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Published June 3, 1988 | public
Journal Article

Location and Chemical Synthesis of a Binding Site for HIV-1 on the CD4 Protein


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.

Additional Information

© 1988 American Association for the Advancement of Science. 18 February 1988; accepted 18 April 1988. Principal support for this work was provided by a Marshall Field's Award from the American Foundation for AIDS Research, grant No. 00465R (S.B.H.K.). The cell fusion assays were supported by AI25784 (G.S. and B.H.). We thank P. Rieber for MT151, D. Wernicke-Jameson for discussions, P. Dervan for the use of computer facilities, S. Perry, S. E. McAnaney, and L. Martin Selk for tec assistance, C. Elkins for manuscript typing, and D. Noskowitz for figure preparation.

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