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Science 3 June 1988:
Vol. 240. no. 4857, pp. 1335 - 1339
DOI: 10.1126/science.2453925
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Articles

Science, Vol 240, Issue 4857, 1335-1339
Copyright © 1988 by American Association for the Advancement of Science

articles

Location and chemical synthesis of a binding site for HIV-1 on the CD4 protein

BA Jameson, PE Rao, LI Kong, BH Hahn, GM Shaw, LE Hood, and SB Kent

Division of Biology, California Institute of Technology, Pasadena 91125.

The human immunodeficiency virus type 1 (HIV-1) uses the CD4 protein as a receptor for infection of susceptible cells. A candidate structure for the HIV-1 binding site on the CD4 protein was identified by epitope mapping with a family of eight functionally distinct CD4-specific monoclonal antibodies in conjunction with a panel of large CD4-derived synthetic peptides. All of the seven epitopes that were located reside within two immunoglobulin-like disulfide loops situated between residues 1 and 168 of the CD4 protein. The CD4-specific monoclonal antibody OKT4A, a potent inhibitor of HIV-1 binding, recognized a site between residues 32 and 47 on the CD4 protein. By analogy to other members of the immunoglobulin superfamily of proteins, this particular region has been predicted to exist as a protruding loop. A synthetic analog of this loop (residues 25 to 58) showed a concentration-dependent inhibition of HIV-1-induced cell fusion. It is proposed that a loop extending from residues 37 to 53 of the CD4 protein is a binding site for the AIDS virus.


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