The specificity of guinea pig antisera against large cyanogen bromide-cleaved peptides of the virus capsid protein VP of foot-and-mouth disease virus type O, strain Kaufbeuren has been characterized by double immunodiffusion, virus neutralization and protection tests. Antibodies to purified 146S particles and the cleavage peptides of VP showed an incomplete cross-section against VP peptide antigen when reacted in immunodiffusion tests, indicating that new antigenic determinants are exhibited by the peptides which are not recognized by the antiserum against the native virus proteins.

The immune response against the reduced, unfolded chain constituents of VP was lower in comparison to that of native virus particles but still some immunological determinants remained actively capable of inducing virus-neutralizing antibodies in immunized guinea pigs.


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