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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.

Original publication

DOI

10.1128/jvi.65.1.489-493.1991

Type

Journal article

Journal

Journal of virology

Publication Date

01/1991

Volume

65

Pages

489 - 493

Addresses

Aaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016.

Keywords

Humans, HIV-1, Dithiothreitol, HIV Envelope Protein gp120, Tunicamycin, Antibodies, Monoclonal, Antigen-Antibody Complex, Epitopes, Neutralization Tests, Species Specificity, Protein Conformation, CD4 Antigens