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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.
- Source :
-
Journal of virology [J Virol] 1991 Jan; Vol. 65 (1), pp. 489-93. - Publication Year :
- 1991
-
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.
- Subjects :
- Antigen-Antibody Complex
Dithiothreitol pharmacology
Epitopes analysis
HIV Envelope Protein gp120 ultrastructure
Humans
Neutralization Tests
Protein Conformation
Species Specificity
Tunicamycin pharmacology
Antibodies, Monoclonal immunology
CD4 Antigens immunology
Epitopes immunology
HIV Envelope Protein gp120 immunology
HIV-1 immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0022-538X
- Volume :
- 65
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 1702163
- Full Text :
- https://doi.org/10.1128/JVI.65.1.489-493.1991