pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.

The herpes simplex virus (HSV)-1 protein pUL21 is essential for efficient virus replication and dissemination. While pUL21 has been shown to promote multiple steps of virus assembly and spread, the molecular basis of its function remained unclear. Here we identify that pUL21 is a virus-encoded adapt...

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Autores principales:	Tomasz H Benedyk, Julia Muenzner, Viv Connor, Yue Han, Katherine Brown, Kaveesha J Wijesinghe, Yunhui Zhuang, Susanna Colaco, Guido A Stoll, Owen S Tutt, Stanislava Svobodova, Dmitri I Svergun, Neil A Bryant, Janet E Deane, Andrew E Firth, Cy M Jeffries, Colin M Crump, Stephen C Graham
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/9b5aa75bb49e4f8c89bf26a7c76fbb8a
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spelling	oai:doaj.org-article:9b5aa75bb49e4f8c89bf26a7c76fbb8a2021-12-02T20:00:24ZpUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.1553-73661553-737410.1371/journal.ppat.1009824https://doaj.org/article/9b5aa75bb49e4f8c89bf26a7c76fbb8a2021-08-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009824https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The herpes simplex virus (HSV)-1 protein pUL21 is essential for efficient virus replication and dissemination. While pUL21 has been shown to promote multiple steps of virus assembly and spread, the molecular basis of its function remained unclear. Here we identify that pUL21 is a virus-encoded adaptor of protein phosphatase 1 (PP1). pUL21 directs the dephosphorylation of cellular and virus proteins, including components of the viral nuclear egress complex, and we define a conserved non-canonical linear motif in pUL21 that is essential for PP1 recruitment. In vitro evolution experiments reveal that pUL21 antagonises the activity of the virus-encoded kinase pUS3, with growth and spread of pUL21 PP1-binding mutant viruses being restored in adapted strains where pUS3 activity is disrupted. This study shows that virus-directed phosphatase activity is essential for efficient herpesvirus assembly and spread, highlighting the fine balance between kinase and phosphatase activity required for optimal virus replication.Tomasz H BenedykJulia MuenznerViv ConnorYue HanKatherine BrownKaveesha J WijesingheYunhui ZhuangSusanna ColacoGuido A StollOwen S TuttStanislava SvobodovaDmitri I SvergunNeil A BryantJanet E DeaneAndrew E FirthCy M JeffriesColin M CrumpStephen C GrahamPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 8, p e1009824 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Tomasz H Benedyk Julia Muenzner Viv Connor Yue Han Katherine Brown Kaveesha J Wijesinghe Yunhui Zhuang Susanna Colaco Guido A Stoll Owen S Tutt Stanislava Svobodova Dmitri I Svergun Neil A Bryant Janet E Deane Andrew E Firth Cy M Jeffries Colin M Crump Stephen C Graham pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
description	The herpes simplex virus (HSV)-1 protein pUL21 is essential for efficient virus replication and dissemination. While pUL21 has been shown to promote multiple steps of virus assembly and spread, the molecular basis of its function remained unclear. Here we identify that pUL21 is a virus-encoded adaptor of protein phosphatase 1 (PP1). pUL21 directs the dephosphorylation of cellular and virus proteins, including components of the viral nuclear egress complex, and we define a conserved non-canonical linear motif in pUL21 that is essential for PP1 recruitment. In vitro evolution experiments reveal that pUL21 antagonises the activity of the virus-encoded kinase pUS3, with growth and spread of pUL21 PP1-binding mutant viruses being restored in adapted strains where pUS3 activity is disrupted. This study shows that virus-directed phosphatase activity is essential for efficient herpesvirus assembly and spread, highlighting the fine balance between kinase and phosphatase activity required for optimal virus replication.
format	article
author	Tomasz H Benedyk Julia Muenzner Viv Connor Yue Han Katherine Brown Kaveesha J Wijesinghe Yunhui Zhuang Susanna Colaco Guido A Stoll Owen S Tutt Stanislava Svobodova Dmitri I Svergun Neil A Bryant Janet E Deane Andrew E Firth Cy M Jeffries Colin M Crump Stephen C Graham
author_facet	Tomasz H Benedyk Julia Muenzner Viv Connor Yue Han Katherine Brown Kaveesha J Wijesinghe Yunhui Zhuang Susanna Colaco Guido A Stoll Owen S Tutt Stanislava Svobodova Dmitri I Svergun Neil A Bryant Janet E Deane Andrew E Firth Cy M Jeffries Colin M Crump Stephen C Graham
author_sort	Tomasz H Benedyk
title	pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
title_short	pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
title_full	pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
title_fullStr	pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
title_full_unstemmed	pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
title_sort	pul21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/9b5aa75bb49e4f8c89bf26a7c76fbb8a
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pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.

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