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pubmed-article:2479714pubmed:abstractTextAntibodies 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.lld:pubmed
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pubmed-article:2479714pubmed:dateRevised2003-11-14lld:pubmed
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pubmed-article:2479714pubmed:articleTitleSerological prospects for peptide vaccines against foot-and-mouth disease virus.lld:pubmed
pubmed-article:2479714pubmed:affiliationDepartment of Virology, Wellcome Biotechnology Ltd, Beckenham, Kent, U.K.lld:pubmed
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