Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.
- Resource Type
- article
- Authors
- Seung-Ae Yim; Yun-Sook Lim; Jong-Wook Kim; Soon B Hwang
- Source
- PLoS ONE, Vol 8, Iss 7, p e68170 (2013)
- Subject
- Medicine
Science
- Language
- English
- ISSN
- 1932-6203
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.