Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.
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 carb...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3701667?pdf=render |
| _version_ | 1818623766275555328 |
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| author | Seung-Ae Yim Yun-Sook Lim Jong-Wook Kim Soon B Hwang |
| author_facet | Seung-Ae Yim Yun-Sook Lim Jong-Wook Kim Soon B Hwang |
| author_sort | Seung-Ae Yim |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-16T18:46:17Z |
| format | Article |
| id | doaj.art-59fb8e7fe2ca4143a2e1c2d0d3131f54 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-16T18:46:17Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-59fb8e7fe2ca4143a2e1c2d0d3131f542022-12-21T22:20:51ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0187e6817010.1371/journal.pone.0068170Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.Seung-Ae YimYun-Sook LimJong-Wook KimSoon B HwangHepatitis 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.http://europepmc.org/articles/PMC3701667?pdf=render |
| spellingShingle | Seung-Ae Yim Yun-Sook Lim Jong-Wook Kim Soon B Hwang Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. PLoS ONE |
| title | Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. |
| title_full | Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. |
| title_fullStr | Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. |
| title_full_unstemmed | Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. |
| title_short | Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation. |
| title_sort | nonstructural 5a protein of hepatitis c virus interacts with pyruvate carboxylase and modulates viral propagation |
| url | http://europepmc.org/articles/PMC3701667?pdf=render |
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