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Related Experiment Videos

A second hepatitis C virus-encoded proteinase

A Grakoui1, D W McCourt, C Wychowski

  • 1Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110-1093.

Proceedings of the National Academy of Sciences of the United States of America
|November 15, 1993
PubMed
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Researchers identified a second hepatitis C virus (HCV)-encoded proteinase responsible for cleaving the viral polyprotein at the 2/3 site. This discovery aids in understanding HCV replication and developing new antiviral strategies.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Hepatitis C virus (HCV) polyprotein processing requires host and viral proteinases.
  • Several cleavage sites are processed by host signal peptidase or the HCV NS3 serine proteinase.
  • The enzyme mediating cleavage at the 2/3 site remained unidentified.

Purpose of the Study:

  • To identify the proteinase responsible for cleavage at the HCV 2/3 site.
  • To characterize the mechanism and requirements for 2/3 site processing.
  • To investigate the role of NS2 and NS3 proteins in viral polyprotein maturation.

Main Methods:

  • Site-directed mutagenesis of NS2 and NS3 proteins.
  • Expression of HCV polyprotein in mammalian cells, E. coli, and cell-free systems.

Related Experiment Videos

  • Analysis of polyprotein cleavage products using various expression systems.

    • Main Results:

    • The 2/3 cleavage site was defined and mapped to a region between amino acids 827 and 1207.
    • Mutations in NS2 residues His-952 or Cys-993 abolished 2/3 site cleavage.
    • Cleavage occurred efficiently in diverse expression systems and could be mediated in trans.

    Conclusions:

    • A second, HCV-encoded proteinase, likely within the NS2 protein, mediates 2/3 site cleavage.
    • This cleavage is independent of NS3 serine proteinase activity.
    • The findings facilitate purification and characterization of this novel viral enzyme for antiviral development.