GB virus B and hepatitis C virus NS3 serine proteases share substrate specificity

J Virol. 1997 Jul;71(7):4985-9. doi: 10.1128/JVI.71.7.4985-4989.1997.

Abstract

GB virus B (GBV-B) is a recently discovered virus responsible for hepatitis in tamarins (Saguinus species). GBV-B belongs to the Flaviviridae family and is closely related to the human pathogen hepatitis C virus (HCV). Nonstructural protein 3 (NS3) of HCV has been shown to encompass a serine protease domain required for viral maturation. GBV-B and HCV share only about 30% of the amino acid sequence within the NS3 protease domain. The catalytic triad is conserved, and the residue Phe-154, presumed to be a crucial amino acid for determining the S1 specificity pocket of the HCV NS3 protease, is also conserved. We have expressed a synthetic gene encoding the GBV-B NS3 protease domain in Escherichia coli and have characterized the purified recombinant protein for its activity on HCV substrates. We have shown that the NS3 region of the GBV-B genome actually encodes a serine protease that, despite the low sequence homology, shares substrate specificity with the HCV NS3 protease.

MeSH terms

  • Amino Acid Sequence
  • Flaviviridae / enzymology*
  • Hepacivirus / enzymology*
  • Humans
  • Molecular Sequence Data
  • Protein Biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / metabolism*
  • Substrate Specificity
  • Viral Nonstructural Proteins / metabolism*

Substances

  • NS3 protein, hepatitis C virus
  • Recombinant Fusion Proteins
  • Viral Nonstructural Proteins
  • Serine Endopeptidases

Associated data

  • GENBANK/U22304