BVD monoclonal antibodies: relationship between viral protein specificity and viral strain specificity.
Seventeen monoclonal antibodies raised against bovine viral diarrhoea virus were divided into three groups on the basis of radioimmunoprecipitation results. Seven monoclonal antibodies precipitated a polypeptide of 80kD and defined four domains, all of which showed considerable conservation amongst the 180 pestivirus strains and isolates examined. Nine monoclonal antibodies, including six with virus neutralizing activity, precipitated a 53kD polypeptide and all appeared to be directed towards a single domain of clustered epitopes. Several of these epitopes were present in many ruminant virus strains and isolates, but not in hog cholera viruses. A single monoclonal antibody precipitated a 48kD polypeptide, defining an epitope that was also present on many ruminant viruses, but not hog cholera viruses. Most pestiviruses from cattle and some from sheep shared a number of epitopes located on three different proteins.
Paton
D J
DJ
Central Veterinary Laboratory, U.K.
Sands
J J
JJ
Roehe
P M
PM
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001667:Binding, Competitive; D002417:Cattle; D001908:Diarrhea Viruses, Bovine Viral / Q000276:immunology*; D000939:Epitopes; D011233:Precipitin Tests; D013045:Species Specificity; D014764:Viral Proteins / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D014764:Viral Proteins