1991
DOI: 10.1128/jvi.65.1.489-493.1991
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Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody

Abstract: A human monoclonal antibody designated 15e is reactive with the envelope glycoprotein (gpl20) of multiple isolates of human immunodeficiency virus type 1 (HIV-1). Antibody 15e also neutralizes HIV-1 with broad specificity and blocks gpl20 binding to CD4. Characterization of the 15e epitope shows that it is conformation dependent and is distinct from previously recognized functional domains of gpl20, suggesting that this epitope represents a novel site important for HIV-1 neutralization and CD4 binding. These f… Show more

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Cited by 256 publications
(112 citation statements)
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“…During the course of HIV infection the exterior envelope glycoprotein, gp120, elicits NAb against virus. The most abundant NAb are CD4BS antibodies such as monoclonal antibodies F105, 15e, 21h, 1125h, and IgG1b12, which block gp120-CD4 interaction (17). Less common are CD4i antibodies such as monoclonal antibodies 48d and 17b, which disrupt the binding of gp120-CD4 complexes to chemokine receptors (18).…”
Section: Discussionmentioning
confidence: 99%
“…During the course of HIV infection the exterior envelope glycoprotein, gp120, elicits NAb against virus. The most abundant NAb are CD4BS antibodies such as monoclonal antibodies F105, 15e, 21h, 1125h, and IgG1b12, which block gp120-CD4 interaction (17). Less common are CD4i antibodies such as monoclonal antibodies 48d and 17b, which disrupt the binding of gp120-CD4 complexes to chemokine receptors (18).…”
Section: Discussionmentioning
confidence: 99%
“…27). The receptivity/permissiveness of HTLV-I or HTLV-II transformed (transactivated) lymphoid cells to HIV infection followed by rapid viral replication and release, combined with the formation of MNGCs as the culture time progresses (often together with a population of mitotic single uninfected and infected cells) has yielded valuable information on the nature of viral glycoprotein Gpl20, the cellular CD4 antigen and CD4~GpI20 interaction (Clapham et al, 1987;Harada et al, 1985;Hussey et al, 1988;Ho et al, 1991;Lifson et al, 1986aLifson et al, , 1986bMontefiori and Mitchell, 1987;Nara et al, 1987;Sodroski et al, 1986;Yoffe et al, 1987). There is here a clear parallel between the C-type retrovirally-transformed cultured lymphoid cells and the large transformed single lymphocytes seen in lymph node biopsy samples from AIDS patients (Byrnes et al, 1983), which often lie alongside MNGCs.…”
Section: A Multinucleate Giant Cells In Vivo and In Vitromentioning
confidence: 99%
“…The variable domains V1, V2 and V3 of gp120 have been suggested to be involved in HIV-1 fusion and infectivity at a stage subsequent to CD4 binding. Amino acid substitutions in and binding of mAbs directed against these domains affect syncytium formation and infectivity without affecting CD4 binding [65][66][67][68][69][70][71]. Gp120-CD4 interaction induces conformational changes in both CD4 and gp120 [72][73][74][75][76] but the significance of these conformational alterations for the subsequent fusion event remains undefined.…”
Section: Hiv-1 Envelope Proteins and Phenotype Variabilitymentioning
confidence: 99%