Key result
The presence of an arginine residue at position 20 of the 2A protease is essential for the induction of high viraemia and significant disease in pigs infected with swine vesicular disease virus.
Arginine at position 20 of the 2A protease is a key determinant of pathogenicity for swine vesicular disease virus in pigs.
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Arginine at 2A position 20 drives SVDV virulence in pigs; hypothesis-generating for enterovirus research and leaves open any veterinary application.
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.
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Inoue et al. (2007) studied Swine vesicular disease virus (SVDV) infection. Chimeric viruses with arginine residue at position 20 of the 2A protease vs. Parental pathogenic and attenuated strains was evaluated on Induction of high viraemia and appearance of significant disease. The presence of an arginine residue at position 20 of the 2A protease is essential for the induction of high viraemia and significant disease in pigs infected with swine vesicular disease virus.
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