Biophysical characterization of hepatitis C virus core protein: Implications for interactions within the virus and host

Meghan Kunkel, Stanley J. Watowich

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

A primary function of the hepatitis C virus (HCV) core protein is to package the viral genome within a nucleocapsid. In addition, core protein has been shown to interact with more than a dozen cellular proteins, and these interactions have been suggested to play critical roles in HCV pathogenesis. A more complete knowledge of the biophysical properties of the core protein may help to clarify its role in HCV pathogenesis and nucleocapsid assembly and provide a basis for the development of novel anti-HCV therapies. Here we report that recombinant mature core protein exists as a large multimer in solution under physiological conditions. Far-UV circular dichroism (CD) experiments showed that the mature core protein contains stable secondary structure. Studies with truncated core protein demonstrated that the C-terminal region of the core protein is critical for its folding and oligomerization. Intrinsic fluorescence spectroscopy and near-UV CD analysis indicated that the tryptophan-rich region (residues 76-113) is largely solvent-exposed and not likely responsible for multimerization of the mature core protein in vitro.

Original languageEnglish (US)
Pages (from-to)174-180
Number of pages7
JournalFEBS Letters
Volume557
Issue number1-3
DOIs
StatePublished - Jan 16 2004

Keywords

  • Core protein
  • Hepatitis C virus
  • Protein biophysics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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