Collados Rodríguez, M. , Dybas, J. M., Hughes, J. , Weitzman, M. D. and Boutell, C. (2020) The HSV-1 ubiquitin ligase ICP0: modifying the cellular proteome to promote infection. Virus Research, 285, 198015. (doi: 10.1016/j.virusres.2020.198015) (PMID:32416261)
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Abstract
Herpes simplex virus 1 (HSV-1) hijacks ubiquitination machinery to modify the cellular proteome to create an environment permissive for virus replication. HSV-1 encodes its own RING-finger E3 ubiquitin (Ub) ligase, Infected Cell Protein 0 (ICP0), that directly interfaces with component proteins of the Ub pathway to inactivate host immune defences and cellular processes that restrict the progression of HSV-1 infection. Consequently, ICP0 plays a critical role in the infectious cycle of HSV-1 that is required to promote the efficient onset of lytic infection and productive reactivation of viral genomes from latency. This review will describe the current knowledge regarding the biochemical properties and known substrates of ICP0 during HSV-1 infection. We will highlight the gaps in the characterization of ICP0 function and propose future areas of research required to understand fully the biological properties of this important HSV-1 regulatory protein.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Hughes, Dr Joseph and Boutell, Dr Chris and Collados Rodriguez, Dr Milagros |
Authors: | Collados Rodríguez, M., Dybas, J. M., Hughes, J., Weitzman, M. D., and Boutell, C. |
College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research |
Journal Name: | Virus Research |
Publisher: | Elsevier |
ISSN: | 0168-1702 |
ISSN (Online): | 1872-7492 |
Published Online: | 13 May 2020 |
Copyright Holders: | Copyright © 2020 The Authors |
First Published: | First published in Virus Research 285:198015 |
Publisher Policy: | Reproduced under a Creative Commons License |
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