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The variable lipoprotein family participates in the interaction of Mycoplasma hyorhinis with host extracellular matrix and plasminogen

文献类型： 外文期刊

作者： Li, Jun 1 ; Wang, Jia 1 ; Shao, Jia 1 ; Li, Yao 1 ; Yu, Yanfei 1 ; Shao, Guoqing 1 ; Feng, Zhixin 1 ; Xiong, Qiyan 1 ;

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

2.Nanjing Agr Univ, Coll Vet Med, Nanjing, Peoples R China

3.Jiangsu Univ, Sch Life Sci, Zhenjiang, Jiangsu, Peoples R China

4.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang, Jiangsu, Peoples R China

关键词： Mycoplasma hyorhinis; Variable lipoprotein; Extracellular matrix; Plasminogen

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.246； 五年影响因子：3.565 ）

ISSN： 0378-1135

年卷期： 2022 年 265 卷

页码：

收录情况： SCI

摘要： Mycoplasma hyorhinis (Mhr) infects pigs, typically causing polyserositis and polyarthritis. It has also been reported in various human tumors. The variable lipoprotein (Vlp) family is a vital surface component mediating the immune evasion of Mhr. We have previously reported its functions in the adherence of Mhr to pig cells. Herein, we further evaluated its role in interacting with host extracellular matrix (ECM) components (fibronectin, collagen type IV and laminin) and plasminogen. Consequently, the recombinant Vlp proteins of all the seven members (VlpA-VlpG) were able to bind most of the tested host molecules. Further experiment showed that region II of all Vlp members has a strong binding ability, while the binding ability of region III of each member varied between different host molecules. Comparing the Vlps containing short (rVlpX3) or long (rVlpX12) region III, we found that the ability of most Vlps binding NCI-H292 cell membrane proteins became weaker as the molecule grows, except VlpG. However, the binding of VlpA, VlpB, VlpC and VlpG to tested ECM components and plasminogen tended to increase as Vlps became longer, and those of VlpE and VlpF decreased, and that of VlpD did not change. Furthermore, the activation of Vlp-bound plasminogen was proved. In summary, the Vlp family participates in the interaction of Mhr with host ECM and plasminogen in addition to cytoadhesion. The size variation of Vlps is likely to further regulate these interactions. The results may help to elucidate the roles of Vlps in the persistent infection of Mhr.

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