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Identification of a novel protein binding to hepatitis C virus core protein
Author(s) -
Chen Yunru,
Chen Tianyan,
Zhang Shulin,
Lin Shumei,
Zhao Yingren,
Ye Feng,
Zhang Xi,
Shi Lei,
Dang Shuangsuo,
Liu Min
Publication year - 2009
Publication title -
journal of gastroenterology and hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.214
H-Index - 130
eISSN - 1440-1746
pISSN - 0815-9319
DOI - 10.1111/j.1440-1746.2009.05846.x
Subject(s) - immunoprecipitation , hepatitis c virus , core protein , clone (java method) , cytoplasm , complementary dna , binding protein , microbiology and biotechnology , virology , in vitro , in vivo , biology , virus , gene , biochemistry , genetics
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.