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Updated: May 9, 2026

A Protocol for Analyzing Hepatitis C Virus Replication
Published on: June 26, 2014
Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation
Seung-Ae Yim1, Yun-Sook Lim, Jong-Wook Kim
1National Research Laboratory of Hepatitis C Virus, Ilsong Institute of Life Science, Hallym University, Anyang, Korea.
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.
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