Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody.
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.
Aaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016.
D D
DD
Ho
J A
JA
McKeating
X L
XL
Li
T
T
Moudgil
E S
ES
Daar
N C
NC
Sun
J E
JE
Robinson
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000936:Antigen-Antibody Complex; D015704:CD4 Antigens / Q000276:immunology*; D004229:Dithiothreitol / Q000494:pharmacology; D000939:Epitopes / Q000032:analysis / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology* / Q000648:ultrastructure; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D009500:Neutralization Tests; D011487:Protein Conformation; D013045:Species Specificity; D014415:Tunicamycin / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D015704:CD4 Antigens; D000939:Epitopes; D015699:HIV Envelope Protein gp120; D014415:Tunicamycin; D004229:Dithiothreitol