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

doi:10.1080/21505594.2020.1806664

HFCAS OpenIR

	Mycoplasma hyopneumoniaeevades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu)
	Yu, Yanfei 1,2; Wang, Jia 1,3; Han, Rui 1,4; Wang, Li 1; Zhang, Lei1 ; Zhang, Amy Yimin 5; Xin, Jiuqing 6; Li, Shaoli 7; Zeng, Yanhua 8; Shao, Guoqing 1,2; Feng, Zhixin 1; Xiong, Qiyan 1,9
	2020
发表期刊	VIRULENCE
ISSN	2150-5594
通讯作者	Feng, Zhixin(fzxjaas@163.com) ; Xiong, Qiyan(qiyanxiongnj@163.com)
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.
关键词	Mycoplasma elongation factor Tu complement factor H complement activation bacterial adhesion
DOI	10.1080/21505594.2020.1806664
关键词[WOS]	NONTYPABLE HAEMOPHILUS-INFLUENZAE ; MEMBRANE PROTEIN P5 ; SURFACE PROTEIN ; STREPTOCOCCUS-SUIS ; SERUM RESISTANCE ; CONTRIBUTES ; PIGS ; AMPLIFICATION ; FIBRONECTIN ; PERSISTENCE
收录类别	SCI
语种	英语
资助项目	National Natural Science Foundation of China[31700158] ; National Natural Science Foundation of China[31770193]
项目资助者	National Natural Science Foundation of China
WOS研究方向	Immunology ; Infectious Diseases ; Microbiology
WOS类目	Immunology ; Infectious Diseases ; Microbiology
WOS记录号	WOS:000561128300001
出版者	TAYLOR & FRANCIS INC
引用统计	被引频次：25[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	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.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
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).