Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 12, Pages 10051-10057Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.166108
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Funding
- Ministry of Education, Science, Sports, and Culture of Japan [09309011]
- Ministry of Health, Labor, and Welfare, Japan
- MEXT [21370047 22121517]
- JST-SENTAN
- Naito Foundation
- YCU-AMRC
- Grants-in-Aid for Scientific Research [09309011, 21370047] Funding Source: KAKEN
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The cytidine deaminase APOBEC3G, which is incorporated into nascent virus particles, possesses potent antiviral activity and restricts Vif-deficient HIV-1 replication at the reverse transcription step through deamination-dependent and -independent effects. HIV-1 Vif counteracts the antiviral activity of APOBEC3G by inducing APOBEC3G polyubiquitination and its subsequent proteasomal degradation. In this study, we show that overexpression of heat shock protein 70 (HSP70) blocked the degradation of APOBEC3G in the ubiquitin-proteasome pathway by HIV-1 Vif, rendering the viral particles non-infectious. In addition, siRNA targeted knock-down of HSP70 expression enhanced the Vif-mediated degradation of APOBEC3G. A co-immunoprecipitation study revealed that overexpression of HSP70 inhibited APOBEC3G binding to HIV-1 Vif. Thus, we provide evidence for a host protein-mediated suppression of HIV-1 replication in an APOBEC3G-dependent manner.
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