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J Gen Virol 70 (1989), 2919-2930; DOI 10.1099/0022-1317-70-11-2919
© 1989 Society for General Microbiology
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Serological Prospects for Peptide Vaccines against Foot-and-Mouth Disease Virus

N. R. Parry1, E. J. Ouldridge2, P. V. Barnett1, B. E. Clarke1, M. J. Francis1, J. D. Fox1,{dagger}, D. J. Rowlands1 and F. Brown1

1 Department of Virology, Wellcome Biotechnology Ltd, Langley Court, Beckenham, Kent BR3 3BS
and2 Coopers Animal Health Ltd, Ash Road, Pirbright, Surrey GU24 0NQ, U.K.

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.

Keywords: FMDV, peptide vaccines, neutralizing specificity, heterotypic cross-protection

{dagger} Present address: Department of Medical Microbiology, University College and Middlesex School of Medicine, Riding House Street, London WC1E 6JJ, U.K.

Received 12 April 1989; accepted 7 July 1989.




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Copyright © 1989 by the Society for General Microbiology.