Identification of a novel protein binding to hepatitis C virus core protein.

Article Details

Citation

Chen YR, Chen TY, Zhang SL, Lin SM, Zhao YR, Ye F, Zhang X, Shi L, Dang SS, Liu M

Identification of a novel protein binding to hepatitis C virus core protein.

J Gastroenterol Hepatol. 2009 Jul;24(7):1300-4. doi: 10.1111/j.1440-1746.2009.05846.x. Epub 2009 Apr 13.

PubMed ID
19486448 [ View in PubMed
]
Abstract

BACKGROUND: Hepatitis C virus (HCV) core protein is a multi-functional viral protein that interacts with several target proteins of both viral and cellular origin. AIM AND METHODS: To gain insight into the mechanism of action of HCV core protein, we used a yeast two-hybrid system to identify the core protein-interacting cellular targets. RESULTS: A cDNA clone encoding an aspartoacylase was obtained, termed aspartoacylase 3 (ACY3). Interaction between ACY3 and HCV core protein was verified using a co-immunoprecipitation assay in vitro, and a mammalian two-hybrid system in vivo. Fluorescence microscopy showed green fluorescence protein-fused ACY3 localized in the cytoplasm. CONCLUSION: Our data suggest that ACY3 is an HCV core binding protein, which may play a role in the development of HCV-associated diseases.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)Q96HD9Details
Genome polyproteinP27958Details