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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) moonlights as an adhesin in Mycoplasma hyorhinis adhesion to epithelial cells as well as a plasminogen receptor mediating extracellular matrix degradation

文献类型： 外文期刊

作者： Wang, Jia 1 ; Li, Yao 1 ; Pan, Longji 1 ; Li, Jun 1 ; Yu, Yanfei 1 ; Liu, Beibei 1 ; Zubair, Muhammad 1 ; Wei, Yanna 1 ; Pil 1 ;

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

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

关键词： M; hyorhinis; GAPDH; Adhesion; Plasminogen; Extracellular matrix

期刊名称：VETERINARY RESEARCH （ 影响因子：3.699； 五年影响因子：4.113 ）

ISSN： 0928-4249

年卷期： 2021 年 52 卷 1 期

页码：

收录情况： SCI

摘要： Mycoplasma hyorhinis infects pigs causing polyserositis and polyarthritis, and has also been reported in a variety of human tumor tissues. The occurrence of disease is often linked with the systemic invasion of the pathogen. Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH), one of the key enzymes of glycolysis, was reported as a surface multifunctional molecule in several bacteria. Here, we investigated whether GAPDH could manifest binary functions; as an adhesin to promote colonization as well as a plasminogen receptor functioning in extracellular matrix (ECM) degradation to promote systemic invasion. The surface localization of GAPDH was observed in M. hyorhinis with flow cytometry and colony blot analysis. Recombinant GAPDH (rGAPDH) was found to be able to bind porcine-derived PK-15 and human-derived NCI-H292 cells. The incubation with anti-GAPDH antibody significantly decreased the adherence of M. hyorhinis to both cell lines. To investigate its function in recruiting plasminogen, firstly, the interaction between rGAPDH and plasminogen was demonstrated by ELISA and Far-Western blot assay. The activation of the rGAPDH-bound plasminogen into plasmin was proved by using a chromogenic substrate, and furtherly confirmed to degrade extracellular matrix by using a reconstituted ECM. Finally, the ability of rGAPDH to bind different ECM components was demonstrated, including fibronectin, laminin, collagen type IV and vitronectin. Collectively, our data imply GAPDH as an important adhesion factor of M. hyrohinis and a receptor for hijacking host plasminogen to degrade ECM. The multifunction of GAPDH to bind both plasminogen and ECM components is believed to increase the targeting of proteolysis and facilitate the dissemination of M. hyorhinis.

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