Induction of heat-shock protein 70 by prostaglandin A1 inhibits HIV-1 Vif-mediated degradation of APOBEC3G

2013 ◽  
Vol 99 (3) ◽  
pp. 307-311 ◽  
Author(s):  
Ryuichi Sugiyama ◽  
Makoto Abe ◽  
Hironori Nishitsuji ◽  
Yuko Murakami ◽  
Hiroaki Takeuchi ◽  
...  
2000 ◽  
Vol 259 (2) ◽  
pp. 398-403 ◽  
Author(s):  
Isabelle Agostini ◽  
Serguei Popov ◽  
Jianhua Li ◽  
Larisa Dubrovsky ◽  
Tang Hao ◽  
...  

2011 ◽  
Vol 286 (12) ◽  
pp. 10051-10057 ◽  
Author(s):  
Ryuichi Sugiyama ◽  
Hironori Nishitsuji ◽  
Ayako Furukawa ◽  
Masato Katahira ◽  
Yuichiro Habu ◽  
...  

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.


2001 ◽  
Vol 120 (5) ◽  
pp. A152-A152
Author(s):  
H SUZUKI ◽  
S NAGAHASHI ◽  
M MIYAZAWA ◽  
M MORI ◽  
H NAGATA ◽  
...  

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