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Journal of Virology, May 2006, p. 4388-4395, Vol. 80, No. 9
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.9.4388-4395.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Cancer Immunology and AIDS,1 Department of Biostatistical Science, Dana-Farber Cancer Institute,3 Department of Pathology, Division of AIDS, Harvard Medical School, Boston, Massachusetts 02115,2 Department of Biostatistics,4 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 021155
Received 3 November 2005/ Accepted 15 February 2006
The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a homotrimer of gp120/gp41 heterodimers to support virus entry. During the process of virus entry, an individual HIV-1 envelope glycoprotein trimer binds the cellular receptors CD4 and CCR5/CXCR4 and mediates the fusion of the viral and the target cellular membranes. By studying the function of heterotrimers between wild-type and nonfunctional mutant envelope glycoproteins, we found that two wild-type subunits within an envelope glycoprotein trimer are required to support virus entry. Complementation between HIV-1 envelope glycoprotein mutants defective in different functions to allow virus entry was not evident. These results assist our understanding of the mechanisms whereby the HIV-1 envelope glycoproteins mediate virus entry and membrane fusion and guide attempts to inhibit these processes.
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