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Significance of arginine 20 in the 2A protease for swine vesicular disease virus pathogenicity

¹ Research Team for Exotic Diseases, National Institute of Animal Health, Kodaira, Tokyo 187-0022, Japan
² BBSRC Institute for Animal Health, Pirbright, Woking, Surrey GU24 0NF, UK
³ National Veterinary Institute, Technical University of Denmark, Lindholm, DK-4771 Kalvehave, Denmark

Correspondence
Graham J. Belsham
grb{at}vet.dtu.dk

Pathogenic and attenuated strains of swine vesicular disease virus (SVDV), an enterovirus, have been characterized previously and, by using chimeric infectious cDNA clones, the key determinants of pathogenicity in pigs have been mapped to the coding region for 1D–2A. Within this region, residue 20 of the 2A protease is particularly significant. Inoculation of pigs with mutant viruses containing single amino acid substitutions at this residue leads to the appearance of revertants, often containing an arginine at this position encoded by an AGA codon, one of six codons for this residue. The properties in pigs of two chimeric viruses, each with an arginine residue at this position but encoded by different codons, have been investigated in parallel with the parental pathogenic and attenuated strains. Presence of the arginine residue, but not of the AGA codon, is essential for induction of high viraemia and appearance of significant disease.