The hepatitis C virus (HCV) core protein is a structural component of the nucleocapsid and has been shown to modulate cellular signaling pathways by interaction with various cellular proteins. In the present study, we investigated the role of HCV core protein in viral RNA replication. Immunoprecipitation experiments demonstrated that the core protein binds to the amino-terminal region of RNA-dependent RNA polymerase (RdRp), which encompasses the finger and palm domains. Direct interaction between HCV RdRp and core protein led to inhibition of RdRp RNA synthesis activity of in vitro. Furthermore, over-expression of core protein, but not its derivatives lacking the RdRp-interacting domain, suppressed HCV replication in a hepatoma cell line harboring an HCV subgenomic replicon RNA. Collectively, our results suggest that the core protein, through binding to RdRp and inhibiting its RNA synthesis activity, is a viral regulator of HCV RNA replication.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2009 Aug 14|
Bibliographical noteFunding Information:
We thank Drs. Christoph Seeger and Takaji Wakita for providing pZS2 and pJFH1 plasmids, respectively. This work was supported by Korea Research Foundation Grants KRF 2005-015-C00372 and KRF-2004-005-C00148. S.J.K. was the recipient of a postdoctoral fellowship from the BK21 program of the Korea Ministry of Education and Human Resources Development. J.H.K. was supported in part by the BK21 program.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology