Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K.
J Biol Chem
; 273(28): 17651-9, 1998 Jul 10.
Article
in En
| MEDLINE
| ID: mdl-9651361
ABSTRACT
Hepatitis C virus (HCV) core protein, a component of viral nucleocapsid, has been shown to modulate cellular and viral promoter activities. To identify potential cellular targets for HCV core protein, a human liver cDNA library was screened for core-interacting proteins using the yeast two-hybrid system. Among the proteins identified was heterogeneous nuclear ribonucleoprotein K (hnRNP K), which has been demonstrated to be a transcriptional regulator. The interaction of HCV core protein with hnRNP K was confirmed by glutathione S-transferase fusion protein binding assay, protein-protein blotting assay, and coimmunoprecipitation in vitro and in vivo. Additionally, these two proteins were shown to be partially colocalized in the nucleus. The hnRNP K-binding site in HCV core protein was mapped to the region from amino acid residues 25-91, a hydrophilic area near the N terminus. The HCV core protein-binding domain was located within amino acid residues 250 to 392, which contain the three proline-rich domains, of hnRNP K. Furthermore, HCV core protein relieved the suppression effect of hnRNP K on the activity of the human thymidine kinase gene promoter. The specific binding of HCV core protein to hnRNP K suggests that multiple functions of hnRNP K may be disrupted by the core protein during HCV infection and thus explains, in part, the pathogenesis of HCV.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Ribonucleoproteins
/
RNA, Heterogeneous Nuclear
/
Viral Core Proteins
Limits:
Animals
/
Humans
Language:
En
Journal:
J Biol Chem
Year:
1998
Document type:
Article
Affiliation country:
Estados Unidos