Key result
Immunization with a 32-amino acid tandem repeat peptide of FMDV VP1 elicited three distinct neutralizing antibody populations that recognized different epitopes and provided partial cross-protection.
A biosynthetic peptide of FMDV VP1 elicits multiple distinct neutralizing antibody populations, demonstrating potential for cross-protective immunity.
Animal data support exploring multi-epitope FMDV peptides; leaves open translation to livestock efficacy.
Foot-and-mouth disease virus (FMDV) capsid contains 60 copies each of four structural proteins, virus proteins 1-4. Virus protein 1 (VP1) plays an important immunogenic role, being the only VP that is immunogenic as an isolated protein. Even peptides representing a partial amino acid (AA) sequence of VP1 can induce protective immunity in experimental hosts. A 32 AA residue, in a tandem repeat configuration (32dimer), of sero/subtype A-12 Lp ab VP1 (AA 132-168) was highly immunogenic for its homologous subtype and partially protective for FMDV serotype A strain A24. This cross-reactivity was further demonstrable in the ELISA and mouse protection tests. Three different antibody populations were isolated by affinity chromatography (AFC) from the serum of a steer immunized with the 32dimer. Each population seems to recognize a different epitope on the 32dimer peptide since each fraction was defined as unique by its reactivity with different subtypes of FMDV virus in RIA, ELISA, neutralization and competition assays. Considering the neutralizing activity of each of the antibody populations the pattern of neutralization of the 32dimer elicited antiserum can be described. Two of the three epitopes were mapped by competition assays using synthetic peptides.
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Borca et al. (1990) studied Foot-and-mouth disease virus (FMDV). 32dimer of VP1 (AA 132-168) was evaluated on Immunogenicity and cross-reactivity. Immunization with a 32-amino acid tandem repeat peptide of FMDV VP1 elicited three distinct neutralizing antibody populations that recognized different epitopes and provided partial cross-protection.