Journal of Experimental Medicine, Vol 175, 301-304, Copyright © 1992 by Rockefeller University Press

ARTICLES

Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4

GA Schockmel, C Somoza, SJ Davis, AF Williams and D Healey
Medical Research Council Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, United Kingdom.

The human immunodeficiency virus (HIV-1) infects T lymphocytes via an interaction between the virus envelope glycoprotein gp120 and the CD4 antigen of T helper cells. Previous studies demonstrated that mutations in various regions of CD4 domain 1 lead to the loss of gp120 binding. In the present study the gp120 binding site was constructed in rat CD4 by replacing rat with human CD4 sequence. A series of mutants was constructed the best of which bound gp120 with an affinity only twofold less than that of human CD4. The data indicate that the gp120 binding site of human CD4 is constituted by residues 33-58 of domain 1.
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