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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
immunology and microbiology
Contribution of Hypervariable Domains to the Conformation of a Broadly Neutralizing Glycoprotein 120 Epitope
AIDS Research and Human Retroviruses, Volume 11, No. 7, Year 1995
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Description
Three of the five hypervariable domains (V1-V3) of human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 have previously been shown to be dispensable for antigenic epitopes recognized by broadly neutralizing monoclonal antibodies. In this study, the influence of the V4 and V5 domains on an epitope recognized by a broadly neutralizing human monoclonal antibody, 1.5e, was investigated. In contrast with the V1, V2, and V3 domains of gp120, the V4 and V5 domains were found to be critical for binding to both CD4 and 1.5e. Our results suggest that V4 and V5 are in structurally less flexible regions of gp120 than V1, V2, and V3 and raises the question of whether variable domains V4 and V5 are also indispensable for other broadly neutralizing antibodies in the same class as 1.5e. © 1995, Mary Ann Liebert, Inc. All rights reserved.
Authors & Co-Authors
Robinson, James E.
United States, Farmington
Uconn Health
Mazzara, Gail P.
United States, Cambridge
Therion Biologics Corporation
Essex, Max E.
United States, Boston
Harvard T.h. Chan School of Public Health
Lee, Tunhou
United States, Boston
Harvard T.h. Chan School of Public Health
Statistics
Citations: 8
Authors: 4
Affiliations: 4
Identifiers
Doi:
10.1089/aid.1995.11.777
ISSN:
08892229
Research Areas
Infectious Diseases