Antigenic comparison of the polypeptides of foot-and-mouth disease virus serotypes and other picornaviruses.
The cross-reactivity of proteins coded for by the seven serotypes of foot-and-mouth disease virus (FMDV) was assessed by reaction of infected cell lysates with polyclonal and monospecific antisera against the structural and nonstructural proteins of FMDV type A12 strain 119ab. It was shown that the homologous polypeptides from most serotypes are antigenically related. The least cross-reactivity occurred between VP1, VP3, and the protease (3C) of type A12 and South African Territories types 1 and 3. There was also a reduced degree of reactivity of A12 VP1 serum with VP1 from some A subtypes and the other serotypes. Comparison of FMDV proteins with polypeptides from other picornaviruses by a radioimmune binding assay revealed a low level of reactivity of antisera against some A12 polypeptides with encephalomyocarditis virus (EMCV) infected cell lysates but no reactivity with bovine enterovirus type 1 and swine vesicular disease virus infected cells. The same EMCV proteins were immunoprecipitated by the various reactive A12 antisera, but the reaction was abolished if the lysate from EMCV infected cells was denatured prior to immunoprecipitation.
D000818:Animals; D000956:Antigens, Viral / Q000032:analysis*; D005537:Aphthovirus / Q000032:analysis / Q000145:classification / Q000276:immunology*; D002417:Cattle; D003429:Cross Reactions; D004686:Encephalomyocarditis virus / Q000032:analysis / Q000276:immunology; D004770:Enterovirus / Q000032:analysis / Q000276:immunology; D004771:Enteroviruses, Porcine / Q000032:analysis / Q000276:immunology; D000939:Epitopes; D010455:Peptides / Q000276:immunology; D010849:Picornaviridae / Q000032:analysis / Q000276:immunology*; D012703:Serotyping; D014764:Viral Proteins / Q000032:analysis / Q000276:immunology*; D015678:Viral Structural Proteins
D000956:Antigens, Viral; D000939:Epitopes; D010455:Peptides; D014764:Viral Proteins; D015678:Viral Structural Proteins