TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.

Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3-6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation o...

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Autores principales:	Suyan Wang, Mengmeng Yu, Aijing Liu, Yuanling Bao, Xiaole Qi, Li Gao, Yuntong Chen, Peng Liu, Yulong Wang, Lixiao Xing, Lingzhai Meng, Yu Zhang, Linjin Fan, Xinyi Li, Qing Pan, Yanping Zhang, Hongyu Cui, Kai Li, Changjun Liu, Xijun He, Yulong Gao, Xiaomei Wang
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/df7c88b8cc8b4e7db27ac373df6cbab6
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spelling	oai:doaj.org-article:df7c88b8cc8b4e7db27ac373df6cbab62021-12-02T20:00:11ZTRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.1553-73661553-737410.1371/journal.ppat.1009900https://doaj.org/article/df7c88b8cc8b4e7db27ac373df6cbab62021-09-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009900https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3-6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV in vitro and in vivo. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.Suyan WangMengmeng YuAijing LiuYuanling BaoXiaole QiLi GaoYuntong ChenPeng LiuYulong WangLixiao XingLingzhai MengYu ZhangLinjin FanXinyi LiQing PanYanping ZhangHongyu CuiKai LiChangjun LiuXijun HeYulong GaoXiaomei WangPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 9, p e1009900 (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 Suyan Wang Mengmeng Yu Aijing Liu Yuanling Bao Xiaole Qi Li Gao Yuntong Chen Peng Liu Yulong Wang Lixiao Xing Lingzhai Meng Yu Zhang Linjin Fan Xinyi Li Qing Pan Yanping Zhang Hongyu Cui Kai Li Changjun Liu Xijun He Yulong Gao Xiaomei Wang TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
description	Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3-6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV in vitro and in vivo. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.
format	article
author	Suyan Wang Mengmeng Yu Aijing Liu Yuanling Bao Xiaole Qi Li Gao Yuntong Chen Peng Liu Yulong Wang Lixiao Xing Lingzhai Meng Yu Zhang Linjin Fan Xinyi Li Qing Pan Yanping Zhang Hongyu Cui Kai Li Changjun Liu Xijun He Yulong Gao Xiaomei Wang
author_facet	Suyan Wang Mengmeng Yu Aijing Liu Yuanling Bao Xiaole Qi Li Gao Yuntong Chen Peng Liu Yulong Wang Lixiao Xing Lingzhai Meng Yu Zhang Linjin Fan Xinyi Li Qing Pan Yanping Zhang Hongyu Cui Kai Li Changjun Liu Xijun He Yulong Gao Xiaomei Wang
author_sort	Suyan Wang
title	TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
title_short	TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
title_full	TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
title_fullStr	TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
title_full_unstemmed	TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
title_sort	trim25 inhibits infectious bursal disease virus replication by targeting vp3 for ubiquitination and degradation.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/df7c88b8cc8b4e7db27ac373df6cbab6
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TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.

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