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

文献类型： 外文期刊

作者： Yu, Yanfei 1 ; Wang, Jia 1 ; Han, Rui 1 ; Wang, Li 1 ; Zhang, Lei 1 ; Zhang, Amy Yimin 5 ; Xin, Jiuqing 6 ; Li, Shaoli 7 ; Z 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Natl Ctr Engn Res Vet Bioprod, Inst Vet Med, Key Lab Vet Biol Engn & Technol,Minist Agr, Nanjing, Peoples R China

2.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang, Jiangsu, Peoples R China

3.Univ KwaZulu Natal, Coll Agr Engn & Sci, Durban, South Africa

4.Chinese Acad Sci, High Magnet Field Lab, Hefei, Peoples R China

5.Cornell Univ, Coll Vet Med, Cornell, NY USA

6.Chinese Acad Agr Sci, Harbin Vet Res Inst, Harbin, Peoples R China

7.Capital Inst Pediat, Dept Bacteriol, Beijing, Peoples R China

8.Univ South China, Hengyang Med Coll, Inst Pathogen Biol, Hengyang, Peoples R China

9.Jiangsu Univ, Inst Life Sci, Zhenjiang, Jiangsu, Peoples R China

关键词： Mycoplasma; elongation factor Tu; complement factor H; complement activation; bacterial adhesion

期刊名称：VIRULENCE （ 影响因子：5.882； 五年影响因子：6.489 ）

ISSN： 2150-5594

年卷期： 2020 年 11 卷 1 期

页码：

收录情况： SCI

摘要： 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 asMycoplasma hyopneumoniae, Mycoplasma hyorhinis, Mycoplasma hyosynoviae, Mycoplasma gallisepticum, Mycoplasma pneumoniae, Mycoplasma genitalium, Mycoplasma flocculare, andMycoplasma boviscould 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 inM. hyopneumoniae. M. hyopneumoniaebinds 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 theM. hyopneumoniaesurface and ultimately blocks further complement activation. In fact, binding of factor H occurs in a multifactorial manner; factor H is not only exploited byM. hyopneumoniaevia its regulator activity to help mycoplasmas escape from complement killing, but also increasesM. hyopneumoniaeadhesion 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.

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