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• W1552228345 endingPage "3345" @default.
• W1552228345 startingPage "3341" @default.
• W1552228345 abstract "Human immunodeficiency virus type 1 (HIV-1) can readily accept envelope (Env) glycoproteins from distantly related retroviruses. However, we previously showed that the HIV-1 Env glycoprotein complex is excluded even from particles formed by the Gag proteins of another lentivirus, visna virus, unless the matrix domain of the visna virus Gag polyprotein is replaced by that of HIV-1. We also showed that the integrity of the HIV-1 matrix domain is critical for the incorporation of wild-type HIV-1 Env protein but not for the incorporation of a truncated form which lacks the 144 C-terminal amino acids of the cytoplasmic domain of the transmembrane glycoprotein. We report here that the C-terminal truncation of the transmembrane glycoprotein also allows the efficient incorporation of HIV-1 Env proteins into viral particles formed by the Gag proteins of the widely divergent Moloney murine leukemia virus (Mo-MLV). Additionally, pseudotyping of a Mo-MLV-based vector with the truncated rather than the full-length HIV-1 Env allowed efficient transduction of human CD4+ cells. These results establish that Mo-MLV-based vectors can be used to target cells susceptible to infection by HIV-1." @default.
• W1552228345 created "2016-06-24" @default.
• W1552228345 creator A5005401811 @default.
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• W1552228345 date "1997-04-01" @default.
• W1552228345 modified "2023-10-14" @default.
• W1552228345 title "Truncation of the human immunodeficiency virus type 1 envelope glycoprotein allows efficient pseudotyping of Moloney murine leukemia virus particles and gene transfer into CD4+ cells" @default.
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• W1552228345 doi "https://doi.org/10.1128/jvi.71.4.3341-3345.1997" @default.
• W1552228345 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/191476" @default.
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