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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

Archives of Virology

Authors:

Z. W. S ubr, S. Novakova, A. Nagyova, M. Glasa
Institute of Virology, Slovak Academy of Sciences, Dubravska 9, 84505 Bratislava, Slovakia

M. Kamencayova, J. Nosek
Faculty of Natural Sciences, Commenius University, Mlynska dolina, 84215 Bratislava, Slovakia

Abstract:

Plum pox virus (PPV) isolates differ by their capsid protein (CP) mobility in SDS-PAGE. These electrophoretic phenotypes are likely to result from posttranslational 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.