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

FEBS Letters

Watowich, Stanley J¹  Kunkel, Meghan¹ 

[1] Department of Human Biological Chemistry and Genetics and the Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA

关键词: Core protein;    Protein biophysics;    Hepatitis C virus;    HCV;    hepatitis C virus;    CD;    circular dichroism;    S;    sedimentation coefficient;    DTT;    dithiothreitol;   

DOI  :  10.1016/S0014-5793(03)01486-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown