Limited effect on NS3-NS4A protein cleavage after alanine substitutions within the immunodominant HLA-A2-restricted epitope of the hepatitis C virus genotype 3a non-structural 3/4A protease

J Gen Virol. 2012 Aug;93(Pt 8):1680-1686. doi: 10.1099/vir.0.043745-0. Epub 2012 May 16.

Abstract

It has been well established that immunological escape mutations within the hepatitis C virus genotype (gt) 1a non-structural (NS) 3/4A protease are partly prevented by a reduction in viral protease fitness. Surprisingly little is known about whether similar mutations affect proteases from other genotypes. In the present study, we assessed both the HLA-A2-restricted CTL response and gt3a NS3/4A protease fitness. Similar to gt1, the 1073-1081 epitope was immunodominant within the gt3a-specific HLA-A2-restricted CTL response, despite sequence similarity of only 56 % between the gt1a and gt3a genes. However, unlike the gt1a NS3/4A protease, all residues within the gt3a 1073-1081 epitope could be replaced sequentially by alanine while retaining protease activity, at least in part.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / chemistry*
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Cloning, Molecular
  • Gene Expression Regulation, Viral / physiology*
  • Genotype
  • Hepacivirus / genetics*
  • Humans
  • Immunodominant Epitopes / genetics*
  • Molecular Sequence Data
  • Viral Nonstructural Proteins / chemistry
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*

Substances

  • Immunodominant Epitopes
  • NS3 protein, hepatitis C virus
  • NS4B protein, flavivirus
  • Viral Nonstructural Proteins
  • Alanine

Associated data

  • GENBANK/JQ514562
  • GENBANK/JQ514563