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Journal of Virology, November 2005, p. 14057-14068, Vol. 79, No. 22
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.22.14057-14068.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Phosphorylation of the Herpes Simplex Virus Tegument Protein VP22 Has No Effect on Incorporation of VP22 into the Virus but Is Involved in Optimal Expression and Virion Packaging of ICP0

Corinne Potel and Gillian Elliott*

Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey, United Kingdom

Received 20 April 2005/ Accepted 15 August 2005

Herpes simplex virus VP22 is a major tegument protein of unknown function. Very recently, we reported that the predominant effect of deleting the VP22 gene was on the expression, localization, and virion incorporation of ICP0. In addition, the {Delta}22 virus replicated poorly in epithelial MDBK cells. We have also previously shown that VP22 interacts with the tegument protein VP16 and the cellular microtubule network. While the majority of VP22 in infected cells is highly phosphorylated, the nonphosphorylated form of VP22 is the predominant species in the virion, suggesting a differential requirement for phosphorylation through virus replication. Hence, to study the significance of VP22 phosphorylation, we have now constructed two recombinant viruses expressing green fluorescent protein-VP22 (G22) in which the previously identified serine phosphorylation sites have been mutated either to alanine to abolish the phosphorylation status of VP22 (G22P–) or to glutamic acid to mimic permanent phosphorylation (G22P+). Localization studies indicated that the G22P– protein associated tightly with microtubules in some infected cells, suggesting that VP22 phosphorylation may control its interaction with the microtubule network. By contrast, VP22 phosphorylation had no effect on its ability to interact with VP16 and, importantly, had no effect on the relative packaging of VP22. Intriguingly, virion packaging of ICP0 was reduced in the G22P+ virus while ICP0 expression was reduced in the G22P– virus, suggesting that these two ICP0 defects, previously observed in the {Delta}22 virus, were attributable to different forms of VP22. Furthermore, the {Delta}22 virus replication defect in MDBK cells correlated with the expression of constitutively charged VP22 in the G22P+ virus. Taken together, these results suggest an important role for VP22 phosphorylation in its relationship with ICP0.

* Corresponding author. Mailing address: Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom. Phone: 44 01883 722306. Fax: 44 01883 714375. E-mail: g.elliott{at}mcri.ac.uk.

Journal of Virology, November 2005, p. 14057-14068, Vol. 79, No. 22
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.22.14057-14068.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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