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

文献类型：期刊论文

作者Yu, Yanfei2,3; Wang, Jia2,4; Han, Rui2,5; Wang, Li2; Zhang, Lei2; Zhang, Amy Yimin6; Xin, Jiuqing7; Li, Shaoli8; Zeng, Yanhua1; Shao, Guoqing2,3
刊名VIRULENCE
出版日期2020
卷号11
关键词Mycoplasma elongation factor Tu complement factor H complement activation bacterial adhesion
ISSN号2150-5594
DOI10.1080/21505594.2020.1806664
通讯作者Feng, Zhixin(fzxjaas@163.com) ; Xiong, Qiyan(qiyanxiongnj@163.com)
英文摘要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.
WOS关键词NONTYPABLE HAEMOPHILUS-INFLUENZAE ; MEMBRANE PROTEIN P5 ; SURFACE PROTEIN ; STREPTOCOCCUS-SUIS ; SERUM RESISTANCE ; CONTRIBUTES ; PIGS ; AMPLIFICATION ; FIBRONECTIN ; PERSISTENCE
资助项目National Natural Science Foundation of China[31700158] ; National Natural Science Foundation of China[31770193]
WOS研究方向Immunology ; Infectious Diseases ; Microbiology
语种英语
WOS记录号WOS:000561128300001
出版者TAYLOR & FRANCIS INC
资助机构National Natural Science Foundation of China
源URL[http://ir.hfcas.ac.cn:8080/handle/334002/70623]  
专题中国科学院合肥物质科学研究院
通讯作者Feng, Zhixin; Xiong, Qiyan
作者单位1.Univ South China, Hengyang Med Coll, Inst Pathogen Biol, Hengyang, Peoples R China
2.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
3.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang, Jiangsu, Peoples R China
4.Univ KwaZulu Natal, Coll Agr Engn & Sci, Durban, South Africa
5.Chinese Acad Sci, High Magnet Field Lab, Hefei, Peoples R China
6.Cornell Univ, Coll Vet Med, Cornell, NY USA
7.Chinese Acad Agr Sci, Harbin Vet Res Inst, Harbin, Peoples R China
8.Capital Inst Pediat, Dept Bacteriol, Beijing, Peoples R China
9.Jiangsu Univ, Inst Life Sci, Zhenjiang, Jiangsu, Peoples R China
推荐引用方式
GB/T 7714		 Yu, Yanfei,Wang, Jia,Han, Rui,et al. Mycoplasma hyopneumoniaeevades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)[J]. VIRULENCE,2020,11.
APA Yu, Yanfei.,Wang, Jia.,Han, Rui.,Wang, Li.,Zhang, Lei.,...&Xiong, Qiyan.(2020).Mycoplasma hyopneumoniaeevades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu).VIRULENCE,11.
MLA Yu, Yanfei,et al."Mycoplasma hyopneumoniaeevades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)".VIRULENCE 11(2020).

入库方式： OAI收割

来源：合肥物质科学研究院

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