Found 7 matching records:
Download this epitope record as JSON.
MAb ID | G3-136 (G3.136) | |
---|---|---|
HXB2 Location | Env(170-180) DNA(6732..6764) |
Env Epitope Map |
Author Location | gp120(170-180 IIIB) | |
Research Contact | Tanox Biosystems Inc and David Ho, ADARC, NY | |
Epitope |
QKEYAFFYKLD
|
Epitope Alignment
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG) | |
Patient | ||
Immunogen | vaccine | |
Keywords | antibody interactions, vaccine antigen design |
Vaccine type | protein |
---|---|
Vaccine strain | B clade IIIB |
Vaccine component | gp120 |
Showing 16 of 16 notes.
Showing 20 of 20 references.
Isolation Paper
Fung1992
M. S. C. Fung, C. R. Y. Sun, W. L. Gordon, R.-S. Liou, T. W. Chang, W. N. C. Sun, E. S. Daar, and D. D. Ho. Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120. J. Virol., 66:848-856, 1992. Two anti-envelope V2 antibodies were raised that neutralize virus in either a conformation dependent (G3-136) or conformation independent (BAT085) manner. G3-136 has diminished reactivity with deglycosylation or DTT reduced gp120, and sCD4 inhibits binding in a competition assay; BAT085 is not sensitive to these alterations in gp120. PubMed ID: 1370558.
Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
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. Show all entries for this paper.
Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.
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. Show all entries for this paper.
Yoshiyama1994 H. Yoshiyama, H.-M. Mo, J. P. Moore, and D. D. Ho. Characterization of Mutants of Human Immunodeficiency Virus Type 1 That Have Escaped Neutralization by Monoclonal Antibody G3-4 to the gp120 V2 Loop. J. Virol., 68:974-978, 1994. MAb G3-4 binds a conformationally sensitive epitope in the V2 loop of HIV-1 RF. RF was cultured in the presence of G3-4 to select for neutralization resistance. Three independent experiments yielded escape mutants, and sequencing revealed two V2 mutations to be responsible for the neutralization escape phenotype, 177 Y/H and 179 L/P. Experimental introduction of the 179 P substitution resulted in non-viable virus, and 177 H confirmed the resistance phenotype. PubMed ID: 7507188. Show all entries for this paper.
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. Show all entries for this paper.
Stamatatos1995 L. Stamatatos and C. Cheng-Mayer. Structural Modulations of the Envelope gp120 Glycoprotein of Human Immunodeficiency Virus Type 1 upon Oligomerization and the Differential V3 Loop Epitope Exposure of Isolates Displaying Distinct Tropism upon Viral-Soluble Receptor Binding. J. Virol., 69:6191-6198, 1995. PubMed ID: 7545244. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.
Stamatatos1997 L. Stamatatos, S. Zolla-Pazner, M. K. Gorny, and C. Cheng-Mayer. Binding of Antibodies to Virion-Associated gp120 Molecules of Primary-Like Human Immunodeficiency Virus Type 1 (HIV-1) Isolates: Effect on HIV-1 Infection of Macrophages and Peripheral Blood Mononuclear Cells. Virology, 229:360-369, 1997. PubMed ID: 9126249. Show all entries for this paper.
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.
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. Show all entries for this paper.
Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.
Stamatatos1998 L. Stamatatos and C. Cheng-Mayer. An Envelope Modification That Renders a Primary, Neutralization-Resistant Clade B Human Immunodeficiency Virus Type 1 Isolate Highly Susceptible to Neutralization by Sera from Other Clades. J. Virol., 72:7840-7845, 1998. PubMed ID: 9733820. Show all entries for this paper.
Ly2000 A. Ly and L. Stamatatos. V2 Loop Glycosylation of the Human Immunodeficiency Virus Type 1 SF162 Envelope Facilitates Interaction of this Protein with CD4 and CCR5 Receptors and Protects the Virus from Neutralization by Anti-V3 Loop and Anti-CD4 Binding Site Antibodies. J. Virol., 74:6769-6776, 2000. PubMed ID: 10888615. Show all entries for this paper.
Zwick2003a Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | BAT085 (BAT-085) | |
---|---|---|
HXB2 Location | Env(171-180) DNA(6735..6764) |
Env Epitope Map |
Author Location | gp120(170-180 IIIB) | |
Research Contact | Tanox Biosystems Inc and David Ho, ADARC, NY | |
Epitope |
KEYAFFYKLD
|
Epitope Alignment
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | inactivated HIV |
---|---|
Vaccine strain | B clade IIIB |
Vaccine component | HIV-1 |
Showing 13 of 13 notes.
Showing 18 of 18 references.
Isolation Paper
Fung1992
M. S. C. Fung, C. R. Y. Sun, W. L. Gordon, R.-S. Liou, T. W. Chang, W. N. C. Sun, E. S. Daar, and D. D. Ho. Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120. J. Virol., 66:848-856, 1992. Two anti-envelope V2 antibodies were raised that neutralize virus in either a conformation dependent (G3-136) or conformation independent (BAT085) manner. G3-136 has diminished reactivity with deglycosylation or DTT reduced gp120, and sCD4 inhibits binding in a competition assay; BAT085 is not sensitive to these alterations in gp120. PubMed ID: 1370558.
Show all entries for this paper.
Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.
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.
DSouza1994 M. P. D'Souza, S. J. Geyer, C. V. Hanson, R. M. Hendry, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 Envelope by Neutralization and Binding Assays: An International Collaboration. AIDS, 8:169-181, 1994. PubMed ID: 7519019. Show all entries for this paper.
Fung1987 M. S. C. Fung, C. R. Y. Sun, N.-C. Sun, N. T. Chang, and T.-W. Chang. Monoclonal Antibodies That Neutralize HIV-1 Virions and Inhibit Syncytium Formation by Infected Cells. Biotechnology, 5:940-947, 1987. Show all entries for this paper.
Gorny1994 M. K. Gorny, J. P. Moore, A. J. Conley, S. Karwowska, J. Sodroski, C. Williams, S. Burda, L. J. Boots, and S. Zolla-Pazner. Human Anti-V2 Monoclonal Antibody That Neutralizes Primary but Not Laboratory Isolates of Human Immunodeficiency Virus Type 1. J. Virol., 68:8312-8320, 1994. Detailed characterization of the MAb 697-D. PubMed ID: 7525987. Show all entries for this paper.
Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.
Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.
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. Show all entries for this paper.
Moore1994c 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. Show all entries for this paper.
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. Show all entries for this paper.
Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Wu1995 Z. Wu, S. C. Kayman, W. Honnen, K. Revesz, H. Chen, S. V. Warrier, S. A. Tilley, J. McKeating, C. Shotton, and A. Pinter. Characterization of Neutralization Epitopes in the V2 Region of Human Immunodeficiency Virus Type 1 gp120: Role of Glycosylation in the Correct Folding of the V1/V2 Domain. J. Virol., 69:2271-2278, 1995. Most epitopes based only on numbering. PubMed ID: 7533854. Show all entries for this paper.
Yoshiyama1994 H. Yoshiyama, H.-M. Mo, J. P. Moore, and D. D. Ho. Characterization of Mutants of Human Immunodeficiency Virus Type 1 That Have Escaped Neutralization by Monoclonal Antibody G3-4 to the gp120 V2 Loop. J. Virol., 68:974-978, 1994. MAb G3-4 binds a conformationally sensitive epitope in the V2 loop of HIV-1 RF. RF was cultured in the presence of G3-4 to select for neutralization resistance. Three independent experiments yielded escape mutants, and sequencing revealed two V2 mutations to be responsible for the neutralization escape phenotype, 177 Y/H and 179 L/P. Experimental introduction of the 179 P substitution resulted in non-viable virus, and 177 H confirmed the resistance phenotype. PubMed ID: 7507188. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | BAT123 (BAT-123, CGP 47 439) | |
---|---|---|
HXB2 Location | Env(306-322) DNA(7140..7190) |
Env Epitope Map |
Author Location | gp120(308-322 HXB2) | |
Research Contact | Tanox Biosystems Inc and David Ho, ADARC, NY | |
Epitope |
RIRIQRGPGRAFVTIGK
|
Epitope Alignment
|
Subtype | B | |
Ab Type | gp120 V3 // V3 glycan (V3g) | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1κ) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | inactivated HIV |
---|---|
Vaccine strain | B clade IIIB |
Vaccine component | HIV-1 |
Showing 11 of 11 notes.
Showing 13 of 13 references.
Fung1987 M. S. C. Fung, C. R. Y. Sun, N.-C. Sun, N. T. Chang, and T.-W. Chang. Monoclonal Antibodies That Neutralize HIV-1 Virions and Inhibit Syncytium Formation by Infected Cells. Biotechnology, 5:940-947, 1987. Show all entries for this paper.
Liou1989 R. S. Liou, E. M. Rosen, M. S. C. Fung, W. N. C. Sun, C. Sun, W. Gordon, N. T. Chang, and T. W. Chang. A Chimeric Mouse-Human Antibody That Retains Specificity for HIV-1 gp120 and Mediates the Lysis of the HIV-1-Infected Cells. J. Immunol., 143:3967-3975, 1989. PubMed ID: 2480382. Show all entries for this paper.
Fung1990 M. S. C. Fung, C. R. Y. Sun, R. S. Liou, W. Gordon, N. T. Chang, T.-W. Chang, and N.-C. Sun. Monoclonal Anti-Idiotypic Antibody Mimicking the Principal Neutralization Site in HIV-1 gp120 Induces HIV-1 Neutralizing Antibodies in Rabbits. J. Immunol., 145:2199-2206, 1990. PubMed ID: 2398276. Show all entries for this paper.
Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.
Safrit1993 J. T. Safrit, M. S. C. Fung, C. A. Andrews, D. G. Braun, W. N. C. Sun, T. W. Chang, and R. A. Koup. hu-PBL-SCID Mice Can Be Protected from HIV-1 Infection by Passive Transfer of Monoclonal Antibody to the Principal Neutralizing Determinant of Envelope gp120. AIDS, 7:15-21, 1993. PubMed ID: 7680205. Show all entries for this paper.
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. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
Gauduin1995 M. C. Gauduin, J. T. Safrit, R. Weir, M. S. Fung, and R. A. Koup. Pre- and post-exposure protection against human immunodeficiency virus type 1 infection mediated by a monoclonal antibody. J. Infect. Dis., 171:1203-1209, 1995. Passive protection against HIV-1 LAI with MAb BAT123 was achieved in SCID mice reconstituted with human peripheral blood lymphocytes (hu-PBL-SCID) BAT123 is specific for the V3 loop gp120 of HIV-1 LAI. Animals were protected against subsequent infection with LAI strain, but not other virus strains, when BAT123 was given 1 hour before virus inoculation, or up to 4 hours post-exposure. No therapeutic effect was observed when BAT123 was administered after infection had been established. PubMed ID: 7751695. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Andrus1998 L. Andrus, A. M. Prince, I. Bernal, P. McCormack, D. H. Lee, M. K. Gorny, and S. Zolla-Pazner. Passive immunization with a human immunodeficiency virus type 1- neutralizing monoclonal antibody in Hu-PBL-SCID mice: isolation of a neutralization escape variant. J. Infect. Dis., 177:889-97, 1998. PubMed ID: 9534960. Show all entries for this paper.
Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.
Gauduin1998 M. C. Gauduin, R. Weir, M. S. Fung, and R. A. Koup. Involvement of the complement system in antibody-mediated post-exposure protection against human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 14:205-11, 1998. Post-exposure passive transfer of murine BAT123 can confer protection to hu-PBL-SCID mice challenged with HIV-1 LAI, and the mechanism is by complement-mediated cytolysis or virolysis. This protection was not conferred by CGP 47 439, a BAT123 chimera that has a human IgG$_1$ Fc domain, substituted in place of a murine IgG$_1$ Fc domain, suggesting that the protection is mediated by complement. Further evidence was that the protective ability of BAT123 is lost when mice were treated with cobra venom factor, which inactivates serum complement. IgG$_1$ does not fix complement efficiently, so an IgG$_2$ MAb might perform better. Therefore, in spite of the potential for enhancement in some circumstances, in this circumstance complement activation provided a protective advantage. PubMed ID: 9491910. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 110.4 | |
---|---|---|
HXB2 Location | Env(310-317) DNA(7152..7175) |
Env Epitope Map |
Author Location | gp120(308-328 BRU) | |
Research Contact | Genetic Systems Corp, Seattle WA, E. Kinney-Thomas | |
Epitope |
QRGPGRAF
|
Epitope Alignment
|
Ab Type | gp120 V3 // V3 glycan (V3g) | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1κ) | |
Patient | ||
Immunogen | vaccine | |
Keywords | anti-idiotype, antibody binding site, antibody interactions, antibody sequence, contact residues, escape |
Vaccine type | HIV infected-cell lysate |
---|---|
Vaccine strain | B clade BRU |
Vaccine component | HIV-1 |
Showing 11 of 11 notes.
Showing 15 of 15 references.
Arendrup1993 M. Arendrup, A. Sonnerborg, B. Svennerholm, L. Akerblom, C. Nielsen, H. Clausen, S. Olofsson, J. O. Nielsen, and J. E. S. Hensen. Neutralizing antibody response during human immunodeficiency virus type 1 infection: type and group specificity and viral escape. J. Gen. Virol., 74:855-863, 1993. PubMed ID: 7684062. Show all entries for this paper.
Boudet1994 F. Boudet, J. Theze, and M. Zouali. Anti-Idiotypic Antibodies to the Third Variable Domain of gp120 Induce an Anti-HIV-1 Antibody Response in Mice. Virology, 200:176-188, 1994. PubMed ID: 7510435. Show all entries for this paper.
Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.
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. Show all entries for this paper.
Connelly1994 R. J. Connelly, M. Kahn, J. Blake, O. K. Haffar, and E. K. Thomas. Dual Specificity of a Monoclonal Anti-Idiotypic Antibody for HIV-1 Neutralizing Monoclonals 110.3 and 110.4 as Well as the V3 Loop of gp120. Virology, 205:554-557, 1994. PubMed ID: 7526543. Show all entries for this paper.
Guillerm1998 C. Guillerm, V. Robert-Hebmann, U. Hibner, M. Hirn, and C. Devaux. An Anti-CD4 (CDR3-Loop) Monoclonal Antibody Inhibits Human Immunodeficiency Virus Type 1 Envelope Glycoprotein-Induced Apoptosis. Virology, 248:254-263, 1998. PubMed ID: 9721234. Show all entries for this paper.
Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.
McDougal1996 J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
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. Show all entries for this paper.
Thali1992b M. Thali, C. Furman, B. Wahren, M. Posner, D. Ho, J. Robinson, and J. Sodroski. Cooperativity of Neutralizing Antibodies Directed against the V3 and CD4 Binding Regions of the HIV-1 gp120 Envelope Glycoprotein. J. Acquir. Immune Defic. Syndr., 5:591-599, 1992. PubMed ID: 1588493. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.
Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 110.3 | |
---|---|---|
HXB2 Location | Env(310-317) DNA(7152..7175) |
Env Epitope Map |
Author Location | gp120(308-328 BRU) | |
Epitope |
QRGPGRAF
|
Epitope Alignment
|
Ab Type | gp120 V3 // V3 glycan (V3g) | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1κ) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | HIV infected-cell lysate |
---|---|
Vaccine strain | B clade BRU |
Vaccine component | HIV-1 |
Showing 4 of 4 notes.
Showing 5 of 5 references.
Connelly1994 R. J. Connelly, M. Kahn, J. Blake, O. K. Haffar, and E. K. Thomas. Dual Specificity of a Monoclonal Anti-Idiotypic Antibody for HIV-1 Neutralizing Monoclonals 110.3 and 110.4 as Well as the V3 Loop of gp120. Virology, 205:554-557, 1994. PubMed ID: 7526543. Show all entries for this paper.
Evans1989 D. J. Evans, J. McKeating, J. M. Meredith, K. L. Burke, K. Katrak, A. John, M. Ferguson, P. D. Minor, R. A. Weiss, and J. W. Almond. An Engineered Poliovirus Chimera Elicits Broadly Reactive HIV-1 Neutralizing Antibodies. Nature, 339:385-388, 1989. PubMed ID: 2542797. Show all entries for this paper.
Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 110.5 | |
---|---|---|
HXB2 Location | Env(310-317) DNA(7152..7175) |
Env Epitope Map |
Author Location | gp120(308-328 BRU) | |
Research Contact | E. Kinney-Thomas or Genetic Systems, Seattle WA | |
Epitope |
QRGPGRAF
|
Epitope Alignment
|
Ab Type | gp120 V3 // V3 glycan (V3g) | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1κ) | |
Patient | ||
Immunogen | vaccine | |
Keywords | antibody binding site, antibody interactions, binding affinity |
Vaccine type | HIV infected-cell lysate |
---|---|
Vaccine strain | B clade BRU |
Vaccine component | HIV-1 |
Showing 15 of 15 notes.
Showing 20 of 20 references.
Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.
Cordell1991 J. Cordell, J. P. Moore, C. J. Dean, P. J. Klasse, R. A. Weiss, and J. A. McKeating. Rat Monoclonal Antibodies to Nonoverlapping Epitopes of Human Immunodeficiency Virus Type I gp120 Block CD4 Binding In Vitro. Virology, 185:72-79, 1991. PubMed ID: 1718090. Show all entries for this paper.
Jeffs1996 S. A. Jeffs, J. McKeating, S. Lewis, H. Craft, D. Biram, P. E. Stephens, and R. L. Brady. Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein. J. Gen. Virol., 77:1403-1410, 1996. PubMed ID: 8757980. Show all entries for this paper.
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. Show all entries for this paper.
Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.
McDougal1996 J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033. Show all entries for this paper.
McKeating1992a J. A. McKeating, J. Cordell, C. J. Dean, and P. Balfe. Synergistic Interaction between Ligands Binding to the CD4 Binding Site and V3 Domain of Human Immunodeficiency Virus Type I gp120. Virology, 191:732-742, 1992. PubMed ID: 1280382. Show all entries for this paper.
Moore1990 J. P. Moore, J. A. McKeating, R. A. Weiss, and Q. J. Sattentau. Dissociation of gp120 from HIV-1 Virions Induced by Soluble CD4. Science, 250:1139-1142, 1990. PubMed ID: 2251501. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
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. Show all entries for this paper.
Reitz1988 M. S. Reitz, Jr., C. Wilson, C. Naugle, and M. Robert-Guroff. Generation of a Neutralization-Resistant Variant of HIV-1 Is Due to Selection for a Point Mutation in the Envelope Gene. Cell, 54:57-63, 1988. Growth of HXB2 in the constant presence of a neutralizing antiserum yielded a viral population resistant to the same serum. gp41 mutation 582 (Ala to Thr) conferred the resistant phenotype. PubMed ID: 2838179. Show all entries for this paper.
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. Show all entries for this paper.
Sattentau1995 Q. J. Sattentau, S. Zolla-Pazner, and P. Poignard. Epitope Exposure on Functional, Oligomeric HIV-1 gp41 Molecules. Virology, 206:713-717, 1995. Most gp41 epitopes are masked when associated with gp120 on the cell surface. Weak binding of anti-gp41 MAbs can be enhanced by treatment with sCD4. MAb 2F5 binds to a membrane proximal epitope which binds in the presence of gp120 without sCD4. PubMed ID: 7530400. Show all entries for this paper.
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. Show all entries for this paper.
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. Show all entries for this paper.
Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.
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. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 110.6 | |
---|---|---|
HXB2 Location | Env(311-318) DNA(7155..7178) |
Env Epitope Map |
Author Location | gp120( BRU) | |
Epitope |
RGPGRAFV
|
Epitope Alignment
|
Ab Type | gp120 V3 // V3 glycan (V3g) | |
Neutralizing | L (weak) | |
Species (Isotype) | mouse(IgG1λ) | |
Patient | ||
Immunogen | vaccine | |
Keywords | antibody binding site, antibody interactions, binding affinity, optimal epitope |
Vaccine type | HIV infected-cell lysate |
---|---|
Vaccine strain | B clade BRU |
Vaccine component | HIV-1 |
Showing 2 of 2 notes.
Showing 3 of 3 references.
Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.
Pirofski1993 L.-A. Pirofski, E. K. Thomas, and M. D. Scharff. Variable region gene utilization and mutation in a group of neutralizing murine anti-human immunodeficiency virus type 1 principal neutralizing determinant antibodies. AIDS Res. Hum. Retroviruses, 9:41-49, 1993. Observed restricted subset of murine V heavy and light chain gene elements in a set of 5 antibodies that bind to the tip of the V3 loop. PubMed ID: 7678971. Show all entries for this paper.
Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.
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