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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 PVYO,C and PVYN strains, although its coat protein (CP) belongs to the PVYN strain. Analysis of the CP of PVY-12 revealed that a point mutation in its N terminus switched it from PVYN-li...
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Published in: | Virus genes 2007-10, Vol.35 (2), p.359-367 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | A Syrian isolate of Potato virus Y (PVY), named PVY-12, reacted to two monoclonal antibodies that are specific to PVYO,C and PVYN strains, although its coat protein (CP) belongs to the PVYN strain. Analysis of the CP of PVY-12 revealed that a point mutation in its N terminus switched it from PVYN-like to PVYO-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 Glu₂₉ to Gly₂₉. The role of Gly₂₉ in the binding of PVY-12 to PVYO,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 Gly₂₉ to Glu₂₉ 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 Gly₂₉ was conserved in the CP of PVYO, PVYC, PVYNW, and non-potato isolates of PVY while Gln₁₇ and Glu₃₁ were conserved in the CP of PVYN/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. |
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ISSN: | 0920-8569 1572-994X |
DOI: | 10.1007/s11262-007-0115-y |