title: Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.
abstract: 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.
authors.affiliation: Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom. g.elliott@mcri.ac.uk
authors.forename: G
authors.initials: G
authors.lastname: Elliott
authors.forename: D
authors.initials: D
authors.lastname: O'Reilly
authors.forename: P
authors.initials: P
authors.lastname: O'Hare
mesh_terms: 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*
chemical_list: D015678:Viral Structural Proteins; C073413:herpes simplex virus type 1 protein VP22; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases