A structurally flexible and antigenically variable N-terminal domain of the hepatitis C virus E2/NS1 protein: implication for an escape from antibody

Virology. 1993 Jul;195(1):297-301. doi: 10.1006/viro.1993.1378.

Abstract

Hepatitis C virus persists in most infected hosts, and causes chronic hepatitis, liver cirrhosis, and/or hepatocellular carcinoma in humans. During the infection the RNA genome of hepatitis C virus undergoes frequent missense mutations at one or two "hypervariable" regions within a presumptive envelope gene (Okamoto et al., 1992, Virology 190, 894-899; Ogata et al., 1991, Proc. Natl. Acad. Sci. USA 88, 3392-3396). In the present study, we analyzed three cases of hepatitis C virus infection, two in chimpanzees and one in humans, for the antigenicity of peptides predicted from the hypervariable region of viral RNA obtained during the follow-up. Our results showed a successive appearance of hepatitis C virus mutants with antigenically distinct amino acid sequence within the domain; and the amino acid replacement was associated with an alteration of predicted local secondary structure of the epitope region. Hence, the hypervariable domain of the hepatitis C virus envelope appeared to be structurally flexible and antigenically variable, providing the virus a way to escape from host immunity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigenic Variation*
  • Antigens, Viral / chemistry
  • Antigens, Viral / immunology*
  • Epitopes
  • Hepacivirus / genetics
  • Hepacivirus / immunology*
  • Hepatitis Antibodies / immunology*
  • Hepatitis C / immunology*
  • Hepatitis C Antibodies
  • Hepatitis C Antigens
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Pan troglodytes
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid

Substances

  • Antigens, Viral
  • Epitopes
  • Hepatitis Antibodies
  • Hepatitis C Antibodies
  • Hepatitis C Antigens

Associated data

  • GENBANK/D01217
  • GENBANK/D10750