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Journal of Virology, October 2005, p. 12185-12198, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12185-12198.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of VP22 in Herpes Simplex Virus-Infected Cells

G. Mouzakitis,1,{dagger} John McLauchlan,2 Cristina Barreca,1 Lisa Kueltzo,1,{ddagger} and P. O'Hare1*

Marie Curie Research Institute, Oxted, United Kingdom,1 MRC Virology Unit, Glasgow, United Kingdom2

Received 11 April 2005/ Accepted 8 July 2005

We examine biochemical characteristics of the herpes simplex virus (HSV) tegument protein VP22 by gel filtration, glycerol sedimentation, and chemical cross-linking experiments and use time course radiolabeling and immunoprecipitation assays to analyze its synthesis and interaction with other infected-cell proteins. VP22 was expressed as a delayed early protein with optimal synthesis requiring DNA replication. In immunoprecipitation assays, VP22 was found in association with several additional proteins including VP16 and a kinase activity likely to be that of UL13. Furthermore, in sizing chromatography experiments, VP22 was present in several higher-order complexes in infected cells. From gel filtration analysis the major form of VP22 migrated with a molecular mass of approximately 160 kDa, consistent with its presence as a tetramer, or a dimer complexed with other proteins, with a fraction of the protein migrating at larger molecular mass. In vitro-synthesized VP22 sedimented in a size range consistent with a mixture of tetramers and dimers. Short N- or C-terminal deletions resulted in migration almost exclusively as dimers, indicating that VP22, in the absence of additional virus-encoded proteins, could form higher-order assemblies, most likely tetramers, but that both N-and C-terminal determinants were required for stabilizing such assemblies. Consistent with this we found that isolated proteins encompassing either the N-terminal or C-terminal region of VP22 sedimented as dimers, and that the purified C-terminal domain could be cross-linked into dimeric structures. These results are discussed with regard to possible virus and host interactions involved in VP22 recruitment into virus particles.

* Corresponding author. Mailing address: MCRI, The Chart, Oxted, Surrey RH8 OTL, United Kingdom. Phone: 44 (0)1883 722306. Fax: 44 (0)1883 714375. E-mail: P.OHare{at}mcri.ac.uk.

{dagger} Present address: Environmental Research Institute, University College Cork, Cork, Ireland.

{ddagger} Present address: University of Colorado, Denver, Colorado.

Journal of Virology, October 2005, p. 12185-12198, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12185-12198.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Blondeau, C., Marc, D., Courvoisier, K., Vautherot, J.-F., Denesvre, C. (2008). Functional Homologies between Avian and Human Alphaherpesvirus VP22 Proteins in Cell-to-Cell Spreading as Revealed by a New cis-Complementation Assay. J. Virol. 82: 9278-9282 [Abstract] [Full Text]  
  • Sciortino, M. T., Taddeo, B., Giuffre-Cuculletto, M., Medici, M. A., Mastino, A., Roizman, B. (2007). Replication-Competent Herpes Simplex Virus 1 Isolates Selected from Cells Transfected with a Bacterial Artificial Chromosome DNA Lacking Only the UL49 Gene Vary with Respect to the Defect in the UL41 Gene Encoding Host Shutoff RNase. J. Virol. 81: 10924-10932 [Abstract] [Full Text]  


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