Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23861867.
- Also identified by DOI 10.1371/journal.pone.0068170 and PMC identifier 3701667.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Fatty Acid Synthase, Type I
- Hepacivirus
- Hepatocytes
- Pyruvate Carboxylase
- Viral Nonstructural Proteins