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

Varrasso A, Drummer HE, Huang JA, Stevenson RA, Ficorilli N, Studdert MJ, Hartley CA

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  • Journal Journal of virology

  • Published 25 Oct 2001

  • Volume 75

  • ISSUE 21

  • Pagination 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.