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

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.

SUBMITTER: Varrasso A

PROVIDER: S-EPMC114636 | biostudies-literature | 2001 Nov

REPOSITORIES: biostudies-literature

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

Varrasso A A Drummer H E HE Huang J A JA Stevenson R A RA Ficorilli N N Studdert M J MJ Hartley C A CA

Journal of virology 20011101 21

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 discrim ...[more]

PMID: 11581430

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