| Literature DB >> 2441877 |
L A Lasky, G Nakamura, D H Smith, C Fennie, C Shimasaki, E Patzer, P Berman, T Gregory, D J Capon.
Abstract
The primary event in the infection of cells by HIV is the interaction between the viral envelope glycoprotein, gp120, and its cellular receptor, CD4. A recombinant form of gp120 was found to bind to a recombinant CD4 antigen with high affinity. Two gp120-specific murine monoclonal antibodies were able to block the interaction between gp120 and CD4. The gp120 epitope of one of these antibodies was isolated by immunoaffinity chromatography of acid-cleaved gp120 and shown to be contained within amino acids 397-439. Using in vitro mutagenesis, we have found that deletion of 12 amino acids from this region of gp120 leads to a complete loss of binding. In addition, a single amino acid substitution in this region results in significantly decreased binding, suggesting that sequences within this region are directly involved in the binding of gp120 to the CD4 receptor.Entities:
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Year: 1987 PMID： 2441877 DOI： 10.1016/0092-8674(87)90524-1
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582