Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells

Jiadong Wang, Wenyan Tong, Xiaonan Zhang, Li Chen, Zhigang Yi, Tingting Pan, Yunwen Hu, Li Xiang, Zhenghong Yuan

Research output: Contribution to journalReview articlepeer-review

53 Citations (Scopus)

Abstract

Hepatitis C virus non-structural protein NS5A plays an important role in viral replication and various cellular events. To gain further insight into the function of NS5A, we screened a human fetal liver cDNA library for its interacting proteins using the yeast two-hybrid system. FKBP38, a 38 kDa immunosuppressant FK506-binding protein, was identified and its interaction with NS5A was confirmed by both in vitro and in vivo. The interaction was mapped to the amino acids 148-236 of NS5A containing a BH domain (Bcl-2 homology domain). Besides, both NS5A and FKBP38 were found to localize in mitochondria and endoplasmic reticulum. Moreover, NS5A stably expressing Huh7 hepatoma cells showed more resistance to apoptosis and such inhibition of apoptosis could specifically be abrogated by depletion of FKBP38 using RNA interference. These results indicate that HCV NS5A inhibits apoptosis through interaction with FKBP38.

Original languageEnglish
Pages (from-to)4392-4400
Number of pages9
JournalFEBS Letters
Volume580
Issue number18
DOIs
Publication statusPublished - 7 Aug 2006
Externally publishedYes

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