Sequence conservation and antigenic variation of the structural proteins of equine rhinitis A virus

J Virol. 2001 Nov;75(21):10550-6. doi: 10.1128/JVI.75.21.10550-10556.2001.

Abstract

The nucleotide and deduced amino acid sequences of the P1 region of the genomes of 10 independent equine rhinitis A virus (ERAV) isolates were determined and found to be very closely related. A panel of seven monoclonal antibodies to the prototype virus ERAV.393/76 that bound to nonneutralization epitopes conserved among all 10 isolates was raised. In serum neutralization assays, rabbit polyclonal sera and sera from naturally and experimentally infected horses reacted in a consistent and discriminating manner with the 10 isolates, which indicated the existence of variation in the neutralization epitopes of these viruses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology
  • Aphthovirus / chemistry
  • Aphthovirus / classification
  • Aphthovirus / immunology*
  • Capsid / chemistry*
  • Capsid / immunology
  • Capsid Proteins
  • Conserved Sequence
  • Epitopes
  • Horses / virology*
  • Molecular Sequence Data
  • Phylogeny
  • Rabbits

Substances

  • Antibodies, Monoclonal
  • Capsid Proteins
  • Epitopes