The immunogenic capsid protein (VPt), circa 30 kilodaltons (kd), of foot-and-mouth disease virus was examined for (i) its ability to induce neutralizing antibody in guinea pigs after chemical modifications and CNBr or tryptic cleavages and (ii) N-terminal amino acid sequence homology across three virus types. The immunogenicity of VPt was inactivated by glutaraldehyde treatment, carboxymethylation and maleylation or citraconylation. However, de-citraconylation restored part of the lost activity. Cleavage of type A12 VPt with CNBr produced an immunogenic peptide of circa 13 kd. A slightly larger (ca. 16 kd) immunogenic doublet, VPτa¾, was obtained by tryptic cleavage of VPt in the virion. Sequence homologies of circa 85% were found between the first 26 amino acids at the N-terminus of VP chains from virus types A12 strain 119 (A12), C3 Resende (C311) and Oi Brugge (Oib).

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