Serological prospects for peptide vaccines against foot-and-mouth disease virus.

The Journal of General Virology
N R ParryF Brown

Abstract

Antibodies to a synthetic peptide corresponding to the 141 to 160 amino acid sequence of the protein VP1 of type O foot-and-mouth disease virus (FMDV) neutralize a wider range of type O isolates than anti-virion serum. Extending this peptide at the amino terminus reduced the number of strains neutralized by the antipeptide sera. Reactions with antisera to peptides representing non-contiguous native sequences showed that it was also possible to increase the number of strains effectively neutralized. Selected substitutions of a single amino acid at position 148 markedly altered the neutralizing specificity of antibodies elicited by the 141 to 160 peptide. In particular, a peptide with an L----S substitution at this position induced antibodies which neutralized a type O and a type A virus equally, and guinea-pigs inoculated with it were protected from challenge with either virus. Attempts to isolate variant viruses resistant to neutralization with anti-peptide antibody indicated that these occurred at low frequency, and there was some evidence that resistance may be partially conferred by mutations outside the peptide sequence.

Citations

Mar 1, 1996·Journal of Peptide Science : an Official Publication of the European Peptide Society·M PegnaP Mascagni
Mar 26, 2011·Expert Review of Vaccines·Luis L Rodriguez, Cyril G Gay
Aug 28, 2020·Frontiers in Veterinary Science·Rodrigo Cañas-ArranzFrancisco Sobrino
Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Rodrigo Cañas-ArranzFrancisco Sobrino

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