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Journal of Virology, August 2005, p. 9735-9745, Vol. 79, No. 15
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.15.9735-9745.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Deletion of the Herpes Simplex Virus VP22-Encoding Gene (UL49) Alters the Expression, Localization, and Virion Incorporation of ICP0

Gillian Elliott,* Wali Hafezi,{dagger} Alison Whiteley,{ddagger} and Emmanuelle Bernard

Marie Curie Research Institute, Oxted, Surrey, United Kingdom

Received 7 February 2005/ Accepted 20 April 2005

The role of the herpes simplex virus tegument protein VP22 is not yet known. Here we describe the characterization of a virus in which the entire VP22 open reading frame has been deleted. We show that VP22 is not essential for virus growth but that virus lacking VP22 ({Delta}22) displays a cell-specific replication defect in epithelial MDBK cells. Virus particles assembled in the absence of VP22 show few obvious differences to wild-type (WT) particles, except for a moderate reduction in glycoproteins gD and gB. In addition, the {Delta}22 virus exhibits a general delay in the initiation of virus protein synthesis, but this is not due to a glycoprotein-related defect in virus entry. Intriguingly, however, the absence of VP22 has an obvious effect on the intracellular level of the immediate-early (IE) protein ICP0. Moreover, following translocation from the nucleus to the cytoplasm, ICP0 is unable to localize to the characteristic cytoplasmic sites observed in a WT infection. We demonstrate that, in WT-infected cells, VP22 and ICP0 are concentrated in the same cytoplasmic sites. Furthermore, we show that, while ICP0 and ICP4 are components of WT extracellular virions, the altered localization of ICP0 in the cytoplasm of {Delta}22-infected cells correlates with an absence of both ICP0 and ICP4 from {Delta}22 virions. Hence, while a role has not yet been defined for virion IE proteins in virus infection, our results suggest that their incorporation is a specific event requiring the tegument protein VP22. This report provides the first direct evidence that VP22 influences virus assembly.

* Marie Curie Research Institute, Oxted, Surrey, United Kingdom. Phone: 44 01883 722306. Fax: 44 01883 714375. E-mail: g.elliott{at}mcri.ac.uk.

{dagger} Present address: Institute of Medical Microbiology, University of Muenster, Germany.

{ddagger} Present address: School of Animal and Microbial Sciences, University of Reading, Whiteknights, Reading RG6 6AJ, United Kingdom.

Journal of Virology, August 2005, p. 9735-9745, Vol. 79, No. 15
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.15.9735-9745.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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