A point mutation changes the serotype of a potato virus Y isolate; genomic determination of the serotype of PVY strains.

A Syrian isolate of Potato virus Y (PVY), named PVY-12, reacted to two monoclonal antibodies that are specific to PVY(O,C) and PVY(N) strains, although its coat protein (CP) belongs to the PVY(N) strain. Analysis of the CP of PVY-12 revealed that a point mutation in its N terminus switched it from PVY(N)-like to PVY(O)-like at this position. This mutation changed the second nucleotide of the codon that encodes the 29th amino acid of the CP of PVY-12 from A to G, which resulted in one amino acid substitution from Glu(29 )to Gly(29). The role of Gly(29) in the binding of PVY-12 to PVY(O,C)-specific monoclonal antibody was confirmed by gene expression in Escherichia coli. The N terminus of the CP gene of PVY-12 and another PVY isolate of the N serotype with identical CP to PVY-12 except for one amino acid substitution from Gly(29 )to Glu(29) was cloned and expressed in E. coli using a pUC18 vector. Resulting antigens showed similar reactivity to the relevant antibodies as same as the native CPs of these two isolates. Further analysis of the CP of PVY isolates showed that Gly(29) was conserved in the CP of PVY(O), PVY(C), PVY(N)W, and non-potato isolates of PVY while Gln(17) and Glu(31 )were conserved in the CP of PVY(N/NTN). Therefore, these amino acids are characteristic of the CP for these strain groups and subgroups in agreement with the serotype and phylogenetic relationships previously determined.