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Journal of Virology, May 2009, p. 5204-5218, Vol. 83, No. 10
0022-538X/09/$08.00+0     doi:10.1128/JVI.00069-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway{triangledown}

Julianna Stylianou,1,{dagger} Kevin Maringer,1,{dagger} Rachelle Cook,2 Emmanuelle Bernard,2 and Gillian Elliott1,2*

Department of Virology, Faculty of Medicine, Imperial College London, London, United Kingdom,1 Marie Curie Research Institute, Oxted, Surrey, United Kingdom2

Received 12 January 2009/ Accepted 26 February 2009

The mechanism by which herpesviruses acquire their tegument is not yet clear. One model is that outer tegument proteins are recruited by the cytoplasmic tails of viral glycoproteins. In the case of herpes simplex virus tegument protein VP22, interactions with the glycoproteins gE and gD have been shown. We have previously shown that the C-terminal half of VP22 contains the necessary signal for assembly into the virus. Here, we show that during infection VP22 interacts with gE and gM, as well as its tegument partner VP16. However, by using a range of techniques we were unable to demonstrate VP22 binding to gD. By using pulldown assays, we show that while the cytoplasmic tails of both gE and gM interact with VP22, only gE interacts efficiently with the C-terminal packaging domain of VP22. Furthermore, gE but not gM can recruit VP22 to the Golgi/trans-Golgi network region of the cell in the absence of other virus proteins. To examine the role of the gE-VP22 interaction in infection, we constructed a recombinant virus expressing a mutant VP22 protein with a 14-residue deletion that is unable to bind gE ({Delta}gEbind). Coimmunoprecipitation assays confirmed that this variant of VP22 was unable to complex with gE. Moreover, VP22 was no longer recruited to its characteristic cytoplasmic trafficking complexes but exhibited a diffuse localization. Importantly, packaging of this variant into virions was abrogated. The mutant virus exhibited poor growth in epithelial cells, similar to the defect we have observed for a VP22 knockout virus. These results suggest that deletion of just 14 residues from the VP22 protein is sufficient to inhibit binding to gE and hence recruitment to the viral envelope and assembly into the virus, resulting in a growth phenotype equivalent to that produced by deleting the entire reading frame.

* Corresponding author. Mailing address: Department of Virology, Faculty of Medicine, Imperial College London, London, United Kingdom. Phone: 44 0207 594 5037. Fax: 44 0207 594 3973. E-mail: g.elliott{at}imperial.ac.uk

{triangledown} Published ahead of print on 11 March 2009.

{dagger} Both authors contributed equally to this work.

Journal of Virology, May 2009, p. 5204-5218, Vol. 83, No. 10
0022-538X/09/$08.00+0     doi:10.1128/JVI.00069-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhang, J., Nagel, C.-H., Sodeik, B., Lippe, R. (2009). Early, Active, and Specific Localization of Herpes Simplex Virus Type 1 gM to Nuclear Membranes. J. Virol. 83: 12984-12997 [Abstract] [Full Text]  


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