@article{mbs:/content/journal/jgv/10.1099/0022-1317-70-11-2919, author = "Parry, N. R. and Ouldridge, E. J. and Barnett, P. V. and Clarke, B. E. and Francis, M. J. and Fox, J. D. and Rowlands, D. J. and Brown, F.", title = "Serological Prospects for Peptide Vaccines against Foot-and-Mouth Disease Virus", journal= "Journal of General Virology", year = "1989", volume = "70", number = "11", pages = "2919-2930", doi = "https://doi.org/10.1099/0022-1317-70-11-2919", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-70-11-2919", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "peptide vaccines", keywords = "heterotypic cross-protection", keywords = "neutralizing specificity", keywords = "FMDV", abstract = "Summary 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 anti-peptide 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.", }