A single amino acid mutation alters the capsid protein electrophoretic double-band phenotype of the Plum pox virus strain PPV-Rec.
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.
Subr
Z W
ZW
Institute of Virology, Slovak Academy of Sciences, 84505 Bratislava, Slovakia. virusubr@savba.sk
Kamencayová
M
M
Nováková
S
S
Nagyová
A
A
Nosek
J
J
Glasa
M
M
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D036022:Capsid Proteins / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary; D004279:DNA, Viral / Q000235:genetics; D004586:Electrophoresis; D016679:Genome, Viral; D008969:Molecular Sequence Data; D009154:Mutation; D010641:Phenotype; D017801:Plum Pox Virus / Q000145:classification / Q000235:genetics* / Q000378:metabolism
D036022:Capsid Proteins; D018076:DNA, Complementary; D004279:DNA, Viral