Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2

J Virol. 1994 Apr;68(4):2731-4. doi: 10.1128/JVI.68.4.2731-2734.1994.

Abstract

We determined the partial amino (N)-terminal amino acid sequence of hepatitis C virus p21 (nonstructural protein 2 [NS2]). Cleavage at the p21 (NS2) N terminus depended on the presence of microsomal membranes. The amino-terminal position of p21 (NS2) was assigned to amino acid 810 of the hepatitis C virus strain IIJ precursor polyprotein. Mutation of the alanine residue at position P1 of the putative cleavage site inhibited membrane-dependent processing. This alteration in processing together with the fact that hydrophobic amino acid residues are clustered upstream of the putative cleavage site suggested the involvement of a signal peptidase(s) in the cleavage. Furthermore, mutation analysis of this possible cleavage site revealed the presence of another microsome membrane-dependent cleavage site upstream of the N terminus of p21 (NS2).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • DNA Mutational Analysis
  • Hepacivirus / metabolism*
  • Microsomes / metabolism
  • Molecular Sequence Data
  • Protein Processing, Post-Translational*
  • Recombinant Fusion Proteins / metabolism
  • Sequence Analysis
  • Tetrahydrofolate Dehydrogenase / biosynthesis
  • Tetrahydrofolate Dehydrogenase / genetics
  • Viral Nonstructural Proteins / genetics*

Substances

  • Recombinant Fusion Proteins
  • Viral Nonstructural Proteins
  • Tetrahydrofolate Dehydrogenase