Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.
The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22.
Elliott
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Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom. g.elliott@mcri.ac.uk
O'Reilly
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O'Hare
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D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D047390:Casein Kinase II; D006801:Humans; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism*
D015678:Viral Structural Proteins; C073413:herpes simplex virus type 1 protein VP22; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases