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MAb ID BAT123 (BAT-123, CGP 47 439)
HXB2 Location gp160(306-322)
DNA(7140..7190)
gp160 Epitope Map
Author Location gp120(308-322 HXB2)
Research Contact Tanox Biosystems Inc and David Ho, ADARC, NY
Epitope RIRIQRGPGRAFVTIGK Epitope Alignment
RIRIQRGPGRAFVTIGK epitope logo
Subtype B
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type inactivated HIV
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

Showing 11 of 11 notes.

References

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.


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