Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

J Virol

Publication Date

07/1999

Volume

73

Pages

6203 - 6206

Keywords

Animals, Binding Sites, COS Cells, Casein Kinase II, Humans, Phosphorylation, Protein-Serine-Threonine Kinases, Viral Structural Proteins