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PMID: 1702163 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody.

Journal of virology ·Vol. 65 ·No. 1 ·1991-01-00 ·Pages 489-93

Ho DD, McKeating JA, Li XL, Moudgil T, Daar ES, Sun NC, Robinson JE

Abstract

A human monoclonal antibody designated 15e is reactive with the envelope glycoprotein (gp120) of multiple isolates of human immunodeficiency virus type 1 (HIV-1). Antibody 15e also neutralizes HIV-1 with broad specificity and blocks gp120 binding to CD4. Characterization of the 15e epitope shows that it is conformation dependent and is distinct from previously recognized functional domains of gp120, suggesting that this epitope represents a novel site important for HIV-1 neutralization and CD4 binding. These findings have implications for the development of a vaccine for AIDS.

MeSH Terms
Antibodies, Monoclonal/immunology Antigen-Antibody Complex CD4 Antigens/immunology Dithiothreitol/pharmacology Epitopes/analysis,immunology HIV Envelope Protein gp120/immunology,ultrastructure HIV-1/immunology Humans Neutralization Tests Protein Conformation Species Specificity Tunicamycin/pharmacology
Chemicals
Antibodies, Monoclonal Antigen-Antibody Complex CD4 Antigens Epitopes HIV Envelope Protein gp120 Tunicamycin Dithiothreitol
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ho D D
Aaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016.
McKeating J A
Li X L
Moudgil T
Daar E S
Sun N C
Robinson J E
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.65.1.489-493.1991
Published
1991-01-00
Pages
489-93
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC240544
Subset
IM
Grants
NIAID NIH HHS · AI25541 · United States
NIAID NIH HHS · AI27742 · United States
NIAID NIH HHS · AI28747 · United States
External Links
PubMed source DOI: 10.1128/JVI.65.1.489-493.1991 PMC Full Text View journal details
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