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Journal of Virology, December 2002, p. 12703-12711, Vol. 76, No. 24
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.24.12703-12711.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Detection of the Potyviral Genome-Linked Protein VPg in Virions and Its Phosphorylation by Host Kinases

Institute of Biotechnology, Viikki Biocenter,¹ Department of Applied Biology, FIN-00014 University of Helsinki, Finland,³ Department of Plant Biology, Genetics Centre, SLU, S-750 07 Uppsala, Sweden²

Received 8 April 2002/ Accepted 18 September 2002

The multifunctional genome-linked protein (VPg) of Potato virus A (PVA; genus Potyvirus) was found to be phosphorylated as a part of the virus particle by a cellular kinase activity from tobacco. Immunoprecipitation, immunolabeling, and immunoelectron microscopy experiments showed that VPg is exposed at one end of the virion and it is accessible to protein-protein interactions. Substitution Ser185Leu at the C-proximal part of VPg reduces accumulation of PVA in inoculated leaves of the wild potato species Solanum commersonii and delays systemic infection, which is not observed in tobacco plants. Our data show that kinases of S. commersonii differentially recognize the VPg containing Ser or Leu at position 185, whereas both forms of VPg are similarly recognized by tobacco kinases. Taken together, our data imply that the virion-bound VPg may interact with host proteins and that phosphorylation of VPg may play a role in the VPg-mediated functions during the infection cycle of potyviruses.

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