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• W2121248674 abstract "ABSTRACT 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." @default.
• W2121248674 created "2016-06-24" @default.
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• W2121248674 date "2006-05-01" @default.
• W2121248674 modified "2023-09-26" @default.
• W2121248674 title "Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells" @default.
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• W2121248674 doi "https://doi.org/10.1128/jvi.80.9.4388-4395.2006" @default.
• W2121248674 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1472027" @default.
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