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Identification of a novel adhesin-like glycoprotein from Mycoplasma hyopneumoniae
1Department of Pathobiology, Pig Research Institute Taiwan, Chunan, Miaoli, Taiwan.
Abstract:
This study identifies an adhesin-like glycoprotein, which was a 110 kDa protein (P110) under HPLC-GPC assay. This adhesin consisted of one P54 and two P28 subunits. In addition, N-glycosidase F could cleave all N-linked oligosaccharides on the P54 subunit. Experimental results indicated that P110 with native conformations significantly inhibited the adherence of biotin-labeled porcine tracheal epithelial cell extracts to the intact M. hyopneumoniae cells (p < 0.01). Furthermore, the biotin-labeled porcine tracheal epithelial cell extracts specifically bound to P54 and P28 subunits. This binding could be competitively inhibited by unlabeled porcine tracheal epithelial extracts and SPF porcine antisera against Mycoplasma hyopneumoniae. Both P54 and P28 subunits were constitutively expressed in different strains of M. hyopneumoniae. Their production was negligibly changed at various passages during in vitro cultivation. The significant role of this adhesin-like glycoprotein in the pathogenesis of swine pneumonia is under study.
Insights
Researchers identified a novel adhesin-like glycoprotein (P110) in Mycoplasma hyopneumoniae. This protein, composed of P54 and P28 subunits, inhibits bacterial adherence to swine respiratory cells, suggesting a role in swine pneumonia.
Area of Science:
- Veterinary Microbiology
- Molecular Biology
- Protein Biochemistry
Background:
- Mycoplasma hyopneumoniae is a primary cause of swine respiratory disease.
- Understanding bacterial adherence mechanisms is crucial for developing effective control strategies.
- Adhesins play a key role in the colonization and pathogenesis of M. hyopneumoniae.
Purpose of the Study:
- To identify and characterize a novel adhesin-like glycoprotein involved in M. hyopneumoniae adherence.
- To investigate the role of this adhesin in the interaction with porcine respiratory epithelial cells.
Main Methods:
- High-Performance Liquid Chromatography-Gel Permeation Chromatography (HPLC-GPC) was used to determine protein size.
- N-glycosidase F treatment was employed to assess glycosylation.
- Binding assays using biotin-labeled porcine tracheal epithelial cell extracts were performed.
- Western blot analysis with porcine antisera was utilized.
Main Results:
- A 110 kDa adhesin-like glycoprotein (P110) composed of P54 and P28 subunits was identified.
- P110 significantly inhibited M. hyopneumoniae adherence to porcine tracheal epithelial cells.
- Porcine epithelial cell extracts specifically bound to P54 and P28 subunits.
- Binding was competitively inhibited by unlabeled extracts and M. hyopneumoniae-specific antisera.
- P54 and P28 subunits were constitutively expressed across M. hyopneumoniae strains.
Conclusions:
- The identified adhesin-like glycoprotein (P110) and its subunits (P54, P28) are key mediators of M. hyopneumoniae adherence to swine respiratory cells.
- These findings provide insights into the pathogenesis of swine pneumonia.
- Further studies are warranted to elucidate the precise role of this adhesin in disease development.