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A multifunctional enolase mediates cytoadhesion and interaction with host plasminogen and fibronectin in Mycoplasma hyorhinis

文献类型： 外文期刊

作者： Wang, Jia 1 ; Yu, Yanfei 1 ; Li, Yao 1 ; Li, Shiyang 1 ; Wang, Li 1 ; Wei, Yanna 1 ; Wu, Yuzi 1 ; Pillay, Bala 2 ; Olaniran, Ademola Olufolahan 2 ; Chiliza, Thamsanqa E. 2 ; Shao, Guoqing 1 ; Feng, Zhixin 1 ; Xiong, Qiyan 1 ;

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

2.Univ KwaZulu Natal, Coll Agr Engn & Sci, Durban, South Africa

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

4.Hunan Agr Univ, Coll Vet Med, Changsha, Peoples R China

关键词： Mycoplasma hyorhinis; virulence factor; enolase; adhesion; plasminogen; fibronectin; moonlighting protein

期刊名称：VETERINARY RESEARCH （ 影响因子：3.829； 五年影响因子：4.269 ）

ISSN： 0928-4249

年卷期： 2022 年 53 卷 1 期

页码：

收录情况： SCI

摘要： Mycoplasma hyorhinis may cause systemic inflammation of pigs, typically polyserositis and arthritis, and is also associated with several types of human cancer. However, the pathogenesis of M. hyorhinis colonizing and breaching the respiratory barrier to establish systemic infection is poorly understood. Glycolytic enzymes are important moonlighting proteins and virulence-related factors in various bacteria. In this study, we investigated the functions of a glycolytic critical enzyme, enolase in the infection and systemic spread of M. hyorhinis. Bacterial surface localization of enolase was confirmed by flow cytometry and colony hybridization assay. Recombinant M. hyorhinis enolase (rEno) was found to adhere to pig kidney (PK-15) cells, and anti-rEno serum significantly decreased adherence. The enzyme was also found to bind host plasminogen and fibronectin, and interactions were specific and strong, with dissociation constant (K-D) values of 1.4 nM and 14.3 nM, respectively, from surface plasmon resonance analysis. Activation of rEno-bound plasminogen was confirmed by its ability to hydrolyze plasmin-specific substrates and to degrade a reconstituted extracellular matrix. To explore key sites during these interactions, C-terminal lysine residues of enolase were replaced with leucine, and the resulting single-site and double-site mutants show significantly reduced interaction with plasminogen in far-Western blotting and surface plasmon resonance tests. The binding affinities of all mutants to fibronectin were reduced as well. Collectively, these results imply that enolase moonlights as an important adhesin of M. hyorhinis, and interacts with plasminogen and fibronectin. The two lysine residues in the C-terminus are important binding sites for its multiple binding activities.

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