HIV molecular immunology database
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MAb ID | G45-60 | |
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HXB2 Location | gp160(431-440) DNA(7515..7544) |
gp160 Epitope Map |
Author Location | gp120(429-438 BRU) | |
Epitope |
GKAMYAPPIS
|
Epitope Alignment
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Ab Type | gp120 C4 | |
Neutralizing | L | |
Species (Isotype) | mouse(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | virus derived protein |
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Vaccine strain | B clade IIIB |
Vaccine component | gp120 |
Showing 4 of 4 notes.
Showing 5 of 5 references.
Sun1989 N. C. Sun, D. D. Ho, C. R. Y. Sun, R.-S. Liou, W. Gordon, M. S. C. Fung, X. L. Li, R. C. Ting, T.-H. Lee, N. T. Chang, and T. W. Chang. Generation and Characterization of Monoclonal Antibodies to the Putative CD4-Binding Domain of Human Immunodeficiency Virus Type 1 gp120. J. Virol., 63:3579-3585, 1989. PubMed ID: 2474670. 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.
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.
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.
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. Show all entries for this paper.