Biophysical characterization of hepatitis C virus core protein

Implications for interactions within the virus and host

Meghan Kunkel, Stanley Watowich

Research output: Contribution to journalArticle

31 Citations (Scopus)

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

Fingerprint

Viruses
Hepacivirus
Proteins
Nucleocapsid
Circular Dichroism
Oligomerization
Viral Genome
Fluorescence Spectrometry
Fluorescence spectroscopy
Protein C
Hepatitis C virus nucleocapsid protein
Tryptophan
Genes
Experiments

Keywords

  • Core protein
  • Hepatitis C virus
  • Protein biophysics

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Biophysical characterization of hepatitis C virus core protein : Implications for interactions within the virus and host. / Kunkel, Meghan; Watowich, Stanley.

In: FEBS Letters, Vol. 557, No. 1-3, 16.01.2004, p. 174-180.

Research output: Contribution to journalArticle

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