Sequence conservation and antigenic variation of the structural proteins of equine rhinitis A virus.
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.
Varrasso
A
A
Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Parkville, Victoria 3010, Australia.
Drummer
H E
HE
Huang
J A
JA
Stevenson
R A
RA
Ficorilli
N
N
Studdert
M J
MJ
Hartley
C A
CA
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D005537:Aphthovirus / Q000737:chemistry / Q000145:classification / Q000276:immunology*; D002213:Capsid / Q000737:chemistry* / Q000276:immunology; D036022:Capsid Proteins; D017124:Conserved Sequence; D000939:Epitopes; D006736:Horses / Q000821:virology*; D008969:Molecular Sequence Data; D010802:Phylogeny; D011817:Rabbits
D000911:Antibodies, Monoclonal; D036022:Capsid Proteins; D000939:Epitopes