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Mycoplasma synoviae surface-located elongation factor G functions as a cytoadhesin to promote adhesion to synovial sheath cells through binding to vimentin

文献类型： 外文期刊

作者： Xu, Bin 1 ; Sun, Yu 3 ; Wang, Shu 1 ; Yao, Weiping 1 ; Wang, Qing 5 ; Yuan, Ting 1 ; Ma, Sunting 1 ; Wang, Xiaoli 1 ; Lyu, Lixin 1 ; Yu, Yanfei 1 ; Zhang, Xiaofei 1 ; Shao, Guoqing 1 ; Ouyang, Wei 1 ; Xiong, Qiyan 1 ; Feng, Zhixin 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Minist Sci & Technol,State Key Lab Cultivat Base, Inst Vet Med,Key Lab Vet Biol Engn & Technol,Minis, Natl Res Ctr Vet Biol Engn & Technol,Jiangsu Key L, Nanjing 210014, Peoples R China

2.GuoTai Taizhou Ctr Technol Innovat Vet Biol, Taizhou 225300, Peoples R China

3.Nanjing Agr Univ, Coll Vet Med, Nanjing 210095, Peoples R China

4.Jiangsu Univ, Sch Life Sci, Zhenjiang 212013, Jiangsu, Peoples R China

5.Anhui Agr Univ, Coll Anim Sci & Technol, Hefei 230036, Peoples R China

6.Jiangsu Univ, Sch Med, Zhenjiang 212013, Peoples R China

关键词： Mycoplasma synoviae; Elongation factor G; Synovial sheath cells; Vimentin; Adhesion

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：2.7； 五年影响因子：2.9 ）

ISSN： 0378-1135

年卷期： 2024 年 298 卷

页码：

收录情况： SCI

摘要： Mycoplasma synoviae infection has caused serious economic losses to the poultry industry worldwide. The molecular mechanism by which M. synoviae colonizes the synovium and induces synovitis is unclear. In this study, desthiobiotin pull-down and liquid chromatography-tandem mass spectrometry analyses were used to screen M. synoviae membrane proteins that bind the membrane proteins of synovial sheath cells (SSCs). Among the 128 screened proteins, elongation factor G (EF-G) of M. synoviae was identified as a surface-located protein using colony blotting and dual fluorescence analyses. The immunogenicity of EF-G was confirmed by the preparation of a rabbit polyclonal antibody. EF-G was identified as a cytoadhesin that directly binds to SSCs using indirect immunofluorescence assay and ELISA plate binding assay. In addition, antibody adhesion inhibition and protein adhesion inhibition demonstrated that EF-G could significantly promote the adhesion of M. synoviae to SSCs. CoIP, GST pull-down, bacterial two-hybridization, and ELISA plate binding assays were performed to demonstrate the binding of EF-G and vimentin in vivo and in vitro. Antibody adhesion inhibition, protein adhesion inhibition, and siRNA interference adhesion inhibition assays demonstrated that vimentin significantly affected M. synoviae adhesion to SSCs. These studies indicate that two interacting proteins, EF-G, a novel cytoadhesin, and vimentin, an important cell surface receptor, play important roles in the adhesion of M. synoviae to SSCs, laying a foundation for subsequent studies on the mechanism of M. synoviae-induced synovitis and providing meaningful targets for screening target drugs against M. synoviae infection.

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