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Hepatitis C virus NS5A protein modulates c-Jun N-terminal kinase through interaction with tumor necrosis factor receptor-associated factor 2

Title
Hepatitis C virus NS5A protein modulates c-Jun N-terminal kinase through interaction with tumor necrosis factor receptor-associated factor 2
Authors
Park K.-J.Choi S.-H.Choi D.-H.Park J.-M.Yie S.W.Lee S.Y.Hwang S.B.
Ewha Authors
이수영
SCOPUS Author ID
이수영scopus
Issue Date
2003
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 278, no. 33, pp. 30711 - 30718
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The nonstructural 5A (NS5A) protein of hepatitis C virus (HCV) is a phosphoprotein possessing various functions. We have previously reported that the HCV NS5A protein interacts with tumor necrosis factor (TNF) receptor-associated factor (TRAF) domain of TRAF2 (Park, K.-J., Choi, S.-H., Lee, S. Y., Hwang, S. B., and Lai, M. M. C. (2002) J. Biol. Chem. 277, 13122-13128). Both TNF-α- and TRAF2-mediated nuclear factor-κB (NF-κB) activations were inhibited by NS5A-TRAF2 interaction. Because TRAF2 is required for the activation of both NF-κB and c-Jun N-terminal kinase (JNK), we investigated HCV NS5A protein for its potential capacity to modulate TRAF2-mediated JNK activity. Using in vitro kinase assay, we have found that NS5A protein synergistically activated both TNF-α- and TRAF2-medidated JNK in human embryonic kidney 293T cells. Furthermore, synergism of NS5A-mediated JNK activation was inhibited by dominant-negative form of MEK kinase 1. Our in vivo binding data show that NS5A does not inhibit interaction between TNF receptor-associated death domain and TRAF2 protein, indicating that NS5A and TRAF2 may form a ternary complex with TNF receptor-associated death domain. These results indicate that HCV NS5A protein modulates TNF signaling of the host cells and may play a role in HCV pathogenesis.
DOI
10.1074/jbc.M209623200
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자연과학대학 > 생명과학전공 > Journal papers
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