N-terminal hemagglutinin tag renders lysine-deficient APOBEC3G resistant to HIV-1 vif-induced degradation by reduced polyubiquitination

Yudi Wang, Qiujia Shao, Xianghui Yu, Wei Kong, James Hildreth, Bindong Liu

Research output: Contribution to journalArticle

25 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)4510-4519
Number of pages10
JournalJournal of Virology
Volume85
Issue number9
DOIs
StatePublished - May 2011
Externally publishedYes

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ASJC Scopus subject areas

  • Immunology
  • Virology

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