TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4

TcpC is a well characterised multifunctional virulence factor expressed by uropathogenic Eschericia coli. Here the authors show that TcpC also targets neutrophil NETosis via its E3 ligase functionality promoting the degradation of PAD4, and represents an additional immune evasion function of this ba...

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Autores principales:	Qian Ou, Jia-qi Fang, Zhe-sheng Zhang, Zhe Chi, Jie Fang, Di-yan Xu, Kai-zhong Lu, Meng-qing Qian, Da-yong Zhang, Jun-ping Guo, Wei Gao, Na-ru Zhang, Jian-ping Pan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c5d2af311ed14389a1ad2c707549eaa0
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spelling	oai:doaj.org-article:c5d2af311ed14389a1ad2c707549eaa02021-12-02T17:52:38ZTcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 410.1038/s41467-021-23881-82041-1723https://doaj.org/article/c5d2af311ed14389a1ad2c707549eaa02021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23881-8https://doaj.org/toc/2041-1723TcpC is a well characterised multifunctional virulence factor expressed by uropathogenic Eschericia coli. Here the authors show that TcpC also targets neutrophil NETosis via its E3 ligase functionality promoting the degradation of PAD4, and represents an additional immune evasion function of this bacterially derived virulence factor.Qian OuJia-qi FangZhe-sheng ZhangZhe ChiJie FangDi-yan XuKai-zhong LuMeng-qing QianDa-yong ZhangJun-ping GuoWei GaoNa-ru ZhangJian-ping PanNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Qian Ou Jia-qi Fang Zhe-sheng Zhang Zhe Chi Jie Fang Di-yan Xu Kai-zhong Lu Meng-qing Qian Da-yong Zhang Jun-ping Guo Wei Gao Na-ru Zhang Jian-ping Pan TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
description	TcpC is a well characterised multifunctional virulence factor expressed by uropathogenic Eschericia coli. Here the authors show that TcpC also targets neutrophil NETosis via its E3 ligase functionality promoting the degradation of PAD4, and represents an additional immune evasion function of this bacterially derived virulence factor.
format	article
author	Qian Ou Jia-qi Fang Zhe-sheng Zhang Zhe Chi Jie Fang Di-yan Xu Kai-zhong Lu Meng-qing Qian Da-yong Zhang Jun-ping Guo Wei Gao Na-ru Zhang Jian-ping Pan
author_facet	Qian Ou Jia-qi Fang Zhe-sheng Zhang Zhe Chi Jie Fang Di-yan Xu Kai-zhong Lu Meng-qing Qian Da-yong Zhang Jun-ping Guo Wei Gao Na-ru Zhang Jian-ping Pan
author_sort	Qian Ou
title	TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
title_short	TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
title_full	TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
title_fullStr	TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
title_full_unstemmed	TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
title_sort	tcpc inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c5d2af311ed14389a1ad2c707549eaa0
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TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4

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