Electrophoretic mobility of the capsid protein of the Plum pox virus strain PPV-Rec indicates its partial phosphorylation.
A double-band SDS-PAGE profile was found reproducible for capsid protein (CP) of Plum pox virus (PPV) isolates belonging to the strain PPV-Rec. The double-band was also present in the virus population multiplied in various plants. A single-lesion passage in a hypersensitive host Chenopodium foetidum showed that its presence was not a result of a mixed infection. We found that the two electrophoretic forms of CP shared identical N-terminus. Therefore, they did not originate from an alternative proteolytic processing, but were different in their posttranslational modification. The slower band of CP could be converted to the faster one by the phosphatase treatment. We assumed that CP protein was present in both phosphorylated and dephosphorylated forms in the infected plants.
Subr
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Z
Institute of Virology, Slovak Academy of Sciences, 84505 Bratislava, Slovak Republic. virusubr@savba.sk
Ryslava
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H
Kollerova
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D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism*; D027462:Chenopodium / Q000821:virology; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010935:Plant Diseases / Q000821:virology; D017801:Plum Pox Virus / Q000145:classification / Q000378:metabolism* / Q000472:pathogenicity*; D014026:Nicotiana / Q000821:virology
D036022:Capsid Proteins