期刊
JOURNAL OF VIROLOGY
卷 80, 期 9, 页码 4388-4395出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.80.9.4388-4395.2006
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资金
- NIAID NIH HHS [AI24755, R37 AI024755, AI31782, AI46725, U01 AI046725] Funding Source: Medline
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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