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

Stylianou, J, Maringer, K, Cook, R, Bernard, E and Elliott, G (2009) Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway Journal of Virology, 83 (10). pp. 5204-5218.

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Abstract

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 ( 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.

Item Type: Article
Subjects : Biosciences
Divisions : Faculty of Health and Medical Sciences > School of Biosciences and Medicine
Authors :
AuthorsEmailORCID
Stylianou, JUNSPECIFIEDUNSPECIFIED
Maringer, KUNSPECIFIEDUNSPECIFIED
Cook, RUNSPECIFIEDUNSPECIFIED
Bernard, EUNSPECIFIEDUNSPECIFIED
Elliott, GUNSPECIFIEDUNSPECIFIED
Date : 15 May 2009
Funders : Medical Research Council (MRC)
Identification Number : https://doi.org/10.1128/JVI.00069-09
Copyright Disclaimer : Copyright © 2009, American Society for Microbiology. All Rights Reserved.
Uncontrolled Keywords : Science & Technology, Life Sciences & Biomedicine, Virology, VIROLOGY, TRANS-GOLGI NETWORK, C-TERMINAL DOMAIN, IN-VITRO, PSEUDORABIES VIRUS, CYTOPLASMIC TAIL, SECONDARY ENVELOPMENT, VIRAL-PROTEINS, NULL MUTATION, GENE-PRODUCT, UL36 GENE
Depositing User : Symplectic Elements
Date Deposited : 22 Feb 2017 15:18
Last Modified : 22 Feb 2017 16:28
URI: http://epubs.surrey.ac.uk/id/eprint/813605

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