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

Veterinary Research

Bala Pillay¹  Thamsanqa E. Chiliza¹  Ademola Olufolahan Olaniran¹  Longji Pan²  Jun Li²  Yanna Wei²  Muhammad Zubair²  Zhixin Feng²  Beibei Liu²  Jia Wang³  Guoqing Shao⁴  Qiyan Xiong⁵  Yanfei Yu⁶  Yao Li⁷ 

[1] College of Agriculture, Engineering & Science, University of KwaZulu-Natal, Durban, South Africa;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;College of Agriculture, Engineering & Science, University of KwaZulu-Natal, Durban, South Africa;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;College of Agriculture, Engineering & Science, University of KwaZulu-Natal, Durban, South Africa;School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;College of Agriculture, Engineering & Science, University of KwaZulu-Natal, Durban, South Africa;School of Life Sciences, Jiangsu University, Zhenjiang, China;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;College of Veterinary Medicine, Hunan Agricultural University, Changsha, China;School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China;Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of Agricultural Sciences, Nanjing, China;School of Life Sciences, Jiangsu University, Zhenjiang, China;

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

DOI  :  10.1186/s13567-021-00952-8

来源: Springer

【 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.

【 授权许可】

CC BY