Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization

Biochem Biophys Res Commun. 2006 Sep 15;348(1):271-7. doi: 10.1016/j.bbrc.2006.07.062. Epub 2006 Jul 24.

Abstract

By use of the yeast two-hybrid system, hepatitis C virus (HCV) F protein was found to interact with a cellular protein named prefoldin 2. The interaction was confirmed by confocal immunofluorescence microscopy as well as coimmunoprecipitation experiments. Prefoldin 2 is a subunit of a hexameric molecular chaperone complex, named prefoldin, which delivers nascent actin and tubulin proteins to the eukaryotic cytosolic chaperonin for facilitated folding. Functional prefoldin spontaneously assembles from its six subunits (prefoldin 1-6). In the yeast three-hybrid system, it was found that expression of HCV F protein impeded the interaction between prefoldin 1 and 2. By performing immunofluorescence experiment and non-denaturing gel electrophoresis, it was shown that expression of HCV F protein resulted in aberrant organization of tubulin cytoskeleton. Since HCV replication requires intact microtubule and actin polymerization, HCV F protein may serve as a modulator to prevent high level of HCV replication and thus contributes to viral persistence in chronic HCV infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chlorocebus aethiops
  • Cytoskeleton / metabolism
  • Cytoskeleton / ultrastructure
  • Gene Expression Regulation, Viral
  • Hepacivirus / physiology
  • Hepatitis C, Chronic / metabolism
  • Hepatitis C, Chronic / virology
  • Humans
  • Molecular Chaperones / metabolism*
  • Protein Binding
  • Tubulin / metabolism
  • Vero Cells
  • Viral Core Proteins / metabolism*
  • Virus Replication

Substances

  • Molecular Chaperones
  • Tubulin
  • Viral Core Proteins
  • hepatitis C protein F, Hepatitis C virus
  • prefoldin