Foot-and-mouth disease virus challenge experiments in guinea-pigs and immunoassays with a range of peptides equivalent to either or both of the sequences 141 to 158 and 200 to 213 of VP1 showed the most effective structure, in terms of protection, to be one in which both ‘sites’ were present with a minimum of additional amino acids. An 80 residue peptide comprising amino acids 134 to 213 was considerably less effective than 40 or 45 residue peptides. The major site for the induction of protection was deduced to be in the region 141 to 158. Thus, protection with the 40 or 45 residue peptide did not appear to be due to the presence of antibody directed solely to the 200 to 213 sequence. Finally, induction of antibody to the latter site appeared to be dependent on both the size of the peptide and the disposition of ‘sites’ within it.

Keyword(s): FMDV , immunization and peptide vaccines

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