| Content Provider | Springer Nature : BioMed Central |
|---|---|
| Author | Wang, Jia Li, Yao Pan, Longji Li, Jun Yu, Yanfei Liu, Beibei Zubair, Muhammad Wei, Yanna Pillay, Bala Olaniran, Ademola Olufolahan Chiliza, Thamsanqa E. Shao, Guoqing Feng, Zhixin Xiong, Qiyan |
| Abstract | 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. |
| Related Links | https://veterinaryresearch.biomedcentral.com/counter/pdf/10.1186/s13567-021-00952-8.pdf |
| Ending Page | 14 |
| Page Count | 14 |
| Starting Page | 1 |
| File Format | HTM / HTML |
| ISSN | 12979716 |
| DOI | 10.1186/s13567-021-00952-8 |
| Journal | Veterinary Research |
| Issue Number | 1 |
| Volume Number | 52 |
| Language | English |
| Publisher | BioMed Central |
| Publisher Date | 2021-06-03 |
| Access Restriction | Open |
| Subject Keyword | Veterinary Medicine Veterinary Science Virology Microbiology Immunology M. hyorhinis GAPDH Adhesion Plasminogen Extracellular matrix Veterinary Medicine/Veterinary Science |
| Content Type | Text |
| Resource Type | Article |
| Subject | Veterinary Medicine |
| Journal Impact Factor | 3.7/2023 |
| 5-Year Journal Impact Factor | 3.8/2023 |
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