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Modulation of mitogen-activated protein kinase-activated protein kinase 3 by hepatitis C virus core protein.

J. Virol.2013 May;87(10):5718-31. Epub 2013 Mar 13
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摘要


Hepatitis C virus (HCV) is highly dependent on cellular proteins for its own propagation. In order to identify the cellular factors involved in HCV propagation, we performed protein microarray assays using the HCV core protein as a probe. Of ~9,000 host proteins immobilized in a microarray, approximately 100 cellular proteins were identified as HCV core-interacting partners. Of these candidates, mitogen-activated protein kinase-activated protein kinase 3 was selected for further characterization. is a serine/threonine protein kinase that is activated by stress and growth inducers. Binding of HCV core to MAduanyu1529PK3 was confirmed by in vitro pulldown assay and further verified by coimmunoprecipitation assay. HCV core protein interacted with MAduanyu1529PK3 through amino acid residues 41 to 75 of core and the N-terminal half of kinase domain of In addition, both RNA and protein levels of MAduanyu1529PK3 were elevated in both HCV subgenomic replicon cells and cell culture-derived HCV (HCVcc)-infected cells. Silencing of MAduanyu1529PK3 expression resulted in decreases in both protein and HCV infectivity levels but not in the intracellular HCV RNA level. We showed that MAduanyu1529PK3 increased HCV IRES-mediated translation and HCV IRES activity was further increased by core protein. These data suggest that HCV core may modulate MAduanyu1529PK3 to facilitate its own propagation.

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