugates.
Gopi2008
-
17b: Requirements for elicitation of CD4i Abs were examined by immunizing non-primate monkeys, rabbits, and human-CD4 transgenic (huCD4) rabbits with trimeric gp140. The trimers were well recognized by 17b in the absence of CD4 but the relative binding affinity increased 2-5-fold in the presence of sCD4. The avidity of the trimers for 17b in the absence of CD4 was determined to be in the low nanomolar range. Sera from immunized monkeys were able to inhibit 17b binding at a 10-fold higher dilution than sera from immunized rabbits. 17b could bind to the gp140 trimers bound to cell-surface CD4 as well, confirming that the co-receptor site is accessible after trimer binding to membrane-bound CD4.
Forsell2008
(antibody binding site, binding affinity)
-
17b: Neutralization of JRFL, ADA, and YU2 isolates by 17b increased only modestly with increased dose of sCD4, and was never above 50%, indicating that the dose of sCD4, although enough to expose the V3 region, was insufficient to induce full conformational exposure of the co-receptor binding site.
Wu2008
(neutralization)
-
17b: 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 17b 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 17b epitope. gp140DF162ΔV2 was purified by the miniCD4 method to assess its ability to capture gp140 trimers. Binding of 17b 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)
-
17b: 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.17b provided some inhibition of binding of the three neutralizing VHH Abs to gp120, suggesting that 17b imposes steric hinderance to binding of the VHH Abs to gp120.
Forsman2008
(antibody interactions)
-
17b: Three-dimensional structures of trimeric Env displayed on native HIV-1 in complex with CD4 and the Fab fragment of 17b were compared to the unligated state, using cryo-electron tomography combined with three-dimensional image classification and averaging. Binding of 17b and CD4 resulted in dramatic conformational changes, including lever-like opening of the trimer. Binding of CD4 made way for exposure of gp41 stalk, and the V3 region was released from the lateral edge of the spike to point towards the target cell. V1/V2 and CD4 binding site moved away from the centre of the spike.
Liu2008
(antibody binding site, structure)
-
17b: V3 loop deletions were introduced into three different primary HIV-1 strains: R3A, DH12, and TYBE. The deletions included: ΔV3(12,12) containing the first and the last 12 residues of the V3 loop, ΔV3(9,9) containing first and last 9 residues, and ΔV3(6,6) containing first and last 6 residues. Only HIV-1 R3A ΔV3(9,9) was able to support cell fusion. Passaging of this virus resulted in a virus strain (TA1) that replicated with wildtype kinetics, and that acquired several adaptive changes in gp120 and gp41 while retaining the V3 loop truncation. 17b neutralized a ΔV1/V2 virus but failed to neutralize R3A or LAI. TA1 was 100-fold more sensitive to neutralization by 17b than the ΔV1/V2 virus.
Laakso2007
(neutralization)
-
17b: 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 17b, as the glycan at position 301 in the V3 loop was intact.
Hu2007
(neutralization, escape)
-
17b: 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. 17b captured both pseuduvirion preparations weakly in the absence of sCD4, but its binding was increased when sCD4 was also present. 17b failed to inhibit infection by either pseudovirus.
Dey2008
(binding affinity)
-
17b: 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 17b was used to analyze antigenic properties of construct 92UG-gp140-Fd, derived from isolate 92UG037.8 and stabilized by a C-terminal foldon tag. Uncleaved 92UG-gp140-Fd binds 17b, but only in the presence of CD4.
Frey2008
(binding affinity)
-
17b: 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 17b compared to wildtype. Also, there was no association between increased sensitivity to 17b neutralization and enhanced macrophage tropism.
Dunfee2007
(neutralization)
-
17b: 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 17b and other MAbs. Binding of 17b following CD4 also indicated presence of functionally relevant conformational changes of the proteins.
Gao2007
(review)
-
17b: 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 highest competition titers, being able to block gp120-CD4 complex interactions with 17b more efficiently than sera from animals immunized with the three other proteins.
DeVico2007
(neutralization)
-
17b: Interactions of this Ab with gp120 monomer and two cleavage-defective gp140 trimers were studied. It was shown that 17b interactions with the soluble monomers and trimers were dramatically decreased by GA cross-linking of the proteins, indicating that the 17b epitope was affected by cross-linking. This Ab was associated with a large entropy change upon gp120 binding. 17b 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)
-
17b: The neutralizing activity of coreceptor-binding site Abs, such as 17b, is reviewed.
Pantophlet2006
(antibody binding site, neutralization)
-
17b: The G314E escape variant highly resistant to KD-247 was shown to be more sensitive to 17b Ab than the wildtype virus. 17b was shown to be able to bind and neutralize the escape virus even in the absence of rsCD4 while rsCD4 was necessary for binding of 17b to the wildtype virus, indicating that the G314E mutation induces the expression of epitopes for Abs against CD4i epitope and V3 loop.
Yoshimura2006
(neutralization, escape, binding affinity)
-
17b: Binding of 17b in the presence or absence of CD4 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. In concordance with previous studies, 17b did not bind wt gp120 in absence of CD4 but did bind it in the presence of CD4. In contrast, the two deletion constructs did not bind 17b regardless of presence or absence of CD4 indicating that the loop-deleted gp120 is unable to close up the bridging sheet and display the coreceptor site and the 17b epitope.
Rits-Volloch2006
(antibody binding site, binding affinity)
-
17b: gp120 (monomer), gp120deltaV2 (trimer), gp140 (monomer) and gp140deltaV2 (trimer) from subtype B SF162 were expressed in cells and their affinity for 17b was assessed. All four Envs bound to 17b in the absence of CD4 but the monomers showed 3-fold higher affinity for this Ab than trimers. In the presence of CD4, the 17b epitope was up-regulated in all Envs.
Sharma2006
(antibody binding site, binding affinity)
-
17b: This Ab was used in a microcantilever deflection assay to detect gp120 from solution. Deflection twice that of the baseline that was detected upon specific binding of gp120 to cantilevers decorated on one side with A32 was further increased by subsequent incubation with 17b.
Lam2006
(assay or method development)
-
17b: Viruses with V2 mutations R166K, D167N and P175L were resistant to 17b and a reduction of binding 17b to these viral variants was observed.
Shibata2007
(escape, binding affinity)
-
1.7b: 1.7b-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 1.7b-HIV-1 complex was disassembled upon capture by DC-SIGN-cells.
vanMontfort2007
(neutralization, dendritic cells)
-
17b: Chimeric VLPs, containing chimeric Con-S ΔCFI Env proteins with heterologous signal peptide (SP), transmembrane (TM), and cytoplasmic tail (CT) sequences, were all induced to bind to 17b after binding to CD4, indicating that chimeric Envs in VLPs undergo conformational changes induced by CD4.
Wang2007a
(antibody binding site, vaccine antigen design, binding affinity)
-
17b: The structure of the 17b MAb, particularly its CDRH3 region tyrosine sulfation, is reviewed. Also, the mechanism of its binding to the coreceptor binding site of gp120, and comparisons of the neutralizing potencies of 17b Ab fragments vs the whole IgG molecule are discussed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed.
Burton2005
(antibody binding site, neutralization, review, structure)
-
17b: Monomeric gp120 and trimeric gp140CF proteins synthesized from an artificial group M consensus Env gene (CON6) did not bind to 17b directly, but bound to it following binding to sCD4 and A32, indicating correct conformational change and subsequent exposure of the 17b epitope.
Gao2005a
(antibody binding site, binding affinity)
-
17b: The structure of the V3 region in the context of gp120 core complexed to the CD4 receptor and to the 17b Ab was attempted to be determined by X-ray resolution, but only the structure for V3 complexed with CD4 and X5 Ab was solved. Accessibility of the co-receptor binding site to this MAb is shown in a 3D figure.
Huang2005
(antibody binding site, structure)
-
17b: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alterations of both gp41 and gp120. The alterations 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. 17b exhibited similar levels of binding to both the LLP-2 mutant and wildtype viruses, indicating that sCD4 binding to the LLP-2 mutant successfully triggered conformational change of gp120 and exposure of the co-receptor binding site.
Kalia2005
(antibody binding site, binding affinity)
-
17b: 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 17b, three of the modified proteins expressed in insect cells, including dV1V2 mutant (V1V2 deletions) followed by 3G-dV2-1G mutant (3G being mutations in three glycosylation sites and 1G being a mutation near the TM domain) and 3G-dV2 mutant, showed higher binding to the Ab than the wildtype did. This indicated that the dV1V2 mutant may expose 17b epitope better than the other Env proteins. When expressed in animal cells, only mutants 3G and dV2 showed enhanced binding to 17b but only at high concentrations of the MAb.
Kang2005
(antibody binding site, binding affinity)
-
17b: A stable trimerization motif, GCN4, was appended to the C terminus of YU2gp120 to obtain stable gp120 trimers (gp120-GCN4). Each trimer subunit was capable of binding IgG1b12, indicating that they were at least 85% active. D457V mutation in the CD4 binding site resulted in a decreased affinity of the gp120-GCN4 trimers for CD4 and for 17b. Both the CNG-gp120 trimers and the D457V mutants showed a restricted stochiometry to 17b of one Ab molecule binding per trimer. Removal of the V1-V2 loops resulted in binding of three 17b molecules per trimer.
Pancera2005a
(binding affinity, structure)
-
17b: R-FL and YU2 HIV-1 strains were not neutralized by 17b.17b and other non-neutralizing Abs only recognized JR-FL cleavage-defective glycoproteins, while the neutralizing Abs (2G12 and IgG1b12) recognized both cleavage competent and 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.17b, along with other Abs able to neutralize lab-adapted isolates, displayed enhanced viral entry at higher Ab concentrations, whereas the Abs that cannot neutralize any virus did not display such enhancement.
Pancera2005
(antibody binding site, enhancing activity, neutralization, binding affinity)
-
17b: 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 17b. 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)
-
17b: 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, variant cross-reactivity, review, structure)
-
17b: This Ab bound with an intermediate affinity to gp120IIIb, it did not prevent uptake of gp120 by APCs, and had no inhibitory effect on gp120 antigen presentation by MHC class II. 17b disassociated from gp120 at acidic pH. Lysosomal enzyme digestion of gp120 treated with 17b yielded fragmentation similar to that of gp120 alone, and digestion rate was intermediate, between the rapid digestion of gp120 alone and the slow digestion of gp120 in complex with high-affinity Ab5145A. It is thus concluded that CD4i Ab 17b does not have an inhibitory effect on gp120 processing and presentation.
Tuen2005
(antibody interactions, binding affinity)
-
17b: 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)
-
17b: A substantial fraction of soluble envelope glycoprotein trimers contained inter-subunit disulfide bonds. Reduction of these disulfide bonds decreased binding of 17b to the glycoprotein, indicating that the inter-S-S bonds contribute to the exposure of the CD4-induced region.
Yuan2005
(antibody binding site)
-
17b: Conformation of two gp120 constructs, gp120 bound to CD4D12 (the first two domains of human CD4), and gp120 bound to M9 (a 27-residue CD4 analog), was characterized by binding assays with Ab b17 in the presence or absence of soluble CD4D12. JRFL gp120 alone did not bind to b17 in the absence of CD4D12 but did bind in the presence of CD4D12. The gp120-CD4D12 construct bound to b17 in the absence of soluble CD4D12, and no enhancement in binding was observed when soluble CD4D12 was present, suggesting that all of the single chain was properly folded in the CD4i conformation. gp120-M9 construct also bound to 17b but with much lower affinity, and the binding was enhanced with presence of soluble CD4D12. This suggested that gp120-M9 single chain may contain both molecules where gp120 is bound to M9 in the CD4i conformation, and molecules resembling free gp120.
Varadarajan2005
(antibody binding site, kinetics, binding affinity)
-
17b: 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 were able to block binding of biotin-labeled 17b, indicating presence of CD4i Abs. These were the most frequently produced Abs from all three patients, suggesting that CD4i epitopes are much more immunogenic than previously appreciated.
Robinson2005
(assay or method development, HAART, ART)
-
17b: This review summarizes data on 447-52D and 2219 crystallographic structures when bound to V3 peptides and their corresponding neutralization capabilities. 17b, 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)
-
17b: A T-cell line adapted strain (TCLA) of CRF01_AE primary isolate DA5 (PI) was more neutralization sensitive to 17b than the primary isolate. Mutant virus derived from the CRF01_AE PI strain, that lacked N-linked glycosylation at position 197 in the C2 region of gp120, was significantly more sensitive to neutralization by 17b then the PI strain. Deglycosylated subtype B mutants at positions 197 and 234 were slightly more neutralizable by 17b.
Teeraputon2005
(antibody binding site, neutralization, subtype comparisons)
-
17b: 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). 17b bound to SF162gp140 and ΔV3gp140 more efficiently than to ΔV2gp140 and ΔV2ΔV3gp140. The neutralization of SF162 by 17b was enhanced in a concentration-dependent manner by pre-incubation with sCD4.
Derby2006
(antibody binding site, neutralization)
-
17b: This Ab bound to the Fc-gp120 construct, but only weakly to the chimeras lacking the V3 loop. sCD4 restored high affinity binding to all constructs.
Binley2006
(binding affinity)
-
17b: 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. Binding of this protein to the CCR5 co-receptor was inhibited by MAb 17b in a dose-dependent manner. The fusion protein did not activate the co-receptor by binding, and it potently neutralized primary R5 HIV-1.
Vu2006
(co-receptor)
-
17b: 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 17b.
Cham2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
17b: Neutralization of HIV-1 primary isolates from clade B by different formats of 17b 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 17b in cell lines with low CCR5.
Choudhry2006
(co-receptor, neutralization, variant cross-reactivity)
-
1.7b: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs.
Holl2006
(neutralization, dendritic cells)
-
17b: 17b was used as a negative control to test CDR3 tyrosine sulfation of MAbs 47e, 412d, CM51, E51, C12 and Sb1, since its CDR3 tyrosines are buried. As expected, 17b did not incorporate sulfates while the other MAbs did. Thus, the expression of 17b, or its binding to gp120 bound to CD4-Ig, was not affected by sulfation-inhibition. In addition, 17b was used as a positive control to test whether MAbs 47e, 412d, E51, Sc1 and C12 are CD4i Abs. Binding efficiency of all MAbs to ADA gp120 was doubled in the presence of CD4, showing that they are CD4-induced. scFv 17b was shown to efficiently bind to gp120 of three R5 isolates and to the HXBc2 X4 isolate. Neutralization assays showed that 17b was less efficient at neutralizing primary R5 and R5X4 isolates than MAbs 412d and E51, however, it was more efficient at neutralizing X4 isolates than these MAbs.
Choe2003
(antibody binding site, neutralization)
-
17b: The CDR3 regions of CD4i Abs (E51, 412d, 17b, C12 and 47e) were cloned onto human IgG1 and tested for their ability to inhibit CCR5 binding. Only E51 successfully immunoprecipitated gp120.
Dorfman2006
(co-receptor)
-
17b: 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. Both CD4 induced and A32 induced 17b was shown to bind specifically to all recombinant proteins except for the gp140δFI derived from subtype C virus. This Ab also bound specifically to one of the two tested subtype B gp120 proteins. The specific binding of his Ab to CON-S indicated that its conformational epitope was intact.
Liao2006
(antibody binding site, vaccine antigen design, subtype comparisons)
-
17b: The small molecule HIV-1 entry inhibitor IC9564 significantly enhanced binding of 17b Ab to gp120 on cell surface and on viral particles. The binding was independent of the presence of soluble CD4 suggesting that IC9564 induces conformational change in gp120 that exposes the concealed 17b epitope. Significant increase in neutralizing activity of 17b in the presence of IC9564 was observed for NLDH120 and NL4-3 virus strains. In contrast to CD4, IC9564 does not induce a conformational change in gp41, and inhibits CD4-induced gp41 conformational changes.
Huang2007
(antibody binding site)
-
17b: 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. 17b binding was induced similarly by sCD4 in the WT and stabilized forms. Non-neutralizing MAbs PA-1 and b6 bound less efficiently to the stabilized trimer.
Dey2007
(vaccine antigen design)
-
17b: 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. Protein disulfide isomerase treatment of rgp120 and rgp140 was found to severely inhibit binding of 17b, suggesting a structural need for V3-derived disulfide bonds in coreceptor binding. gp140 binding to 17b was 2-fold enhanced with by sCD4, indicating the proteolytically immature protein was able to undergo CD4i conformational changes.
Billington2007
(antibody binding site, co-receptor, vaccine antigen design)
-
17b: 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. CD4 inducible MAbs 17b and E51 were tested for the ability to neutralize the various forms of Con B; as anticipated gp160 and gp145 were not neutralized by these two MAbs, but the gp160-201N/S mutant was neutralized with IC50 values of 10 ug/ml, suggesting increased formation and/or exposure of the co-receptor binding site. The poorly infectious clone WITO4160.27 was also somewhat susceptible to neutralization by these clones.
Kothe2007
(vaccine antigen design, variant cross-reactivity)
-
17b: 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. CD4i MAbs (48d, 17b) did not bind to either GDMR or mCHO even with sCD4.
Selvarajah2005
(vaccine antigen design, vaccine-induced immune responses)
-
17b: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication 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 F105, IgG1b12, 17b and 48d, 2G12 and 447-52D. 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
-
17b: 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. D19b is unique among CD4i antibodies in that it binds to the V3 loop. CD4i MAbs 17b and 48d were used as controls for CD4i characterization; in contrast to D19, other CD4i MAbs bind to the conserved bridging sheet and do not differentiate between R5 and X4 using strains. 17b, like D19, was able to neutralize the BaL isolate only in combination with sCD4.
Lusso2005
-
17b: IgG antibody phage display libraries were created from HIV-1+ individuals after pre-selection of PBMC with gp120, as an alternative to using bone marrow for generating libraries. 17b was among a set of Abs used for competition studies to define the binding sites of the newly isolated MAbs, representing a MAb with a CD4i epitope.
Koefoed2005
-
17b: Called 1.7B. 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. 1.7B has no indication of polyspecific autoreactivity.
Haynes2005
(antibody binding site)
-
17b: 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 17b.
Pantophlet2004
(vaccine antigen design)
-
17b: 17b is known to be comprised of elements from four discontinuous beta strands. Using 17b MAb to select peptides from a combinatorial library, and analyzing the peptides using a novel discontinuous epitope reconstruction program, enabled epitope prediction. Segments of gp120 were reconstructed as an antigenic protein mimetic recognized by 17b. Comparisons then were made with a similar prediction of contact residues for CG10, a CD4i MAb that competes with 17b, but has a distinct binding site. Database note: First author "Enshell-Seijffers" is also found as "EnshellSeijffers" on annotated papers in this database.
Enshell-Seijffers2003
(antibody binding site, mimotopes, computational prediction)
-
17b: 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. Three CD4i MAbs were tested; all preferentially neutralized SF162, and JRFL became neutralization sensitive to CD4i Abs if the SF162 V1V2 loop was exchanged.
Pinter2004
(variant cross-reactivity)
-
17b: 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)
-
17b: 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 two sites adjacent to V3, C2 (GM292 C2) and (GM329 C3), increased neutralization susceptibility to CD4i FAb X5, but each of the glycan mutants and SF162 were refractive to neutralization with 48d and 17b. The loss of sites in C4 (GM438 C4), or V5 (GM454 V5) did not increase neutralization susceptibility to FAb X5. 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)
-
17b: 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 was decreased by trypsin, but increased by thrombin. Thrombin may increase HIV-induced cell fusion in blood by causing a conformational activating shift in gp120.
Ling2004
(antibody binding site)
-
17b: A pseudotyping assay showed that an X4 V3 loop peptide could enhance infectivity of X4 virus, R5 and R5X4 V3 loops peptides could enhance infectivity of an R5 virus, and R5X4 peptides could enhance infectivity of an R5X4 virus. Neither R5 nor R5X4 peptides influenced binding of CD4BS MAbs F105 and Ig1Gb12, but did increase binding of CD4i MAb 17b.
Ling2002
(antibody binding site, co-receptor)
-
17b: A32-rgp120 complexes opened 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. 17b was used as a control to show A32-bound rgp120 had enhanced binding to this CD4-inducible MAb.
Liao2004
(vaccine antigen design)
-
17b: 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
-
17b: Vaccination of a gp120-CD4 fusion complex in six transgenic XMG2 XenoMouse mice that produce human IgG2 with K light chain did not produce any neutralizing antibodies. 36/39 MAbs derived from one of these mice were in one of two competition groups that were conformational and specific for the complex, suggesting this chimeric vaccine may be of little value, as immunodominant responses recognized epitopes not present in native Env. MAbs from the two CD4-gp120 complex-specific competition groups did not compete with MAbs with known targets on HIV-1 gp120, but their binding was enhanced by binding of 17b.
He2003
-
17b: Using a cell-fusion system, it was found CD4i antibodies 17b, 48d, and CG10 reacted faintly with Env expressing HeLA cells even in the absence of sCD4 or CD4 expressing target cells. Reactivity increased after sCD4 addition, but not after CD4 expressing target cell addition, and binding was not increased at the cell-to-cell CD4-Env interface. This suggests the CD4i co-receptor binding domain is largely blocked at the cell-fusion interface, and so CD4i antibodies would not be able access this site and neutralize cell-mediated viral entry.
Finnegan2001
-
17b: This review summarizes MAbs directed to HIV-1 Env. There are six CD4 inducible MAbs and Fabs in the database. The MAb forms neutralize TCLA strains only, but the smaller Fabs and scFv fragments can neutralize primary isolates.
Gorny2003
(antibody binding site, review)
-
17b: 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)
-
17b: 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. This is a CD4i MAb that had no impact on 4KG5 binding.
Zwick2003a
(antibody interactions)
-
17b: The HIV-1 primary isolate DH012 has preserved the epitopes for the MAbs IgG1b12, 2G12, 17b, however natural DH012 infection in chimpanzees and DH012 gp120 vaccination in guinea pigs does not give rise to Abs against these epitopes.
Zhu2003
(vaccine-induced immune responses)
-
17b: 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. 17b recognized most variants, some from each of the four individuals, by gp120 immunoprecipitation.
Ohagen2003
(brain/CSF, variant cross-reactivity)
-
17b: 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)
-
17b: This paper describes the generation of CD4i MAb E51, that like CD4i MAb 17b, blocks CCR5 binding to sCD4-bound gp120. E51 has more cross-neutralizing potency than other prototype CD4i MAbs (17b) for B and C clade isolates. E51 and 17b both neutralized HIV-1 clade B strains HXBc2 and ADA, while JR-FL and 89.6 were only neutralized by E51, not 17b. Clade C strains MCGP1.3 and SA32 were both inhibited by 17b and E51, but E51 was more potent against SA32. The substitutions E381R, F383S, R419D I420R, K421D, Q422L, I423S, and Y435S (HXB2 numbering) all severely reduce 17b and E51 binding. All but I423S also diminish CCR5 binding by more than 50%. The mutation F383S also inhibits sCD4 binding and F105 binding, and K421D inhibits F105 binding, but not sCD4.
Xiang2003
(antibody binding site, variant cross-reactivity, subtype comparisons)
-
17b: This study shows the fragments of CD4i MAbs are better able to neutralize virus than whole IgG. Neutralization of HIV-1 R5 isolates JRFL, JR-CSF and ADA by CD4i MAbs X5, 17b, and 48d decreased with increased molecule size, the neutralizing potency of single-chain Fv (scFv) > than Fab fragments > whole Ab molecules. (With the exception of IgG 48d neutralization of HIV-1 ADA.) HIV-1 X4 isolates 89.6 and HxB2 are both relatively sensitive even to the larger IgG version. R5X4 isolate neutralization was dependent on the isolate and co-receptor usage. The CD4i MAb fragments neutralize HIV-1 subsequent to CD4 binding. The CD4i MAbs bind near the co-receptor binding sites on gp120. Co-receptors bind to the conserved beta19 strand and part of the V3 loop, regions that are masked by the V1V2 loops in the CD4-unbound state. When CD4 is bound, the co-receptor site is exposed near the membrane surface where it would be optimally accessible to co-receptors, and the smaller versions of the molecules are better able to overcome the steric hindrance.
Labrijn2003
(antibody binding site, co-receptor, variant cross-reactivity)
-
17b: 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. 17b was used to demonstrate that the Cluster I and II MAbs bound to gp120/gp41 complexes, not to gp41 after shedding of gp120.
Finnegan2002
-
17b: 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. It neutralized 5/6 R5 and X4 strains from the B clade, but was only moderately protective against a D clade isolate, and did not neutralize clade A, C, E, and F isolates.
Dey2003
(co-receptor, immunoprophylaxis, variant cross-reactivity, immunotherapy, subtype comparisons)
-
17b: Called 1.7b. The MAb B4e8 binds to the base of the V3 loop, neutralizes multiple primary isolates and was studied for interaction with other MAbs. B4e8 enhanced binding of CD4i MAbs 4.8d, 1.7b, and A1g8 to R5X4 virus 92HT593, but only of 48d to the R5 virus 92US660, and there was only a modest impact of the combination of B4e8 and CD4i MAbs on neutralization.
Cavacini2003
(antibody interactions, co-receptor)
-
17b: 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. Anti-V3 MAb B4a1 increased binding of CD4i MAbs 48d, 17b and A1g8, but only A1g8 binding was increased by B4a1 to the R5 isolate. Additive effects on neutralization of the R5X4 isolate with B4a1 and CD4i MAbs was observed, presumably due to increased exposure of the CD4i binding site, but not for the R5 isolate. Anti-gp41 MAb F240 had a synergistic effect on neutralization with CD4i MAbs 48d and 17b, but not with A1g8 for the R5X4 virus.
Cavacini2002
(antibody interactions, co-receptor, variant cross-reactivity)
-
17b: 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. CD4i Abs 17b and X5 were weakly neutralizing in all formats, WT, SOS, and when added postbinding.
Binley2003
(vaccine antigen design)
-
17b: NIH AIDS Research and Reference Reagent Program: 4091.
-
17b: The two N-terminal domains of CD4, termed D1 and D2, when expressed in the absence of the remaining domains of CD4 retain the capacity to bind to gp120---coding sequences of D1D2 and Igαtp were fused to create a large, multivalent rec protein D1D2Igαtp, which, unlike CD4, does not enhance infection at sub-optimal concentrations---the MAb 17b can also enhance viral replication at sub-optimal concentrations, but D1D2-Igα inhibited the 17b enhancement of two primary isolates.
Arthos2002
(variant cross-reactivity)
-
17b: 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
-
17b: gp120 mutants were used to define the CXCR4 binding site using CXCR4 displayed on paramagnetic proteoliposomes (PMPLs) to reduce non-specific gp120 binding---basic residues in the V3 loop and the β19 strand (RIKQ, positions 419-422) were involved, and deletion of the V1-V2 loops allowed CD4-independent CXCR4 binding---MAbs 17b (CD4i) and F105 (CD4BS) were used to study conformational changes in the mutants---the affinity of ΔV1 and ΔV1-V2 for 17b was dramatically increased and no longer inducible in the presence of sCD4---V3 mutants R298A and R327A were not recognized by 17b except in the presence of sCD4---mutations in the β19 strand dramatically reduced 17b affinity in the presence or absence of sCD4, consistent with known 17b contact residues in this region.
Basmaciogullar2002
-
17b: 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---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---non-neutralizing MAbs C11 and A32 bound with lower affinity than NAb IgG1b12---the MAb 17b was sCD4 inducible on gp160ΔCT PL.
Grundner2002
(vaccine antigen design)
-
17b: 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
(vaccine-induced immune responses)
-
17b: Five CD4i MAbs were studied, 17b, 48d and three new MAbs derived by Epstein-Barr virus transformation of PBMC from an HIV+ long term non-progressor -- 23e and 21c were converted to hybridomas to increase Ab production -- all compete with the well-characterized 17b CD4i MAb in an ELISA antigen capture assay -- critical binding residues are mapped and the CD4i MAb epitopes were distinct but share a common element near isoleucine 420, also important for CCR5 binding, and all five can block CCR5 binding to a sCD4-gp120 complex -- the MAb 48d has the epitope most similar to the CCR5 binding site.
Xiang2002b
(antibody binding site)
-
17b: 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
(variant cross-reactivity)
-
17b: CD4 residue Phe43 significantly contributes to the affinity of CD4-gp120 interactions -- despite decreased affinities for gp120, CD4 proteins and CD4-mimetic peptides lacking a Phe side-chain enhance binding of gp120 to 17b in a manner similar to Phe-bearing ligands indicating the Phe42 interaction is not critical for CD4-induced conformational changes in gp120.
Dowd2002
-
17b: 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 gp140Δ683(-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 C11, A32, and 30D which did not bind the stabilized oligomer.
Yang2002
-
17b: 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.
Schulke2002
(vaccine antigen design)
-
17b: 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
-
17b: 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 -- 17b recognized both gp120 monomer and o-gp140.
Srivastava2002
-
17b: 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 -- the 17b epitope is masked prior to CD4 binding by the V1-V2 loop and in contrast to sCD4, the binding of cell surface CD4 to virus does not appear to make the epitope accessible to binding by 17b to allow neutralization.
Poignard2001
(antibody binding site, review)
-
17b: 17b binds to a CD4 inducible epitope which partially overlaps the CCR5 binding site -- JRFL, YU2, 89.6, and HXB2 and their C1-, V1/V2-, C5 -deletion mutants were used to study how 17b binding affects gp120-CD4 interactions -- 17b reduced CD4-gp120 interactions by decreasing the on-rate and increasing the off-rate of sCD4, while enhanced binding of sCD4 binding was observed for the 17b-bound, V1/V2 deleted gp120s -- 17b was considered to be a surrogate for CCR5, and the authors suggest that 17b binding may shift V1/V2 into a position that interferes with CD4 binding, forcing a release.
Zhang2001a
(antibody binding site, kinetics)
-
17b: 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 -- 17b bound at somewhat greater levels to 168C than to 168P, but this is not a general feature of 17b binding to primary versus TCLA strains.
York2001
(variant cross-reactivity)
-
17b: 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 17b---only the CD4i antibodies 17b and 48d showed an increased affinity of the CD4 independent viruses relative to wild-type.
Kolchinsky2001
(antibody binding site, variant cross-reactivity)
-
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
(variant cross-reactivity)
-
17b: Mutagenesis defines Ile-420, Lys-421, Gln-422, Pro-438, and Gly-441 to be important residues for CCR5 binding -- these positions are located on two strands that connect the gp120 bridging sheet and outer domain, suggesting a mechanism for conformational shifts induced by CD4 binding to facilitate CCR5 binding.
Rizzuto2000
(antibody binding site)
-
17b: 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) that preserve and expose some neutralizing epitopes while occluding some non-neutralizing epitopes -- CD4BS MAbs (F105 and F91) and CD4i (17b and 48d) recognized gp140-GNC4 as well as gp120 or gp140 -- non-neutralizing MAbs C11, A32, 522-149, M90, and #45 bound to the gp140-GNC4 glycoprotein at reduced levels compared to gp120 -- MAbs directed at the extreme termini of gp120 C1 (135/9 and 133/290) and C5 (CRA-1 and M91) bound efficiently to gp140-GNC4.
Yang2000
(vaccine antigen design)
-
17b: Soluble gp140 derived from SF162, a neutralization-resistant primary isolate, and SF162AV2 a neutralization-susceptible isolate with 30 amino acids deleted from the V2 loop, were generated with or without the gp120-gp41 cleavage site intact -- all forms are recognized by oligomer-specific MAb T4 and show enhanced binding of CD4i MAb 17b when sCD4 is bound -- the fused forms are less efficiently recognized than the cleaved forms by polyclonal neutralizing sera from HIV-infected patients -- the V3 loop is more exposed on the fused form.
Stamatatos2000
(vaccine antigen design)
-
17b: sCD4 can activate fusion between effector cells expressing Env and target cells expressing coreceptor (CCR5 or CXCR4) alone without CD4 -- CD4i MAbs 17b and 48d have little effect on a standard cell fusion assay but potently block sCD4 activated fusion -- 17b was broadly cross-reactive inhibiting sCD4 activated fusion with Env from clades A, B, C, D, E, F, and F/B.
Salzwedel2000
(subtype comparisons)
-
17b: 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)
-
17b: SF162 is a neutralization-resistant HIV-1 isolate -- N-linked glycosylation modifications in the V2 loop of the SF162 gp120 revealed that these sites prevent neutralization by CD4BS MAbs (IgG1b12 and IgGCD4), and protect against neutralization by V3 MAbs (447-D and 391-95D) -- V2-region glycosylation site mutations did not alter neutralization resistance to V2 MAbs (G3.4 and G3.136) or CD4i MAbs (17b and 48d) -- V2 glycosylation site modification allows infection of macrophages, probably due to glycosylated forms requiring fewer CCR5 molecules for viral entry.
Ly2000
(variant cross-reactivity)
-
17b: 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)
-
17b: 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
(vaccine antigen design)
-
17b: A CD4-independent viral variant of IIIB, IIIBx, was generated on CXCR4-expressing cells -- IIIBx exhibited greater exposure of the 17b and 48d epitopes and enhanced neutralization by CD4i MAbs and by polyclonal human sera -- the 17b epitope has significant overlap with the CCR5 coreceptor binding site.
Hoffman1999
(antibody binding site, variant cross-reactivity)
-
17b: 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 enabled neutralization by CD4i MAbs 17b and 48d.
Stamatatos1998
(antibody binding site, vaccine antigen design)
-
17b: A panel of MAbs was 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 -- CD4i MAbs 17b and 48d bound better to the deleted protein than to wild type.
Binley1998
(antibody binding site)
-
17b: 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, and the presence of V1/V2 increased the enhancement -- a similar effect is observed by sub-neutralizing concentrations of sCD4 and the effect is dependent of CCR5 -- 17b enhances YU2 enhanced viral entry 10-fold, whereas HXBc2 was neutralized.
Sullivan1998b
-
17b: sCD4 induces 17b binding in primary isolates and TCLA strains -- amino acids that reduce the efficiency of binding were determined and found also to compromise syncytia formation and viral entry -- V1V2 deletion or sCD4 binding can expose the 17b epitope for both HXBc2 and macrophage tropic YU2 -- neutralizing potency of 17b is probably weak due to poor exposure of the epitope -- 17b epitope exposure upon sCD4 binding can occur over a wide range of temperatures, consistent with the energy of CD4 binding being sufficient to drive the V1/V2 loop into a new conformation.
Sullivan1998
(antibody binding site, variant cross-reactivity)
-
17b: Site directed mutagenesis of a WU2 protein with the V1-V2 loops deleted revealed key residues for 17b-gp120 interaction and interaction of gp120 and CCR5 -- mutations in residues that reduced 17b by 70% were R/D 419, I/R 420, Q/L 422, Y/S 435, I/S 423, K/D 121 and K/D 421-- 17b can neutralize HIV-1 strains that use different chemokine receptors, supporting a common region in gp120 in chemokine-receptor interaction.
Rizzuto1998
(antibody binding site, variant cross-reactivity)
-
17b: Moore and Binley provide a commentary on the papers by Rizzuto1998, Wyatt1998 and Kwong1998 -- they point out 17b shares binding elements in gp120 with chemokine receptor molecules, and that CD4 needs to bind to gp120 first to make the 17b epitope accessible and it may be sterically blocked in the CD4 bound virus, thus making it a poor NAb for primary isolates Moore1998.
Kwong1998,Moore1998,Rizzuto1998,Wyatt1998
(review, structure)
-
17b: Summary of the implications of the crystal structure of a gp120 core bound to CD4 and 17b, combined with what is known about mutations that reduce NAb binding to gp120 -- probable mechanism of neutralization is interference with chemokine receptor binding -- mutations in 88N, 117K, 121K, 256S, 257T, N262, Delta V3, E370, E381, F 382, R 419, I 420, K 421, Q 422, I 423, W 427, Y 435, P 438, M 475 of HXBc2 (IIIB) reduce binding -- the only variable residues in gp120 that contact 17b are 202T and 434M -- the contact points for 17b with the crystallized incomplete gp120 are mostly in the heavy chain of the Ab, and there is a gap between 17b's light chain and the partial gp120 which may be occupied by the V3 loop in a complete gp120 molecule -- the authors propose that the V2 and V3 loops may mask the CD4i Ab binding site, and that the V2 loop may be repositioned upon CD4 binding.
Wyatt1998
(structure)
-
17b: 17b Fab was co-crystallized with a gp120 core and CD4, and its binding site can be directly visualized---17b binds to the "bridging sheet" of gp120, an antiparallel beta sheet region, contacting residues from the C4 region and the V1/V2 stem---the contact area is small for an Ab-antigen interactive surface, and dominated in the Ab by the heavy chain---the center of the binding region has hydrophobic interactions, and the periphery charge interactions, acidic on 17b and basic on gp120.
Kwong1998
(structure)
-
17b: Neutralizes TCLA strains, but not primary isolates.
Parren1997
(variant cross-reactivity)
-
17b: Binds to sgp120 efficiently, but not soluble gp120+gp41, suggesting its gp120 epitope is blocked by gp41 binding -- partial re-exposure if sCD4 was bound -- could not bind to HXBc2 gp120 if the 19 C-term amino acids were deleted in conjunction with amino acids 31-93 in C1, but binding was restored in the presence of sCD4.
Wyatt1997
(antibody binding site)
-
17b: Virus with the V1-V2 loop deleted was viable and more susceptible to neutralization by CD4i mAb 17b, and anti-V3 MAbs 1121, 9284, and 110.4, but not to a CD4BS mAb, F105, or sCD4.
Cao1997
(vaccine antigen design)
-
17b: 48d binds to the IIIB protein and not IIIB V3 peptide, while binding to the Can0A V3 peptide, suggesting Can0A V3 is a conformer that mimics the 48d -- it does not bind to 17b, distinguishing the epitopes.
Weinberg1997
-
17b: One of 14 human mAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env -- 17b has synergistic response in combination with anti-V3 mAb 694/98-D.
Li1997
-
17b: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 17b bound monomer, oligomer, and neutralized JRFL in the presence of sCD4, but if sCD4 was not present, 17b only bound monomer.
Fouts1997
-
17b: Neutralizes JR-FL -- inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study.
Trkola1996b
-
17b: MIP-1α binding to CCR-5 expressing cells can be inhibited by gp120-sCD4 --- binding of 17b blocks this inhibition.
Wu1996
-
17b: Binding did not result in significant gp120 dissociation from virion, in contrast to 48d, although the gp41 epitope of mAb 50-69 was exposed.
Poignard1996b
(antibody interactions)
-
17b: Many mAbs inhibit binding (anti-C1, -C5, -C4, -CD4BS) -- anti-V3 mAb 5G11 enhances binding, as do C1-C4 discontinuous epitopes A32 and 2/11c -- enhances binding of some anti-V2 MAbs.
Moore1996
(antibody interactions)
-
17b: Binds with higher affinity to monomer and oligomer, slow association rate, poor neutralization of lab strain -- this is in contrast to 48d, which has very different kinetics.
Sattentau1995a
(kinetics, binding affinity)
-
17b: Studies using a V1/V2 deletion mutant demonstrated that enhanced binding of 17b in the presence sCD4 involves the V1/V2 loops, with more significant involvement of V2 -- similar effect observed for 48d and A32.
Wyatt1995
(antibody binding site, vaccine antigen design)
-
17b: A mutation in gp41, 582 A/T, confers resistance to neutralization (also confers resistance to mAbs F105, 48d, 21h and 15e).
Thali1994
(variant cross-reactivity)
-
17b: Binding of 48d is much more influenced by sequence variation among molecular clones of LAI than is binding of 17b.
Moore1993d
(variant cross-reactivity)
-
17b: Epitope is better exposed upon CD4 binding to gp120 -- competes with 15e and 21h, anti-CD4 binding site mAbs -- 113 D/R, 252 R/W, 257 T/A or G, 370 E/D, 382 F/L, 420 I/R, 433A/L, 438 P/R and 475 M/S confer decreased sensitivity to neutralization.
Thali1993
(antibody binding site, antibody interactions)
-
17b: LANL database note - 48d and 17b have similar epitopes, and the pair are unique among human and rodent mAbs. Thali1993 mentions that 17b and 48d were derived from different patients, and cites the original generation of these antibodies to Robinson and Ho, unpublished data. 17b is a CHAVI reagent (http://chavi.org/); Species: human; Category: CD4i MAbs; Contact person: James Robinson.
(antibody binding site, antibody generation)
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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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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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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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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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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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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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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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Ditzel1997
H. J. Ditzel, P. W. Parren, J. M. Binley, J. Sodroski, J. P. Moore, C. F. Barbas, III, and D. R. Burton. Mapping the Protein Surface of Human Immunodeficiency Virus Type 1 gp120 Using Human Monoclonal Antibodies from Phage Display Libraries. J. Mol. Biol., 267:684-695, 1997. (Genbank: U82767 U82768 U82769 U82770 U82771 U82772 U82942 U82943 U82944 U82945 U82946 U82947 U82948 U82949 U82950 U82951 U82952 U82961 U82962) Recombinant monoclonal antibodies from phage display libraries provide a method for Env surface epitope mapping. Diverse epitopes are accessed by presenting gp120 to the library in different forms, such as sequential masking of epitopes with existing MAbs or sCD4 prior to selection or by selection on peptides. Fabs identified by these methods have specificities associated with epitopes presented poorly on native multimeric envelope. PubMed ID: 9126846.
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Dorfman2006
Tatyana Dorfman, Michael J. Moore, Alexander C. Guth, Hyeryun Choe, and Michael Farzan. A Tyrosine-Sulfated Peptide Derived from the Heavy-Chain CDR3 Region of an HIV-1-Neutralizing Antibody Binds gp120 and Inhibits HIV-1 Infection. J. Biol. Chem., 281(39):28529-28535, 29 Sep 2006. PubMed ID: 16849323.
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Douagi2010
Iyadh Douagi, Mattias N. E. Forsell, Christopher Sundling, Sijy O'Dell, Yu Feng, Pia Dosenovic, Yuxing Li, Robert Seder, Karin Loré, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. Influence of Novel CD4 Binding-Defective HIV-1 Envelope Glycoprotein Immunogens on Neutralizing Antibody and T-Cell Responses in Nonhuman Primates. J. Virol., 84(4):1683-1695, Feb 2010. PubMed ID: 19955308.
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Dowd2002
Cynthia S. Dowd, Stephanie Leavitt, Gregory Babcock, Alexis P. Godillot, Don Van Ryk, Gabriela A. Canziani, Joseph Sodroski, Ernesto Freire, and Irwin M. Chaiken. Beta-Turn Phe in HIV-1 Env Binding Site of CD4 and CD4 Mimetic Miniprotein Enhances Env Binding Affinity but Is Not Required for Activation of Co-Receptor/17b Site. Biochemistry, 41(22):7038-7046, 4 Jun 2002. PubMed ID: 12033937.
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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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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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Enshell-Seijffers2003
David Enshell-Seijffers, Dmitri Denisov, Bella Groisman, Larisa Smelyanski, Ronit Meyuhas, Gideon Gross, Galina Denisova, and Jonathan M. Gershoni. The Mapping and Reconstitution of a Conformational Discontinuous B-Cell Epitope of HIV-1. J. Mol. Biol., 334(1):87-101, 14 Nov 2003. PubMed ID: 14596802.
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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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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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Finnegan2001
Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Envelope during Cell-Cell Fusion. J. Virol., 75(22):11096-11105, Nov 2001. PubMed ID: 11602749.
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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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Finzi2010
Andrés Finzi, Beatriz Pacheco, Xin Zeng, Young Do Kwon, Peter D. Kwong, and Joseph Sodroski. Conformational Characterization of Aberrant Disulfide-Linked HIV-1 gp120 Dimers Secreted from Overexpressing Cells. J Virol Methods, 168(1-2):155-161, Sep 2010. PubMed ID: 20471426.
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Forsell2008
Mattias N. E. Forsell, Barna Dey, Andreas Mörner, Krisha Svehla, Sijy O'dell, Carl-Magnus Högerkorp, Gerald Voss, Rigmor Thorstensson, George M. Shaw, John R. Mascola, Gunilla B. Karlsson Hedestam, and Richard T. Wyatt. B Cell Recognition of the Conserved HIV-1 Co-Receptor Binding Site Is Altered by Endogenous Primate CD4. PLoS Pathog., 4(10):e1000171, 2008. PubMed ID: 18833294.
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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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Fouda2013
Genevieve G. Fouda, Tatenda Mahlokozera, Jesus F. Salazar-Gonzalez, Maria G. Salazar, Gerald Learn, Surender B. Kumar, S. Moses Dennison, Elizabeth Russell, Katherine Rizzolo, Frederick Jaeger, Fangping Cai, Nathan A. Vandergrift, Feng Gao, Beatrice Hahn, George M. Shaw, Christina Ochsenbauer, Ronald Swanstrom, Steve Meshnick, Victor Mwapasa, Linda Kalilani, Susan Fiscus, David Montefiori, Barton Haynes, Jesse Kwiek, S. Munir Alam, and Sallie R. Permar. Postnatally-Transmitted HIV-1 Envelope Variants Have Similar Neutralization-Sensitivity and Function to That of Nontransmitted Breast Milk Variants. Retrovirology, 10:3, 2013. PubMed ID: 23305422.
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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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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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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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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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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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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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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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Guan2013
Yongjun Guan, Marzena Pazgier, Mohammad M. Sajadi, Roberta Kamin-Lewis, Salma Al-Darmarki, Robin Flinko, Elena Lovo, Xueji Wu, James E. Robinson, Michael S. Seaman, Timothy R. Fouts, Robert C. Gallo, Anthony L. DeVico, and George K. Lewis. Diverse Specificity and Effector Function Among Human Antibodies to HIV-1 Envelope Glycoprotein Epitopes Exposed by CD4 Binding. Proc. Natl. Acad. Sci. U.S.A., 110(1):E69-E78, 2 Jan 2013. PubMed ID: 23237851.
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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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Guenaga2015a
Javier Guenaga, Viktoriya Dubrovskaya, Natalia de Val, Shailendra K. Sharma, Barbara Carrette, Andrew B. Ward, and Richard T. Wyatt. Structure-Guided Redesign Increases the Propensity of HIV Env To Generate Highly Stable Soluble Trimers. J. Virol., 90(6):2806-2817, 30 Dec 2015. PubMed ID: 26719252.
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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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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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Harris2011
Audray Harris, Mario J. Borgnia, Dan Shi, Alberto Bartesaghi, Haifeng He, Robert Pejchal, Yun (Kenneth) Kang, Rafael Depetris, Andre J. Marozsan, Rogier W. Sanders, Per Johan Klasse, Jacqueline L. S. Milne, Ian A. Wilson, William C. Olson, John P. Moore, and Sriram Subramaniam. Trimeric HIV-1 Glycoprotein gp140 Immunogens and Native HIV-1 Envelope Glycoproteins Display the Same Closed and Open Quaternary Molecular Architectures. Proc. Natl. Acad. Sci. U.S.A., 108(28):11440-11445, 12 Jul 2011. PubMed ID: 21709254.
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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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Haynes2010
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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He2003
Yuxian He, Paul D'Agostino, and Abraham Pinter. Analysis of the Immunogenic Properties of a Single-Chain Polypeptide Analogue of the HIV-1 gp120-CD4 Complex in Transgenic Mice That Produce Human Immunoglobulins. Vaccine, 21(27-30):4421-4429, 1 Oct 2003. PubMed ID: 14505925.
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Hicar2010
Mark D. Hicar, Xuemin Chen, Bryan Briney, Jason Hammonds, Jaang-Jiun Wang, Spyros Kalams, Paul W. Spearman, and James E. Crowe, Jr. Pseudovirion Particles Bearing Native HIV Envelope Trimers Facilitate a Novel Method for Generating Human Neutralizing Monoclonal Antibodies Against HIV. J. Acquir. Immune Defic. Syndr., 54(3):223-235, Jul 2010. PubMed ID: 20531016.
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Hoffman1999
T. L. Hoffman, C. C. LaBranche, W. Zhang, G. Canziani, J. Robinson, I. Chaiken, J. A. Hoxie, and R. W. Doms. Stable exposure of the coreceptor-binding site in a CD4-independent HIV-1 envelope protein. Proc. Natl. Acad. Sci. U.S.A., 96(11):6359--64, 25 May 1999. URL: http://www.pnas.org/cgi/content/full/96/11/6359. PubMed ID: 10339592.
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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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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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Huang2005
Chih-chin Huang, Min Tang, Mei-Yun Zhang, Shahzad Majeed, Elizabeth Montabana, Robyn L. Stanfield, Dimiter S. Dimitrov, Bette Korber, Joseph Sodroski, Ian A. Wilson, Richard Wyatt, and Peter D. Kwong. Structure of a V3-Containing HIV-1 gp120 Core. Science, 310(5750):1025-1028, 11 Nov 2005. PubMed ID: 16284180.
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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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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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Jeffries2016
T. L. Jeffries, Jr., C. R. Sacha, J. Pollara, J. Himes, F. H. Jaeger, S. M. Dennison, E. McGuire, E. Kunz, J. A. Eudailey, A. M. Trama, C. LaBranche, G. G. Fouda, K. Wiehe, D. C. Montefiori, B. F. Haynes, H.-X. Liao, G. Ferrari, S. M. Alam, M. A. Moody, and S. R. Permar. The Function and Affinity Maturation of HIV-1 gp120-Specific Monoclonal Antibodies Derived from Colostral B Cells. Mucosal. Immunol., 9(2):414-427, Mar 2016. PubMed ID: 26242599.
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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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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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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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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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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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Klein2013
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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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Anil Korkut and Wayne A. Hendrickson. Structural Plasticity and Conformational Transitions of HIV Envelope Glycoprotein gp120. PLoS One, 7(12):e52170, 2012. PubMed ID: 23300605.
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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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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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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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Kulp2017
Daniel W. Kulp, Jon M. Steichen, Matthias Pauthner, Xiaozhen Hu, Torben Schiffner, Alessia Liguori, Christopher A. Cottrell, Colin Havenar-Daughton, Gabriel Ozorowski, Erik Georgeson, Oleksandr Kalyuzhniy, Jordan R. Willis, Michael Kubitz, Yumiko Adachi, Samantha M. Reiss, Mia Shin, Natalia de Val, Andrew B. Ward, Shane Crotty, Dennis R. Burton, and William R. Schief. Structure-Based Design of Native-Like HIV-1 Envelope Trimers to Silence Non-Neutralizing Epitopes and Eliminate CD4 Binding. Nat. Commun., 8(1):1655, 21 Nov 2017. PubMed ID: 29162799.
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Kwon2012
Young Do Kwon, Andrés Finzi, Xueling Wu, Cajetan Dogo-Isonagie, Lawrence K. Lee, Lucas R. Moore, Stephen D. Schmidt, Jonathan Stuckey, Yongping Yang, Tongqing Zhou, Jiang Zhu, David A. Vicic, Asim K. Debnath, Lawrence Shapiro, Carole A. Bewley, John R. Mascola, Joseph G. Sodroski, and Peter D. Kwong. Unliganded HIV-1 gp120 Core Structures Assume the CD4-Bound Conformation with Regulation by Quaternary Interactions and Variable Loops. Proc. Natl. Acad. Sci. U.S.A., 109(15):5663-5668, 10 Apr 2012. PubMed ID: 22451932.
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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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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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Laakso2007
Meg M. Laakso, Fang-Hua Lee, Beth Haggarty, Caroline Agrawal, Katrina M. Nolan, Mark Biscone, Josephine Romano, Andrea P. O. Jordan, George J. Leslie, Eric G. Meissner, Lishan Su, James A. Hoxie, and Robert W. Doms. V3 Loop Truncations in HIV-1 Envelope Impart Resistance to Coreceptor Inhibitors and Enhanced Sensitivity to Neutralizing Antibodies. PLoS Pathog., 3(8):e117, 24 Aug 2007. PubMed ID: 17722977.
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Labrijn2003
Aran F. Labrijn, Pascal Poignard, Aarti Raja, Michael B. Zwick, Karla Delgado, Michael Franti, James Binley, Veronique Vivona, Christoph Grundner, Chih-Chin Huang, Miro Venturi, Christos J. Petropoulos, Terri Wrin, Dimiter S. Dimitrov, James Robinson, Peter D. Kwong, Richard T. Wyatt, Joseph Sodroski, and Dennis R. Burton. Access of Antibody Molecules to the Conserved Coreceptor Binding Site on Glycoprotein gp120 Is Sterically Restricted on Primary Human Immunodeficiency Virus Type 1. J. Virol., 77(19):10557-10565, Oct 2003. PubMed ID: 12970440.
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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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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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Judith M. LaLonde, Young Do Kwon, David M. Jones, Alexander W. Sun, Joel R. Courter, Takahiro Soeta, Toyoharu Kobayashi, Amy M. Princiotto, Xueling Wu, Arne Schön, Ernesto Freire, Peter D. Kwong, John R. Mascola, Joseph Sodroski, Navid Madani, and Amos B. Smith, 3rd. Structure-Based Design, Synthesis, and Characterization of Dual Hotspot Small-Molecule HIV-1 Entry Inhibitors. J. Med. Chem., 55(9):4382-4396, 10 May 2012. PubMed ID: 22497421.
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Yee Lam, Nehal I. Abu-Lail, Munir S. Alam, and Stefan Zauscher. Using Microcantilever Deflection to Detect HIV-1 Envelope Glycoprotein gp120. Nanomedicine, 2(4):222-229, Dec 2006. PubMed ID: 17292147.
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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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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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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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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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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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Hongyan Liao, Jun-tao Guo, Miles D. Lange, Run Fan, Michael Zemlin, Kaihong Su, Yongjun Guan, and Zhixin Zhang. Contribution of V(H) Replacement Products to the Generation of Anti-HIV Antibodies. Clin. Immunol., 146(1):46-55, Jan 2013. PubMed ID: 23220404.
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Jun Liu, Alberto Bartesaghi, Mario J. Borgnia, Guillermo Sapiro, and Sriram Subramaniam. Molecular Architecture of Native HIV-1 gp120 Trimers. Nature, 455(7209):109-113, 4 Sep 2008. PubMed ID: 18668044.
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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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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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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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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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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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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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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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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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Matsumoto2023
Kaho Matsumoto, Takeo Kuwata, William D. Tolbert, Jonathan Richard, Shilei Ding, Jérémie Prévost, Shokichi Takahama, George P. Judicate, Takamasa Ueno, Hirotomo Nakata, Takuya Kobayakawa, Kohei Tsuji, Hirokazu Tamamura, Amos B. Smith, III, Marzena Pazgier, Andrés Finzi, and Shuzo Matsushita. Characterization of a Novel CD4 Mimetic Compound YIR-821 against HIV-1 Clinical Isolates. J. Virol., 97(1):e0163822, 31 Jan 2023. PubMed ID: 36511698.
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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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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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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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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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Meyerson2013
Joel R. Meyerson, Erin E. H. Tran, Oleg Kuybeda, Weizao Chen, Dimiter S. Dimitrov, Andrea Gorlani, Theo Verrips, Jeffrey D. Lifson, and Sriram Subramaniam. Molecular Structures of Trimeric HIV-1 Env in Complex with Small Antibody Derivatives. Proc. Natl. Acad. Sci. U.S.A., 110(2):513-518, 8 Jan 2013. PubMed ID: 23267106.
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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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Mishra2020a
Nitesh Mishra, Shaifali Sharma, Ayushman Dobhal, Sanjeev Kumar, Himanshi Chawla, Ravinder Singh, Muzamil Ashraf Makhdoomi, Bimal Kumar Das, Rakesh Lodha, Sushil Kumar Kabra, and Kalpana Luthra. Broadly Neutralizing Plasma Antibodies Effective against Autologous Circulating Viruses in Infants with Multivariant HIV-1 Infection. Nat. Commun., 11(1):4409, 2 Sep 2020. PubMed ID: 32879304.
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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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Moore1993d
J. P. Moore, H. Yoshiyama, D. D. Ho, J. E. Robinson, and J. Sodroski. Antigenic Variation in gp120s from Molecular Clones of HIV-1 LAI. AIDS Res. Hum. Retroviruses, 9:1185-1193, 1993. The binding of MAbs to four molecular clones of HIV-1 LAI: HxB2, HxB3, Hx10, and NL4-3, was measured. Despite the close relationship between these clones, there is considerable variation in their antigenic structure, judged by MAb reactivities to the V2, V3, and C4 domains and to discontinuous epitopes. Small variations in sequence can profoundly affect recognition of gp120 by all five groups of defined anti-gp120 neutralizing antibodies. PubMed ID: 7511394.
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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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Moore1998
J. P. Moore and J. Binley. HIV Envelope's Letters Boxed into Shape. Nature, 393:630-631, 1998. Comment on Nature 1998 Jun 18;393(6686):648-59 and Nature 1998 Jun 18;393(6686):705-11. PubMed ID: 9641673.
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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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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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Negi2009
Surendra S. Negi and Werner Braun. Automated Detection of Conformational Epitopes Using Phage Display Peptide Sequences. Bioinform. Biol. Insights, 3:71-81, 2009. PubMed ID: 20140073.
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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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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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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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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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ORourke2012
Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Kathryn A. Mesa, Aaron L. Vollrath, Gwen P. Tatsuno, Briana To, Faruk Sinangil, Kay Limoli, Terri Wrin, and Phillip W. Berman. Sequences in Glycoprotein gp41, the CD4 Binding Site, and the V2 Domain Regulate Sensitivity and Resistance of HIV-1 to Broadly Neutralizing Antibodies. J. Virol., 86(22):12105-12114, Nov 2012. PubMed ID: 22933284.
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Oscherwitz1999
J. Oscherwitz, F. M. Gotch, K. B. Cease, and J. A. Berzofsky. New Insights and Approaches Regarding B- and T-Cell Epitopes in HIV Vaccine Design. AIDS, 13(Suppl A):S163-174, 1999. PubMed ID: 10885773.
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Ozorowski2017
Gabriel Ozorowski, Jesper Pallesen, Natalia de Val, Dmitry Lyumkis, Christopher A. Cottrell, Jonathan L. Torres, Jeffrey Copps, Robyn L. Stanfield, Albert Cupo, Pavel Pugach, John P. Moore, Ian A. Wilson, and Andrew B. Ward. Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike. Nature, 547(7663):360-363, 20 Jul 2017. PubMed ID: 28700571.
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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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Pancera2005a
Marie Pancera, Jacob Lebowitz, Arne Schön, Ping Zhu, Ernesto Freire, Peter D. Kwong, Kenneth H. Roux, Joseph Sodroski, and Richard Wyatt. Soluble Mimetics of Human Immunodeficiency Virus Type 1 Viral Spikes Produced by Replacement of the Native Trimerization Domain with a Heterologous Trimerization Motif: Characterization and Ligand Binding Analysis. J. Virol., 79(15):9954-9969, Aug 2005. PubMed ID: 16014956.
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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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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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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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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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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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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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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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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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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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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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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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Rizzuto1998
C. D. Rizzuto, R. Wyatt, N. Hernandez-Ramos, Y. Sun, P. D. Kwong, W. A. Hendrickson, and J. Sodroski. A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding. Science, 280:1949-1953, 1998. This paper compares the epitope for CD4 inducible MAbs with the chemokine co-receptor binding site on the gp120 molecule. Site-directed mutagenesis of YU2 Env was guided by information obtained from the crystallized CD4-17b-gp120 core structure, Kwong et al, 1998. YU2 is a primary macrophage tropic R5 isolate with high affinity for both CD4 and CCR5. A protein with the V1-V2 loops deleted, called wt$\Delta$ was the basis for the assay which detected binding of virus to cells expressing CCR5 in the presence of sCD4. Preincubaton with MAb 17b blocks binding, as did the natural ligand for CCR5, MIP-1$\beta$ and anti-CCR5 MAb 2D7. Mutations 437 P/A and 442 Q/L increased CCR5 binding affinity. The region of gp120 CCR5 binding is shown to be the highly conserved $\beta$-sheet bridging structure, located proximal to the V3 loop. PubMed ID: 9632396.
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Rizzuto2000
Carlo Rizzuto and Joseph Sodroski. Fine Definition of a Conserved CCR5-Binding Region on the Human Immunodeficiency Virus Type 1 Glycoprotein 120. AIDS Res. Hum. Retroviruses, 16(8):741-749, 20 May 2000. PubMed ID: 10826481.
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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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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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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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Salzwedel2000
K. Salzwedel, E. D. Smith, B. Dey, and E. A. Berger. Sequential CD4-Coreceptor Interactions in Human Immunodeficiency Virus Type 1 Env Function: Soluble CD4 Activates Env for Coreceptor-Dependent Fusion and Reveals Blocking Activities of Antibodies against Cryptic Conserved Epitopes on gp120. J. Virol., 74:326-333, 2000. PubMed ID: 10590121.
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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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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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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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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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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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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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Sharma2006
Victoria A. Sharma, Elaine Kan, Yide Sun, Ying Lian, Jimna Cisto, Verna Frasca, Susan Hilt, Leonidas Stamatatos, John J. Donnelly, Jeffrey B. Ulmer, Susan W. Barnett, and Indresh K. Srivastava. Structural Characteristics Correlate with Immune Responses Induced by HIV Envelope Glycoprotein Vaccines. Virology, 10 Jun 2006. PubMed ID: 16769099.
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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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Shibata2007
Junji Shibata, Kazuhisa Yoshimura, Akiko Honda, Atsushi Koito, Toshio Murakami, and Shuzo Matsushita. Impact of V2 Mutations on Escape from a Potent Neutralizing Anti-V3 Monoclonal Antibody during In Vitro Selection of a Primary Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 81(8):3757-3768, Apr 2007. PubMed ID: 17251298.
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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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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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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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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.
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Stamatatos2000
L. Stamatatos, M. Lim, and C. Cheng-Mayer. Generation and structural analysis of soluble oligomeric gp140 envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV type 1 isolates. AIDS Res. Hum. Retroviruses, 16(10):981--94, 1 Jul 2000. PubMed ID: 10890360.
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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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Stricher2008
François Stricher, Chih-chin Huang, Anne Descours, Sophie Duquesnoy, Olivier Combes, Julie M. Decker, Young Do Kwon, Paolo Lusso, George M. Shaw, Claudio Vita, Peter D. Kwong, and Loïc Martin. Combinatorial Optimization of a CD4-Mimetic Miniprotein and Cocrystal Structures with HIV-1 gp120 Envelope Glycoprotein. J. Mol. Biol., 382(2):510-524, 3 Oct 2008. PubMed ID: 18619974.
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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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Tan2009
Hepan Tan and A. J. Rader. Identification of Putative, Stable Binding Regions through Flexibility Analysis of HIV-1 gp120. Proteins, 74(4):881-894, Mar 2009. PubMed ID: 18704932.
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Tanaka2017
Kazuki Tanaka, Takeo Kuwata, Muntasir Alam, Gilad Kaplan, Shokichi Takahama, Kristel Paola Ramirez Valdez, Anna Roitburd-Berman, Jonathan M. Gershoni, and Shuzo Matsushita. Unique Binding Modes for the Broad Neutralizing Activity of Single-Chain Variable Fragments (scFv) Targeting CD4-Induced Epitopes. Retrovirology, 14(1):44, 22 Sep 2017. PubMed ID: 28938888.
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Tang2011
Haili Tang, James E. Robinson, S. Gnanakaran, Ming Li, Eric S. Rosenberg, Lautaro G. Perez, Barton F. Haynes, Hua-Xin Liao, Celia C. Labranche, Bette T. Korber, and David C. Montefiori. Epitopes Immediately below the Base of the V3 Loop of gp120 as Targets for the Initial Autologous Neutralizing Antibody Response in Two HIV-1 Subtype B-Infected Individuals. J. Virol., 85(18):9286-9299, Sep 2011. PubMed ID: 21734041.
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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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Teeraputon2005
Sirilak Teeraputon, Suda Louisirirojchanakul, and Prasert Auewarakul. N-Linked Glycosylation in C2 Region of HIV-1 Envelope Reduces Sensitivity to Neutralizing Antibodies. Viral Immunol., 18(2):343-353, Summer 2005. PubMed ID: 16035946.
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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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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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Tran2012
Erin E. H. Tran, Mario J. Borgnia, Oleg Kuybeda, David M. Schauder, Alberto Bartesaghi, Gabriel A. Frank, Guillermo Sapiro, Jacqueline L. S. Milne, and Sriram Subramaniam. Structural Mechanism of Trimeric HIV-1 Envelope Glycoprotein Activation. PLoS Pathog., 8(7):e1002797, 2012. PubMed ID: 22807678.
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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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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.
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Vaine2010
Michael Vaine, Shixia Wang, Qin Liu, James Arthos, David Montefiori, Paul Goepfert, M. Juliana McElrath, and Shan Lu. Profiles of Human Serum Antibody Responses Elicited by Three Leading HIV Vaccines Focusing on the Induction of Env-Specific Antibodies. PLoS One, 5(11):e13916, 2010. PubMed ID: 21085486.
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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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Varadarajan2005
Raghavan Varadarajan, Deepak Sharma, Kausik Chakraborty, Mayuri Patel, Michael Citron, Prem Sinha, Ramkishor Yadav, Umar Rashid, Sarah Kennedy, Debra Eckert, Romas Geleziunas, David Bramhill, William Schleif, Xiaoping Liang, and John Shiver. Characterization of gp120 and Its Single-Chain Derivatives, gp120-CD4D12 and gp120-M9: Implications for Targeting the CD4i Epitope in Human Immunodeficiency Virus Vaccine Design. J. Virol., 79(3):1713-1723, Feb 2005. PubMed ID: 15650196.
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Veillette2014
Maxime Veillette, Anik Désormeaux, Halima Medjahed, Nour-Elhouda Gharsallah, Mathieu Coutu, Joshua Baalwa, Yongjun Guan, George Lewis, Guido Ferrari, Beatrice H. Hahn, Barton F. Haynes, James E. Robinson, Daniel E. Kaufmann, Mattia Bonsignori, Joseph Sodroski, and Andres Finzi. Interaction with Cellular CD4 Exposes HIV-1 Envelope Epitopes Targeted by Antibody-Dependent Cell-Mediated Cytotoxicity. J. Virol., 88(5):2633-2644, Mar 2014. PubMed ID: 24352444.
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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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Wang2007a
Bao-Zhong Wang, Weimin Liu, Sang-Moo Kang, Munir Alam, Chunzi Huang, Ling Ye, Yuliang Sun, Yingying Li, Denise L. Kothe, Peter Pushko, Terje Dokland, Barton F. Haynes, Gale Smith, Beatrice H. Hahn, and Richard W. Compans. Incorporation of High Levels of Chimeric Human Immunodeficiency Virus Envelope Glycoproteins into Virus-Like Particles. J. Virol., 81(20):10869-10878, Oct 2007. PubMed ID: 17670815.
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J. Weinberg, H. X. Liao, J. V. Torres, T. J. Matthews, J. Robinson, and B. F. Haynes. Identification of a synthetic peptide that mimics an HIV glycoprotein 120 envelope conformational determinant exposed following ligation of glycoprotein 120 by CD4. AIDS Res. Hum. Retroviruses, 13:657-64, 1997. PubMed ID: 9168234.
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Wen2018
Yingxia Wen, Hung V. Trinh, Christine E Linton, Chiara Tani, Nathalie Norais, DeeAnn Martinez-Guzman, Priyanka Ramesh, Yide Sun, Frank Situ, Selen Karaca-Griffin, Christopher Hamlin, Sayali Onkar, Sai Tian, Susan Hilt, Padma Malyala, Rushit Lodaya, Ning Li, Gillis Otten, Giuseppe Palladino, Kristian Friedrich, Yukti Aggarwal, Celia LaBranche, Ryan Duffy, Xiaoying Shen, Georgia D. Tomaras, David C. Montefiori, William Fulp, Raphael Gottardo, Brian Burke, Jeffrey B. Ulmer, Susan Zolla-Pazner, Hua-Xin Liao, Barton F. Haynes, Nelson L. Michael, Jerome H. Kim, Mangala Rao, Robert J. O'Connell, Andrea Carfi, and Susan W. Barnett. Generation and Characterization of a Bivalent Protein Boost for Future Clinical Trials: HIV-1 Subtypes CR01\_AE and B gp120 Antigens with a Potent Adjuvant. PLoS One, 13(4):e0194266, 2018. PubMed ID: 29698406.
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West2010
Anthony P. West, Jr., Rachel P. Galimidi, Christopher P. Foglesong, Priyanthi N. P. Gnanapragasam, Joshua S. Klein, and Pamela J. Bjorkman. Evaluation of CD4-CD4i Antibody Architectures Yields Potent, Broadly Cross-Reactive Anti-Human Immunodeficiency Virus Reagents. J. Virol., 84(1):261-269, Jan 2010. PubMed ID: 19864392.
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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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White2010
Tommi A. White, Alberto Bartesaghi, Mario J. Borgnia, Joel R. Meyerson, M. Jason V. de la Cruz, Julian W. Bess, Rachna Nandwani, James A. Hoxie, Jeffrey D. Lifson, Jacqueline L. S. Milne, and Sriram Subramaniam. Molecular Architectures of Trimeric SIV and HIV-1 Envelope Glycoproteins on Intact Viruses: Strain-Dependent Variation in Quaternary Structure. PLoS Pathog, 6(12):e1001249, 2010. PubMed ID: 21203482.
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White2011
Tommi A. White, Alberto Bartesaghi, Mario J. Borgnia, M. Jason V. de la Cruz, Rachna Nandwani, James A. Hoxie, Julian W. Bess, Jeffrey D. Lifson, Jacqueline L. S. Milne, and Sriram Subramaniam. Three-Dimensional Structures of Soluble CD4-Bound States of Trimeric Simian Immunodeficiency Virus Envelope Glycoproteins Determined by Using Cryo-Electron Tomography. J. Virol., 85(23):12114-12123, Dec 2011. PubMed ID: 21937655.
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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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Witt2017
Kristen C. Witt, Luis Castillo-Menendez, Haitao Ding, Nicole Espy, Shijian Zhang, John C. Kappes, and Joseph Sodroski. Antigenic Characterization of the Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Precursor Incorporated into Nanodiscs. PLoS One, 12(2):e0170672, 2017. PubMed ID: 28151945.
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Wright2012
Elizabeth R. Wright and Paul W. Spearman. Unraveling the Structural Basis of HIV-1 Neutralization. Future Microbiol., 7(11):1251-1254, Nov 2012. PubMed ID: 23075444.
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L. Wu, N. P. Gerard, R. Wyatt, H. Choe, C. Parolin, N. Ruffing, A. Borsetti, A. A. Cardoso, E. Desjardin, W. Newman, C. Gerard, and J. Sodroski. CD4-Induced Interaction of Primary HIV-1 gp120 Glycoproteins with the Chemokine Receptor CCR-5. Nature, 384:179-183, 1996. Results suggest that HIV-1 attachment to CD4 creates a high-affinity binding site for CCR-5, leading to membrane fusion and virus entry. CD4-induced or V3 neutralizing MAbs block the interaction of gp120-CD4 complexes with CCR-5. PubMed ID: 8906795.
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Wu2008
Xueling Wu, Anna Sambor, Martha C. Nason, Zhi-Yong Yang, Lan Wu, Susan Zolla-Pazner, Gary J. Nabel, and John R. Mascola. Soluble CD4 Broadens Neutralization of V3-Directed Monoclonal Antibodies and Guinea Pig Vaccine Sera against HIV-1 Subtype B and C Reference Viruses. Virology, 380(2):285-295, 25 Oct 2008. PubMed ID: 18804254.
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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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Wu2011
Xueling Wu, Tongqing Zhou, Jiang Zhu, Baoshan Zhang, Ivelin Georgiev, Charlene Wang, Xuejun Chen, Nancy S. Longo, Mark Louder, Krisha McKee, Sijy O'Dell, Stephen Perfetto, Stephen D. Schmidt, Wei Shi, Lan Wu, Yongping Yang, Zhi-Yong Yang, Zhongjia Yang, Zhenhai Zhang, Mattia Bonsignori, John A. Crump, Saidi H. Kapiga, Noel E. Sam, Barton F. Haynes, Melissa Simek, Dennis R. Burton, Wayne C. Koff, Nicole A. Doria-Rose, Mark Connors, NISC Comparative Sequencing Program, James C. Mullikin, Gary J. Nabel, Mario Roederer, Lawrence Shapiro, Peter D. Kwong, and John R. Mascola. Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing. Science, 333(6049):1593-1602, 16 Sep 2011. PubMed ID: 21835983.
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R. Wyatt, J. Moore, M. Accola, E. Desjardin, J. Robinson, and J. Sodroski. Involvement of the V1/V2 Variable Loop Structure in the Exposure of Human Immunodeficiency Virus Type 1 gp120 Epitopes Induced by Receptor Binding. J. Virol., 69:5723-5733, 1995. Deletions in the V1/V2 loops of gp120 resulted in the loss of the ability of sCD4 to induce binding of the MAbs 17b, 48d, and A32. A32 can induce binding of 17b and 48d; this induction does not appear to involve the V1/V2 regions. PubMed ID: 7543586.
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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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Xiang2002b
Shi-Hua Xiang, Najah Doka, Rabeéea K. Choudhary, Joseph Sodroski, and James E. Robinson. Characterization of CD4-Induced Epitopes on the HIV Type 1 gp120 Envelope Glycoprotein Recognized by Neutralizing Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 18(16):1207-1217, 1 Nov 2002. PubMed ID: 12487827.
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Xiang2003
Shi-Hua Xiang, Liping Wang, Mariam Abreu, Chih-Chin Huang, Peter D. Kwong, Eric Rosenberg, James E. Robinson, and Joseph Sodroski. Epitope Mapping and Characterization of a Novel CD4-Induced Human Monoclonal Antibody Capable of Neutralizing Primary HIV-1 Strains. Virology, 315(1):124-134, 10 Oct 2003. PubMed ID: 14592765.
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Xu2013
Xiao-Hong Nancy Xu, Zhaoyang Wen, and William J. Brownlow. Ultrasensitive Analysis of Binding Affinity of HIV Receptor and Neutralizing Antibody Using Solution-Phase Electrochemiluminescence Assay. J. Electroanal. Chem. (Lausanne), 688:53-60, 1 Jan 2013. PubMed ID: 23565071.
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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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Yang2002
Xinzhen Yang, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt, and Joseph Sodroski. Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin. J. Virol., 76(9):4634-4642, 1 May 2002. PubMed ID: 11932429.
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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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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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Yoshimura2006
Kazuhisa Yoshimura, Junji Shibata, Tetsuya Kimura, Akiko Honda, Yosuke Maeda, Atsushi Koito, Toshio Murakami, Hiroaki Mitsuya, and Shuzo Matsushita. Resistance Profile of a Neutralizing Anti-HIV Monoclonal Antibody, KD-247, that Shows Favourable Synergism with Anti-CCR5 Inhibitors. AIDS, 20(16):2065-2073, 24 Oct 2006. PubMed ID: 17053352.
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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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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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Zhang2001a
W. Zhang, A. P. Godillot, R. Wyatt, J. Sodroski, and I. Chaiken. Antibody 17b Binding at the Coreceptor Site Weakens the Kinetics of the Interaction of Envelope Glycoprotein gp120 with CD4. Biochemistry, 40(6):1662-1670, 13 Feb 2001. PubMed ID: 11327825.
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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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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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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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Zhou2010
Tongqing Zhou, Ivelin Georgiev, Xueling Wu, Zhi-Yong Yang, Kaifan Dai, Andrés Finzi, Young Do Kwon, Johannes F. Scheid, Wei Shi, Ling Xu, Yongping Yang, Jiang Zhu, Michel C. Nussenzweig, Joseph Sodroski, Lawrence Shapiro, Gary J. Nabel, John R. Mascola, and Peter D. Kwong. Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01. Science, 329(5993):811-817, 13 Aug 2010. PubMed ID: 20616231.
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Zhu2003
Chongbin Zhu, Thomas J. Matthews, and Chin Ho Chen. Neutralization Epitopes of the HIV-1 Primary Isolate DH012. Vaccine, 21(23):3301-3306, 4 Jul 2003. PubMed ID: 12804861.
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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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Wang2019
Qian Wang, Lihong Liu, Wuze Ren, Agegnehu Gettie, Hua Wang, Qingtai Liang, Xuanling Shi, David C. Montefiori, Tongqing Zhou, and Linqi Zhang. A Single Substitution in gp41 Modulates the Neutralization Profile of SHIV during In Vivo Adaptation. Cell Rep., 27(9):2593-2607.e5, 28 May 2019. PubMed ID: 31141685.
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Displaying record number 707
Download this epitope
record as JSON.
MAb ID |
C11 (c11) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
James Robinson, Tulane University, LA |
Epitope |
(Discontinuous epitope)
|
Ab Type |
gp120 C1-C5, gp120 CD4i cluster A |
Neutralizing |
no |
Species
(Isotype)
|
human(IgG) |
Patient |
|
Immunogen |
HIV-1 infection |
Keywords |
antibody binding site, antibody generation, antibody interactions, assay or method development, binding affinity, brain/CSF, co-receptor, effector function, HAART, ART, neutralization, polyclonal antibodies, review, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity |
Notes
Showing 47 of
47 notes.
-
C11: 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. Non-CD4bs-binding, non-nAb C11 did not recognize negatively-selected JRFL or 16055 SOSIP trimers.
Guenaga2015
(vaccine antigen design, subtype comparisons, structure)
-
C11: 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 C11 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)
-
C11: LANL database note: This monoclonal antibody is a CHAVI reagent (http://chavi.org/); Species: human; Category: C1-C5 MAbs; Contact person: James Robinson
-
C11: 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)
-
C11: This study used the crystal structure of C11 in complex with gp120 to define the putative contact region between C11 and gp120, mapping to the 7-stranded beta-sandwich in the gp41-interactive region. Specific residues of the putative epitope were W45, N68, I491, P493, and G495.
Gohain2015
(antibody binding site, structure)
-
C11: 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. Binding of CD4i-epitope-recognizing non-NAb, C11, to trimers was almost completely eliminated by trimer cross-linking.
Schiffner2016
(assay or method development, binding affinity, structure)
-
C11: 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. C11 was used in co-expression assay to understand the conformational changes in Env upon CD4 binding. The interaction of A32, C11 and RV144 MAbs with Env was greatly increased upon coexpression of CD4 in a dose dependent manner.
Veillette2014
(effector function)
-
C11: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. C11 is discussed as the CD4i Cluster A region-targeting, non-neutralizing anti-gp120 mAb with a discontinuous epitope, exhibiting broad and prototypic ADCC activity similar to A32 (Table-1). It is reported that C11- and A32-blockable mAbs most likely recognize conformational epitopes within the inner domain of gp120 involving the C1 region.
Pollara2013
(effector function, review)
-
C11: ADCC mediated by CD4i mAbs (or anti-CD4i-epitope mAbs) was studied using a panel of 41 novel mAbs. Three epitope clusters were classified, depending on cross-blocking in ELISA by different mAbs: Cluster A - in the gp120 face, cross-blocking by mAbs A32 and/or C11; Cluster B - in the region proximal to CoRBS (co-receptor binding site) involving V1V2 domain, cross-blocking by E51-M9; Cluster C - CoRBS, cross-blocking by 17b and/or 19e. The ADCC half-maximal effective concentrations of the Cluster A and B mAbs were generally 0.5-1 log lower than those of the Cluster C mAbs, and none of the Cluster A or B mAbs could neutralize HIV-1. Cluster A's A32- and C11-blockable mAbs were suggested to recognize conformational epitopes within the inner domain of gp120 that involve the C1 region. Neutralization potency and breadth were also assessed for these mAbs. No correlation was found between ADCC and neutralization Abs' action or functional responses. C11 was used as the positive control in different assays, especially competition ELISA assays to determine epitope specificity.
Guan2013
(antibody interactions, effector function)
-
C11: Crystal structures of unliganded core gp120 from HIV-1 clade B, C, and E were determined to understand the mechanism of CD4 binding capacity of unliganded HIV-1. The results suggest that the CD4 bound conformation represents "a ground state" for the gp120 core with variable loop. C11 was used as a control to prove whether the purified and crystallized gp120 is in the CD4 bound conformational state or not.
Kwon2012
(structure)
-
C11: 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). The nonneutralizing MAbs A32, C11, 19e had a range of PIs (7.4 to 8.8).
Sajadi2012
(polyclonal antibodies)
-
C11: 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. C11 binds effectively to KE in the context of intact virions.
Steckbeck2010
(binding affinity)
-
C11: 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)
-
C11: 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. All of the 14 mutants were shown to be able to bind to C11, indicating correct folding. Binding of C11 to gp120 was also uninhibited by the presence of B40t77.
Joubert2010
(binding affinity, structure)
-
C11: Expression of gp120 was shown to lead to the accumulation of both monomeric gp120 and aberrant dimeric gp120 forms. Dimeric forms of gp120 were not recognized by MAbs against the gp120 inner domain, such as C11, nor by CD4i MAbs, but were recognized by CD4BS MAbs. It is suggested that gp120 dimerization occludes or disrupts the inner domain and/or the co-receptor binding site. Formation of gp120 dimers was reduced by removal of the V1/V2 loops or the N and C termini.
Finzi2010
(antibody binding site)
-
C11: Broadly neutralizing sera from elite neutralizers exhibited significant sensitivities to mutations I165A, N332A, and N160K. C11 binding was tested for pseudoviruses with the mutations relative to the WT. C11 binding was not significantly affected by the three mutations.
Walker2010
(binding affinity)
-
C11: C11 did not compete with the broadly neutralizing Ab PG9 for binding to gp120.
Walker2009a
-
C11: 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. None of the adaptation-associated changes in the HIV-1 env glycoproteins affected isolate recognition by the C11 Ab.
Pacheco2008
(antibody binding site)
-
C11: 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 all the immunized animals were able to block gp120-CD4 complex interactions with C11 equally.
DeVico2007
(neutralization)
-
C11: Interactions of this Ab with gp120 monomer and two cleavage-defective gp140 trimers were studied. It was shown that C11 recognized the soluble monomer more efficiently than the soluble trimers and that treatment of the proteins with GA (cross-linking) further decreased the interactions of this Ab with the trimers to undetectable levels, indicating that the access of the C11 epitope was affected by cross-linking of the trimers but not the monomer.
Yuan2006
(antibody binding site, antibody interactions, binding affinity)
-
C11: 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)
-
C11: A trimeric recombinant gp140 construct was developed for immunization studies. Its structural integrity was assessed by a panel of MAbs. The trimeric gp140 was poorly recognized by C11 compared to monomeric gp120, suggesting poor accessibility of the C11 epitope on the construct.
Kim2005
(antibody binding site)
-
C11: A stable trimerization motif, GCN4, was appended to the C terminus of YU2gp120 to obtain stable gp120 trimers (gp120-GCN4). Each trimer subunit was capable of binding IgG1b12, indicating that they were at least 85% active. D457V mutation in the CD4 binding site resulted in a decreased affinity of the gp120-GCN4 for CD4 and for C11.
Pancera2005a
(binding affinity)
-
C11: R-FL and YU2 HIV-1 strains were not neutralized by C11.C11 and other non-neutralizing Abs only recognized JR-FL cleavage-defective glycoproteins, while the neutralizing Abs (2G12 and IgG1b12) recognized both cleavage competent and 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. Abs able to neutralize lab-adapted isolates displayed enhanced viral entry at higher Ab concentrations, whereas Abs that cannot neutralize any virus, such as C11, did not display such enhancement.
Pancera2005
(antibody binding site, neutralization, binding affinity)
-
C11: A substantial fraction of soluble envelope glycoprotein trimers contained inter-subunit disulfide bonds. Reduction of these disulfide bonds decreased binding of C11 to the glycoprotein, indicating that the inter-S-S bonds contribute to the exposure of the C11 epitope.
Yuan2005
(antibody binding site)
-
C11: 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 were able to block binding of biotin-labeled C11, indicating presence of C11-like Abs.
Robinson2005
(antibody generation, assay or method development, HAART, ART)
-
c11: 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. c11 recognizes monomeric gp120. c11 was unable to neutralize or capture the VLPs studied, indicating that no forms of Env exist on the particles that resemble monomeric gp120 dissociated from gp41.
Moore2006
(antibody binding site, neutralization)
-
C11: 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)
-
C11: 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. V1/V2/V3 MAb 4KG2, C1-C4 MAb A32, C1-C5 MAb C11, and HIVIG all either did not bind or had significantly diminished binding to both antigen constructs.
Selvarajah2005
(vaccine antigen design, vaccine-induced immune responses)
-
C11: 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. C11 has no indication of polyspecific autoreactivity.
Haynes2005
(antibody binding site)
-
C11: 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 C11.
Pantophlet2004
(vaccine antigen design)
-
C11: 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)
-
C11: 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. C11 recognized most variants, some from each of the four individuals, by gp120 immunoprecipitation.
Ohagen2003
(brain/CSF, variant cross-reactivity)
-
C11: 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, and 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 had large entropy contributions to free energy (mean: 26.1 kcal/mol) of binding to the gp120 monomer, except the potent CD4BS neutralizing MAb b6 had a much smaller value of 5.7 kcal/mol. High values suggest surface burial or protein folding and ordering of amino acids. Variable loop MAbs (L17, L78, 19b, 39F, Ag1211, D0142, and G3-299) MAbs that bind to the N and C termini (211/c, A32, L100, P35, and C11) do not have dramatic entropy changes. 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. Authors describe the epitope as N-term and C-term binding.
Kwong2002
(antibody binding site)
-
C11: 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. C11 was used as a negative control, as C11 binding did not alter binding of CD4-independent gp120 to CCR5, nor binding to CCR5-expressing Cf2Th cells.
Raja2003
(co-receptor)
-
C11: gp120 mutants were used to define the CXCR4 binding site using CXCR4 displayed on paramagnetic proteoliposomes (PMPLs) to reduce non-specific gp120 binding -- basic residues in the V3 loop and the beta19 strand (RIKQ, positions 419-422) were involved, and deletion of the V1-V2 loops allowed CD4-independent CXCR4 binding -- MAbs 17b (CD4i) and F105 (CD4BS) were used to study conformational changes in the mutants -- C11 was used to detect gp120 binding to CXCR4 or CCR5 on PMPLs.
Basmaciogullar2002
(antibody binding site)
-
C11: 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 -- 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 -- non-neutralizing MAbs C11 and A32 bound with lower affinity than NAb IgG1b12 -- the MAb 17b was sCD4 inducible on gp160deltaCT PL.
Grundner2002
(antibody binding site, vaccine antigen design)
-
C11: 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 C11, A32, and 30D which did not bind the stabilized oligomer.
Yang2002
(antibody binding site)
-
C11: 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
(vaccine antigen design)
-
C11: Does not compete with binding of MAb generated in response to gp120-CD4 complex, CG10.
Sullivan1998
(antibody interactions)
-
C11: Does not neutralize TCLA strains or primary isolates.
Parren1997
(variant cross-reactivity)
-
C11: Binds efficiently to sgp120 but not soluble gp120+gp41, suggesting its gp120 epitope is blocked by gp41 binding -- partial re-exposure if sCD4 was bound -- does not bind to HXBc2 gp120 if the 19 C-term amino acids are deleted.
Wyatt1997
(antibody binding site)
-
C11: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- C11 bound monomer, did not bind oligomer or neutralize JRFL.
Fouts1997
(antibody binding site)
-
C11: Does not neutralize JR-FL nor block gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study.
Trkola1996b
(antibody binding site)
-
C11: Did not block ability of gp120-sCD4 complexes to inhibit MIP-1alpha binding -- binds to gp41-binding domain.
Wu1996
(antibody binding site)
-
C11: Binding enhanced by anti-V3 MAb 5G11 -- reciprocal inhibition with anti-C1 MAbs.
Moore1996
(antibody interactions)
-
C11: Mutations that inhibit binding: C1 (45 W/S, 88 N/P) -- V5 (463 N/D) -- and C5 (491 I/F, 493 P/K and 495 G/K) and enhance binding: C1 (36 V/L) -- V1-V2 (152/153 GE/SM) -- and DeltaV1/V2/V3.
Moore1994c
(antibody binding site)
References
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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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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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Yongjun Guan, Marzena Pazgier, Mohammad M. Sajadi, Roberta Kamin-Lewis, Salma Al-Darmarki, Robin Flinko, Elena Lovo, Xueji Wu, James E. Robinson, Michael S. Seaman, Timothy R. Fouts, Robert C. Gallo, Anthony L. DeVico, and George K. Lewis. Diverse Specificity and Effector Function Among Human Antibodies to HIV-1 Envelope Glycoprotein Epitopes Exposed by CD4 Binding. Proc. Natl. Acad. Sci. U.S.A., 110(1):E69-E78, 2 Jan 2013. PubMed ID: 23237851.
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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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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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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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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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Kwon2012
Young Do Kwon, Andrés Finzi, Xueling Wu, Cajetan Dogo-Isonagie, Lawrence K. Lee, Lucas R. Moore, Stephen D. Schmidt, Jonathan Stuckey, Yongping Yang, Tongqing Zhou, Jiang Zhu, David A. Vicic, Asim K. Debnath, Lawrence Shapiro, Carole A. Bewley, John R. Mascola, Joseph G. Sodroski, and Peter D. Kwong. Unliganded HIV-1 gp120 Core Structures Assume the CD4-Bound Conformation with Regulation by Quaternary Interactions and Variable Loops. Proc. Natl. Acad. Sci. U.S.A., 109(15):5663-5668, 10 Apr 2012. PubMed ID: 22451932.
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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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J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065.
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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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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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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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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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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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Marie Pancera, Jacob Lebowitz, Arne Schön, Ping Zhu, Ernesto Freire, Peter D. Kwong, Kenneth H. Roux, Joseph Sodroski, and Richard Wyatt. Soluble Mimetics of Human Immunodeficiency Virus Type 1 Viral Spikes Produced by Replacement of the Native Trimerization Domain with a Heterologous Trimerization Motif: Characterization and Ligand Binding Analysis. J. Virol., 79(15):9954-9969, Aug 2005. PubMed ID: 16014956.
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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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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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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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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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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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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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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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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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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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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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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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Veillette2014
Maxime Veillette, Anik Désormeaux, Halima Medjahed, Nour-Elhouda Gharsallah, Mathieu Coutu, Joshua Baalwa, Yongjun Guan, George Lewis, Guido Ferrari, Beatrice H. Hahn, Barton F. Haynes, James E. Robinson, Daniel E. Kaufmann, Mattia Bonsignori, Joseph Sodroski, and Andres Finzi. Interaction with Cellular CD4 Exposes HIV-1 Envelope Epitopes Targeted by Antibody-Dependent Cell-Mediated Cytotoxicity. J. Virol., 88(5):2633-2644, Mar 2014. PubMed ID: 24352444.
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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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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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Wu1996
L. Wu, N. P. Gerard, R. Wyatt, H. Choe, C. Parolin, N. Ruffing, A. Borsetti, A. A. Cardoso, E. Desjardin, W. Newman, C. Gerard, and J. Sodroski. CD4-Induced Interaction of Primary HIV-1 gp120 Glycoproteins with the Chemokine Receptor CCR-5. Nature, 384:179-183, 1996. Results suggest that HIV-1 attachment to CD4 creates a high-affinity binding site for CCR-5, leading to membrane fusion and virus entry. CD4-induced or V3 neutralizing MAbs block the interaction of gp120-CD4 complexes with CCR-5. PubMed ID: 8906795.
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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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Yang2002
Xinzhen Yang, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt, and Joseph Sodroski. Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin. J. Virol., 76(9):4634-4642, 1 May 2002. PubMed ID: 11932429.
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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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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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