HIV molecular immunology database
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|gp160 Epitope Map|
|Author Location||gp120(81-100 LAI)|
|Ab Type||gp120 C1|
|Vaccine strain||B clade IIIB|
Showing 4 of 4 notes.
Showing 5 of 5 references.
Dowbenko1988 D. Dowbenko, G. Nakamura, C. Fennie, C. Shimasaki, L. Riddle, R. Harris, T. Gregory, and L. Lasky. Epitope mapping of the immunodeficiency virus type 1 gp120 with monoclonal antibodies. J. Virol., 62:4703-4711, 1988. PubMed ID: 2460639. Show all entries for this paper.
Berman1991 P. W. Berman, K. Rosenthal, G. Nakamura, L. Riddle, J. P. Porter, D. Dowbenko, M. Hobbes, R. Byrn, J. Groopman, T. Gregory, and B. Fendly. Monoclonal Antibodies to gp160 of HIV-1 That Neutralize HIV-1 Infectivity, Block the Binding of gp120 to CD4, and React with Diverse Isolates. J. Acquir. Immune Defic. Syndr., 4:306, 1991. Show all entries for this paper.
Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.
Nakamura1992 G. R. Nakamura, R. Byrn, K. Rosenthal, J. P. Porter, M. R. Hobbs, L. Riddle, D. J. Eastman, D. Dowbenko, T. Gregory, B. M. Fendly, and P. W. Berman. Monoclonal Antibodies to the Extracellular Domain of HIV-1 IIIB gp160 That Neutralize Infectivity, Block Binding to CD4 React with Diverse Isolates. AIDS Res. Hum. Retroviruses, 8:1875-1885, 1992. PubMed ID: 1283308. 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.