Mutations in the protein kinase-binding domain of the NS5A protein in patients infected with hepatitis C virus type 1a are associated with treatment response

J Infect Dis. 2000 Feb;181(2):432-41. doi: 10.1086/315263.

Abstract

An interaction of the hepatitis C virus (HCV) NS5A protein with the interferon (IFN)-alpha-inducible double-stranded RNA-activated protein kinase (PKR) was demonstrated in vitro. The clinical correlation between amino acid mutations within the HCV NS5A region and response to antiviral treatment is controversial. Thirty-two patients chronically infected with HCV-1a, who were treated with IFN-alpha with or without ribavirin, were studied. The carboxy-terminal half of HCV NS5A was sequenced and was investigated by phylogenetic and conformational analyses. Eight patients achieved a sustained virologic response. An end-of-treatment response but relapse thereafter was observed among 8 patients, whereas 16 patients were nonresponders. The median number of mutations within the PKR-binding domain but not within the previously described IFN sensitivity-determining region was significantly higher for patients with sustained (3 mutations [range, 1-5]) or end-of-treatment (4 mutations [range, 1-5]) virologic response than for nonresponders (2 mutations [range, 0-3]) (P=.0087). Phylogenetic and conformational analyses of NS5A sequences allowed no differentiation between sensitive and resistant strains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Antiviral Agents / therapeutic use*
  • Binding Sites
  • Drug Therapy, Combination
  • Female
  • Hepacivirus / genetics*
  • Hepacivirus / metabolism
  • Hepatitis C Antibodies / blood
  • Hepatitis C, Chronic / drug therapy*
  • Hepatitis C, Chronic / virology
  • Humans
  • Interferon Type I / therapeutic use*
  • Male
  • Middle Aged
  • Molecular Sequence Data
  • Mutation
  • Phylogeny
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Viral / analysis
  • Recombinant Proteins
  • Reverse Transcriptase Polymerase Chain Reaction
  • Ribavirin / therapeutic use
  • Viral Nonstructural Proteins / chemistry
  • Viral Nonstructural Proteins / genetics*
  • Viral Nonstructural Proteins / metabolism
  • eIF-2 Kinase / metabolism*

Substances

  • Antiviral Agents
  • Hepatitis C Antibodies
  • Interferon Type I
  • RNA, Viral
  • Recombinant Proteins
  • Viral Nonstructural Proteins
  • Ribavirin
  • eIF-2 Kinase
  • NS-5 protein, hepatitis C virus