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• W2114328298 abstract "ABSTRACT APOBEC3G, a potent HIV-1 host restriction factor, is overcome by HIV-1 viral infectivity factor (Vif), which induces its polyubiquitination and proteasomal degradation. Here we show that lysine-deficient APOBEC3G with an N-terminal hemagglutinin (HA) tag fusion (HA-A3G20K/R) was resistant to HIV-1 Vif-induced proteasomal degradation. HA-A3G20K/R molecules were packaged into wild-type HIV-1 particles, and HA-A3G20K/R drastically decreased wild-type HIV-1 reverse transcription products and infectivity. We also showed that the N terminus of A3G was a target of polyubiquitination induced by HIV-1 Vif. Thus, fusion of the HA tag to the N terminus of A3G20K/R reduced its polyubiquitination, the likely mechanism for the resistance of this protein to HIV-1 Vif-induced proteasomal degradation. Finding such ways to induce resistance of A3G to Vif may provide new approaches to anti-HIV/AIDS therapy." @default.
• W2114328298 created "2016-06-24" @default.
• W2114328298 creator A5017973379 @default.
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• W2114328298 creator A5062862053 @default.
• W2114328298 creator A5085796521 @default.
• W2114328298 date "2011-05-01" @default.
• W2114328298 modified "2023-10-17" @default.
• W2114328298 title "N-Terminal Hemagglutinin Tag Renders Lysine-Deficient APOBEC3G Resistant to HIV-1 Vif-Induced Degradation by Reduced Polyubiquitination" @default.
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• W2114328298 doi "https://doi.org/10.1128/jvi.01925-10" @default.
• W2114328298 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3126286" @default.
• W2114328298 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21345952" @default.
• W2114328298 hasPublicationYear "2011" @default.
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