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.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • Cytosol / enzymology
  • Hepacivirus / genetics
  • Hepacivirus / metabolism*
  • Humans
  • Immunoprecipitation
  • Liver / enzymology*
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Recombinant Fusion Proteins / metabolism
  • Transfection
  • Two-Hybrid System Techniques
  • Viral Core Proteins / genetics
  • Viral Core Proteins / metabolism*

Substances

  • Recombinant Fusion Proteins
  • Viral Core Proteins
  • Amidohydrolases
  • aspartoacylase