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Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.


ABSTRACT: Hepatitis C virus (HCV) is highly dependent on cellular factors for its own propagation. By employing tandem affinity purification method, we identified pyruvate carboxylase (PC) as a cellular partner for NS5A protein. NS5A interacted with PC through the N-terminal region of NS5A and the biotin carboxylase domain of PC. PC expression was decreased in cells expressing NS5A and HCV-infected cells. Promoter activity of PC was also decreased by NS5A protein. However, FAS expression was increased in cells expressing NS5A and cell culture grown HCV (HCVcc)-infected cells. Silencing of PC promoted fatty acid synthase (FAS) expression level. These data suggest HCV may modulate PC via NS5A protein for its own propagation.

SUBMITTER: Yim SA 

PROVIDER: S-EPMC3701667 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.

Yim Seung-Ae SA   Lim Yun-Sook YS   Kim Jong-Wook JW   Hwang Soon B SB  

PloS one 20130704 7


Hepatitis C virus (HCV) is highly dependent on cellular factors for its own propagation. By employing tandem affinity purification method, we identified pyruvate carboxylase (PC) as a cellular partner for NS5A protein. NS5A interacted with PC through the N-terminal region of NS5A and the biotin carboxylase domain of PC. PC expression was decreased in cells expressing NS5A and HCV-infected cells. Promoter activity of PC was also decreased by NS5A protein. However, FAS expression was increased in  ...[more]

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