Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)

Mycoplasmas persist in the host for a long time, suggesting that they possess mechanisms for immune evasion. Factor H is a negative regulator of the complement system, which binds to host cells to avoid unexpected complement activation. In this study, we revealed that many mycoplasmas, such as Mycop...

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Autores principales:	Yanfei Yu, Jia Wang, Rui Han, Li Wang, Lei Zhang, Amy Yimin Zhang, Jiuqing Xin, Shaoli Li, Yanhua Zeng, Guoqing Shao, Zhixin Feng, Qiyan Xiong
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2020
Materias:	mycoplasma elongation factor tu complement factor h complement activation bacterial adhesion Infectious and parasitic diseases RC109-216
Acceso en línea:	https://doaj.org/article/a582909c29cf4f82a841051927acf0d9
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spelling	oai:doaj.org-article:a582909c29cf4f82a841051927acf0d92021-11-17T14:21:58ZMycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)2150-55942150-560810.1080/21505594.2020.1806664https://doaj.org/article/a582909c29cf4f82a841051927acf0d92020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1806664https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608Mycoplasmas persist in the host for a long time, suggesting that they possess mechanisms for immune evasion. Factor H is a negative regulator of the complement system, which binds to host cells to avoid unexpected complement activation. In this study, we revealed that many mycoplasmas, such as Mycoplasma hyopneumoniae, Mycoplasma hyorhinis, Mycoplasma hyosynoviae, Mycoplasma gallisepticum, Mycoplasma pneumoniae, Mycoplasma genitalium, Mycoplasma flocculare, and Mycoplasma bovis could hijack factor H such that they present themselves as a host tissue and thus escape from complement attack. Furthermore, the mechanism of recruiting factor H was identified in M. hyopneumoniae. M. hyopneumoniae binds factor H via factor H binding proteins, such as elongation factor thermo unstable (EF-Tu), P146, pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha (PdhA), P46, Pyruvate dehydrogenase E1 component subunit beta (PdhB), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and three different hypothetical proteins. The binding of factor H by EF-Tu further contributes to decreased C3 deposition on the M. hyopneumoniae surface and ultimately blocks further complement activation. In fact, binding of factor H occurs in a multifactorial manner; factor H is not only exploited by M. hyopneumoniae via its regulator activity to help mycoplasmas escape from complement killing, but also increases M. hyopneumoniae adhesion to swine tracheal epithelial cells, partially through EF-Tu. Meanwhile, the high sequence identity among EF-Tu proteins in the above-mentioned mycoplasmas implied the universality of the mechanism. This is the first report that mycoplasmas can escape complement killing by binding to factor H.Yanfei YuJia WangRui HanLi WangLei ZhangAmy Yimin ZhangJiuqing XinShaoli LiYanhua ZengGuoqing ShaoZhixin FengQiyan XiongTaylor & Francis Grouparticlemycoplasmaelongation factor tucomplement factor hcomplement activationbacterial adhesionInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 1059-1074 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	mycoplasma elongation factor tu complement factor h complement activation bacterial adhesion Infectious and parasitic diseases RC109-216
spellingShingle	mycoplasma elongation factor tu complement factor h complement activation bacterial adhesion Infectious and parasitic diseases RC109-216 Yanfei Yu Jia Wang Rui Han Li Wang Lei Zhang Amy Yimin Zhang Jiuqing Xin Shaoli Li Yanhua Zeng Guoqing Shao Zhixin Feng Qiyan Xiong Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
description	Mycoplasmas persist in the host for a long time, suggesting that they possess mechanisms for immune evasion. Factor H is a negative regulator of the complement system, which binds to host cells to avoid unexpected complement activation. In this study, we revealed that many mycoplasmas, such as Mycoplasma hyopneumoniae, Mycoplasma hyorhinis, Mycoplasma hyosynoviae, Mycoplasma gallisepticum, Mycoplasma pneumoniae, Mycoplasma genitalium, Mycoplasma flocculare, and Mycoplasma bovis could hijack factor H such that they present themselves as a host tissue and thus escape from complement attack. Furthermore, the mechanism of recruiting factor H was identified in M. hyopneumoniae. M. hyopneumoniae binds factor H via factor H binding proteins, such as elongation factor thermo unstable (EF-Tu), P146, pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha (PdhA), P46, Pyruvate dehydrogenase E1 component subunit beta (PdhB), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and three different hypothetical proteins. The binding of factor H by EF-Tu further contributes to decreased C3 deposition on the M. hyopneumoniae surface and ultimately blocks further complement activation. In fact, binding of factor H occurs in a multifactorial manner; factor H is not only exploited by M. hyopneumoniae via its regulator activity to help mycoplasmas escape from complement killing, but also increases M. hyopneumoniae adhesion to swine tracheal epithelial cells, partially through EF-Tu. Meanwhile, the high sequence identity among EF-Tu proteins in the above-mentioned mycoplasmas implied the universality of the mechanism. This is the first report that mycoplasmas can escape complement killing by binding to factor H.
format	article
author	Yanfei Yu Jia Wang Rui Han Li Wang Lei Zhang Amy Yimin Zhang Jiuqing Xin Shaoli Li Yanhua Zeng Guoqing Shao Zhixin Feng Qiyan Xiong
author_facet	Yanfei Yu Jia Wang Rui Han Li Wang Lei Zhang Amy Yimin Zhang Jiuqing Xin Shaoli Li Yanhua Zeng Guoqing Shao Zhixin Feng Qiyan Xiong
author_sort	Yanfei Yu
title	Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
title_short	Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
title_full	Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
title_fullStr	Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
title_full_unstemmed	Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
title_sort	mycoplasma hyopneumoniae evades complement activation by binding to factor h via elongation factor thermo unstable (ef-tu)
publisher	Taylor & Francis Group
publishDate	2020
url	https://doaj.org/article/a582909c29cf4f82a841051927acf0d9
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Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)

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