文献类型： 外文期刊

作者： Wang, Jiying ¹ ; Li, Shiyang ¹ ; Chen, Junhong ⁵ ; Gan, Lanxi ¹ ; Wang, Jia ² ; Xiong, Qiyan ² ; Feng, Zhixin ² ; Li, Quan ⁷ ; Deng, Zhibang ¹ ; Yuan, Xiaomin ¹ ; Yu, Yanfei ² ;

作者机构： 1.Hunan Agr Univ, Coll Vet Med, Changsha, Peoples R China

2.Jiangsu Acad Agr Sci, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Minist Agr & Rural Affairs, Nanjing, Peoples R China

3.Guotai Taizhou Ctr Technol Innovat Vet Biol, Taizhou, Peoples R China

4.Huaihua Polytech Coll, Dept Anim Sci & Technol, Huaihua, Peoples R China

5.Jinling Inst Technol, Sch Anim Sci & Food Engn, Nanjing, Peoples R China

6.Univ Kwazulu Natal, Sch Life Sci, Discipline Microbiol, Durban, South Africa

7.Yangzhou Univ, Coll Vet Med, Yangzhou, Peoples R China

关键词： Mesomycoplasma hyopneumoniae; GAPDH; adhesion; plasminogen; extracellular matrix

期刊名称：MICROBIOLOGY SPECTRUM （ 影响因子：3.7； 五年影响因子：5.9 ）

ISSN： 2165-0497

年卷期： 2023 年 11 卷 3 期

页码：

收录情况： SCI

摘要： Mesomycoplasma hyopneumoniae is a specific pathogen of pigs that is the etiological agent of mycoplasmal pneumonia of swine (MPS), which is responsible for substantial economic losses to the swine industry worldwide. The pathogenicity mechanism and possible particular virulence determinants of M. hyopneumoniae are not yet completely elucidated. Mesomycoplasma hyopneumoniae is the etiological agent of mycoplasmal pneumonia of swine (MPS), which causes substantial economic losses to the world's swine industry. Moonlighting proteins are increasingly being shown to play a role in the pathogenic process of M. hyopneumoniae. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme in glycolysis, displayed a higher abundance in a highly virulent strain of M. hyopneumoniae than in an attenuated strain, suggesting that it may have a role in virulence. The mechanism by which GAPDH exerts its function was explored. Flow cytometry and colony blot analysis showed that GAPDH was partly displayed on the surface of M. hyopneumoniae. Recombinant GAPDH (rGAPDH) was able to bind PK15 cells, while the adherence of a mycoplasma strain to PK15 was significantly blocked by anti-rGAPDH antibody pretreatment. In addition, rGAPDH could interact with plasminogen. The rGAPDH-bound plasminogen was demonstrated to be activated to plasmin, as proven by using a chromogenic substrate, and to further degrade the extracellular matrix (ECM). The critical site for GAPDH binding to plasminogen was K336, as demonstrated by amino acid mutation. The affinity of plasminogen for the rGAPDH C-terminal mutant (K336A) was significantly decreased according to surface plasmon resonance analysis. Collectively, our data suggested that GAPDH might be an important virulence factor that facilitates the dissemination of M. hyopneumoniae by hijacking host plasminogen to degrade the tissue ECM barrier.IMPORTANCE Mesomycoplasma hyopneumoniae is a specific pathogen of pigs that is the etiological agent of mycoplasmal pneumonia of swine (MPS), which is responsible for substantial economic losses to the swine industry worldwide. The pathogenicity mechanism and possible particular virulence determinants of M. hyopneumoniae are not yet completely elucidated. Our data suggest that GAPDH might be an important virulence factor in M. hyopneumoniae that facilitates the dissemination of M. hyopneumoniae by hijacking host plasminogen to degrade the extracellular matrix (ECM) barrier. These findings will provide theoretical support and new ideas for the research and development of live-attenuated or subunit vaccines against M. hyopneumoniae.