Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.

Journal article

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: Elliott, G; O'Reilly, D; O'Hare, P

• Publication status: Published
• Journal: Journal of virology
• Volume: 73
• Issue: 7
• Pages: 6203-6206
• Publication date: 1999-07-01
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Viral Structural Proteins; Binding Sites; COS Cells; Phosphorylation; Animals; Casein Kinase II; Protein-Serine-Threonine Kinases; Humans