Identification of a neutralizing epitope in the betaE-betaF loop of VP1 of equine rhinitis A virus, defined by a neutralization-resistant variant

J Gen Virol. 2004 Sep;85(Pt 9):2545-2553. doi: 10.1099/vir.0.80175-0.

Abstract

Equine rhinitis A virus strain 393/76 (ERAV.393/76) was passaged in the presence of post-infection ERAV.393/76 equine polyclonal antiserum (EPA). Viruses with increased resistance to neutralization by EPA were obtained after 15 passages. Compared with the parent virus, five plaque-purified, neutralization-resistant mutant viruses, in addition to the non-plaque-purified viruses that were examined, had a Glu-->Lys change at position 658, which is located in the predicted betaE-betaF (EF) loop of VP1. Rabbit antiserum was prepared against the isolated EF loop of ERAV.393/76 VP1 expressed as a fusion protein with glutathione S-transferase. This antiserum bound to purified ERAV.393/76 in Western blots, but not to the neutralization-resistant mutant virus or to ERAV.PERV/62, a naturally occurring ERAV strain that has a Lys residue at position 658. These results suggest that the EF loop of VP1 is involved in a neutralization epitope of ERAV.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Aphthovirus / genetics
  • Aphthovirus / isolation & purification*
  • Capsid Proteins / analysis*
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics
  • Chlorocebus aethiops
  • Epitopes / analysis
  • Genome, Viral
  • Glutamine / chemistry
  • Horse Diseases / virology*
  • Horses
  • Lysine / chemistry
  • Molecular Sequence Data
  • Mutation
  • Neutralization Tests
  • Picornaviridae Infections / veterinary*
  • Picornaviridae Infections / virology
  • Sequence Alignment
  • Vero Cells

Substances

  • Capsid Proteins
  • Epitopes
  • Glutamine
  • Lysine