Binding site for human immunodeficiency virus coat protein gp120 is located in the NH2-terminal region of T4 (CD4) and requires the intact variable-region-like domain.

Journal Article (Journal Article)

The external segment of the T4 (CD4) glycoprotein functions as the T-cell surface receptor for human immunodeficiency virus by binding the major viral coat protein (gp120) with relatively high affinity. To more precisely define the region of T4 involved in gp120 interaction, we used purified, soluble forms of T4 anchor-minus polypeptides (produced in a baculovirus system) in conjunction with proteolytic fragmentation, microsequencing, and a specific T4-gp120 binding assay. The results indicate that the NH2-terminal region of T4 including the immunoglobulin variable-region-like domain is required for gp120 interaction. In contrast, the COOH-terminal half of the molecule, containing the two potential N-linked glycosylation sites, is not necessary. Furthermore, reduction of intrachain disulfide bonds in the T4 molecular abrogates gp120 binding, thereby strongly implying that the binding site for gp120 is dependent on the stabilized domain structure of the active binding region.

Full Text

Duke Authors

Cited Authors

  • Richardson, NE; Brown, NR; Hussey, RE; Vaid, A; Matthews, TJ; Bolognesi, DP; Reinherz, EL

Published Date

  • August 1988

Published In

Volume / Issue

  • 85 / 16

Start / End Page

  • 6102 - 6106

PubMed ID

  • 3261864

Pubmed Central ID

  • PMC281913

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.85.16.6102


  • eng

Conference Location

  • United States