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A single amino acid mutation alters the capsid protein electrophoretic double-band phenotype of the Plum pox virus strain PPV-Rec

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Abstract

Plum pox virus (PPV) isolates differ by their capsid protein (CP) mobility in SDS-PAGE. These electrophoretic phenotypes are likely to result from post-translational modifications of the CP. We demonstrated that the CP mobility was solely determined by the CP N-terminal region. Sequence comparison pinpointed a possible role of mutations at position 66 in determining the CP phenotype of PPV-Rec isolates. Site-directed mutagenesis of a chimeric clone demonstrated that Gly(66) in the CP resulted in the double-band phenotype, while Arg(66) led to a single-band CP pattern, possibly by preventing the phosphorylation of a nearby Ser residue by steric hindrance.

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Acknowledgments

This work was supported by the grants 2/0027/09 from the Scientific Grant Agency of Ministry of Education and Slovak Academy of Sciences, APVV-51-0402-07 from Slovak Research and Development Agency, and partially by the European Union through the FP7 Small Collaborative Project KBBE-204429 (SHARCO acronym). The authors thank Prof. J.A. García, Prof. L. Palkovics and Dr. M. Navrátil for kindly providing the virus isolates and infectious cDNA. We are also grateful to Prof. J.A. García and Dr. T. Candresse for critical reading of the manuscript and for useful comments.

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Correspondence to Z. W. Šubr.

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Šubr, Z.W., Kamencayová, M., Nováková, S. et al. A single amino acid mutation alters the capsid protein electrophoretic double-band phenotype of the Plum pox virus strain PPV-Rec. Arch Virol 155, 1151–1155 (2010). https://doi.org/10.1007/s00705-010-0677-1

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