Multimeric CD4 binding exhibited by human and simian immunodeficiency virus envelope protein dimers.

Journal of virology ·Vol. 66 ·No. 9 ·1992-09-00 ·Pages 5610-4

Earl PL, Doms RW, Moss B

Abstract

The envelope (Env) glycoproteins of human and simian immunodeficiency viruses (HIV and SIV) form noncovalently associated oligomers which mediate virus binding to the cell surface and fusion between the viral envelope and plasma membrane. A high-affinity interaction with CD4 is a critical step in this process. In this report, we show that Env protein dimers, but not monomers, can bind two CD4 molecules simultaneously. Multimeric CD4 binding may have important implications for Env protein-CD4 avidity, CD4-induced release of gp120, and subunit-subunit cooperativity during virus membrane fusion as well as for therapeutic strategies.

MeSH Terms

CD4 Antigens/chemistry,metabolism Gene Products, env/metabolism HIV-1/metabolism Simian Immunodeficiency Virus/metabolism

Chemicals

CD4 Antigens Gene Products, env

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Earl P L

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.

Doms R W

Moss B

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37 references, click to expand

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Article Info

Journal

Journal of virology

Abbr.

J Virol

ISSN

0022-538X

DOI

10.1128/JVI.66.9.5610-5614.1992

Published

1992-09-00

Pages

5610-4

Language

English

Region

United States

NLM ID

0113724

PMCID

PMC289124

Subset

External Links

PubMed source DOI: 10.1128/JVI.66.9.5610-5614.1992 PMC Full Text View journal details

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Multimeric CD4 binding exhibited by human and simian immunodeficiency virus envelope protein dimers.

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