您好，欢迎访问江苏省农业科学院 机构知识库！
江苏省农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface of Mycoplasma hyopneumoniae by Binding to Fibronectin

文献类型： 外文期刊

作者： Yu, Yanfei 1 ; Wang, Hongen 1 ; Wang, Jia 1 ; Feng, Zhixin 1 ; Wu, Meng 1 ; Liu, Beibei 1 ; Xin, Jiuqing 4 ; Xiong, Qiyan 1 ;

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

2.Jiangsu Acad Agr Sci, Natl Ctr Engn Res Vet Bioprod, Nanjing, Jiangsu, Peoples R China

3.Shanxi Agr Univ, Coll Anim Sci & Technol, Taigu, Peoples R China

4.Chinese Acad Agr Sci, Div Bacterial Dis, Natl Contagious Bovine Pleuropneumonia Reference, State Key Lab Vet Biotechnol,Harbin Vet Res Inst, Harbin, Heilongjiang, Peoples R China

5.State Key Lab Breeding Base, Key Lab Food Qual & Safety Jiangsu Prov, Nanjing, Jiangsu, Peoples R China

关键词： Mycoplasma hyopneumoniae; swine tracheal epithelial cells (STEC); adherence; EF-Tu; fibronectin

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：5.64； 五年影响因子：6.32 ）

ISSN： 1664-302X

年卷期： 2018 年 9 卷

页码：

收录情况： SCI

摘要： Mycoplasma hyopneumoniae is a colonizing respiratory pathogen that can cause great economic losses to the pig industry worldwide. Although putative virulence factors have been reported, the pathogenesis of this species remains unclear. Here, we used the virulent M. hyopneumoniae strain 168 to infect swine tracheal epithelial cells (STEC) to identify the infection-associated factors by two-dimensional electrophoresis (2-DE). Whole proteins of M. hyopneumoniae were obtained and compared with samples cultured in broth. Six differentially expressed proteins with an increase in abundance of >= 1.5 in the cell infection group were successfully identified. A String network of virulence-associated proteins showed that all the six differential abundance proteins were involved in virulence of M. hyopneumoniae. One of the most important upregulated hubs in this network, elongation factor thermo unstable (EF-Tu), which showed a relatively higher expression in M. hyopneumoniae-infected STEC and obtained a higher score on mass spectrometry was successfully recombined. In addition to its canonical enzymatic activities in protein synthesis, EF-Tu was also reported to be located on the cell surface as an important adhesin in many other pathogens. The cell surface location of EF-Tu was then observed in M. hyopneumoniae with flow cytometry. Recombinant EF-Tu (rEF-Tu) was found to be able to adhere to STEC and anti-rEF-Tu antibody enclosed M. hyopneumoniae decreased adherence to STEC. In addition, surface plasmon resonance (SPR) analysis showed that rEF-Tu could bind to fibronectin with a specific and moderately strong interaction, a dissociation constant (K-D) of 605 nM. Furthermore, the block of fibronectin in STEC also decreased the binding of M. hyopneumoniae to the cell surface. Collectively, these data imply EF-Tu as an important adhesin of M. hyopneumoniae and fibronectin as an indispensable receptor on STEC. The binding between EF-Tu with fibronectin contributes to the adhesion of M. hyopneumoniae to STEC. HIGHLIGHTS Elongation factor thermo unstable (EF-Tu) exists on the cell surface of M. hyopneumoniae. EF-Tumoonlights as an adhesin of M. hyopneumoniae. The adhesive effect of EF-Tu is partly meditated by fibronectin.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：江苏省农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台