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Journal of Virology, July 1999, p. 6203-6206, Vol. 73, No. 7
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification of Phosphorylation Sites within the Herpes Simplex Virus Tegument Protein VP22

Gillian Elliott,1,* Dawn O'Reilly,2 and Peter O'Hare2

Virus Assembly Group1 and Herpesvirus Group,2 Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom

Received 8 February 1999/Accepted 19 March 1999

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.

* Corresponding author. Mailing address: Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH1 OTL, United Kingdom. Phone: 44 01883 722306. Fax: 44 01883 714375. E-mail: g.elliott{at}mcri.ac.uk.

Journal of Virology, July 1999, p. 6203-6206, Vol. 73, No. 7
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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