Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface of Mycoplasma hyopneumoniae by Binding to Fibronectin.
Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface of Mycoplasma hyopneumoniae by Binding to Fibronectin.
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热不稳定伸长因子 (EF-Tu) 通过与纤连蛋白结合作为猪肺炎支原体表面的粘附素
DOI：
10.3389/fmicb.2018.00974
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发表时间：
2018
影响因子：
5.2
通讯作者：
Shao G
中科院分区：
文献类型：
--
作者：
Yu Y;Wang H;Wang J;Feng Z;Wu M;Liu B;Xin J;Xiong Q;Liu M;Shao G
猪肺炎支原体是一种定植于猪体内的呼吸道病原体，可给养猪业造成巨大的经济损失。虽然已经报道了假定的毒力因子，但该物种的发病机制仍不清楚。在这里，我们使用了致命的M。猪肺炎链球菌168株感染猪气管上皮细胞（STEC），通过双向电泳（2-DE）鉴定感染相关因子。M.并与肉汤中培养的样品进行比较。成功鉴定出细胞感染组中丰度增加≥1.5的6个差异表达蛋白。毒力相关蛋白的String网络分析表明，这6个差异丰度蛋白均与M.下丘脑在这个网络中最重要的上调枢纽之一，延长因子热不稳定（EF-Tu），它在M.成功重组了猪肺炎支原体感染的STEC，并在质谱上获得了较高的分数。除了在蛋白质合成中具有典型的酶活性外，EF-Tu还被报道作为许多其他病原体的重要粘附素位于细胞表面。在M.用流式细胞术检测血小板计数。重组EF-Tu（rEF-Tu）能粘附STEC，抗rEF-Tu抗体包被M.低密度脂蛋白降低了对STEC的粘附。此外，表面等离子体共振（SPR）分析表明，rEF-Tu可以结合纤连蛋白与特异性和中等强度的相互作用，解离常数（KD）为605 nM。此外，纤维连接蛋白在STEC中的阻断也降低了M.在细胞表面形成透明膜。这些数据表明EF-Tu是M.纤维连接蛋白和透明质酸是STEC上不可或缺的受体。EF-Tu与纤连蛋白的结合有助于M.低血压至STEC。研究发现，M.下丘脑EF-Tu也是M.下丘脑EF-Tu的粘附作用部分由纤维连接蛋白介导。
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 (KD) 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-Tu moonlights as an adhesin of M. hyopneumoniae. The adhesive effect of EF-Tu is partly meditated by fibronectin.
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猪肺炎支原体病原168株及其高传代减毒株的比较基因组分析
影响因子：
4.4
作者：
Liu W;Xiao S;Li M;Guo S;Li S;Luo R;Feng Z;Li B;Zhou Z;Shao G;Chen H;Fang L
通讯作者：
Fang L
影响因子：
3.6
作者：
Burnett, TA;Dinkla, K;Djordjevic, SP
通讯作者：
Djordjevic, SP
影响因子：
3.6
作者：
Deutscher, Ania T.;Jenkins, Cheryl;Djordjevic, Steven P.
通讯作者：
Djordjevic, Steven P.
DOI：
10.1513/pats.200801-010aw
发表时间：
2008-08-15
期刊：
Proceedings of the American Thoracic Society
影响因子：
--
作者：
Coraux, Christelle;Roux, Jacqueline;Birembaut, Philippe
通讯作者：
Birembaut, Philippe
影响因子：
3.1
作者：
Adams, C;Pitzer, J;Minion, FC
通讯作者：
Minion, FC