Fructose-1,6-bisphosphate aldolase encoded by a core gene of Mycoplasma hyopneumoniae contributes to host cell adhesion

• Published in: Veterinary research (Paris) Vol. 49; no. 1; p. 114
• Main Authors: Yu, Yanfei, Liu, Maojun, Hua, Lizhong, Qiu, Mingjun, Zhang, Wei, Wei, Yanna, Gan, Yuan, Feng, Zhixin, Shao, Guoqing, Xiong, Qiyan
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 19.11.2018; BioMed Central; BMC
• Subjects: Aldolases; Analysis; Animals; Bacterial Adhesion - physiology; Blotting, Western - veterinary; Cell adhesion; Electrophoresis, Gel, Two-Dimensional - veterinary; Flow Cytometry - veterinary; Fructose-Bisphosphate Aldolase - genetics; Fructose-Bisphosphate Aldolase - physiology; Gene expression; Genetic aspects; Genome, Bacterial - genetics; Life Sciences; Mollicutes; Mycoplasma hyopneumoniae - enzymology; Mycoplasma hyopneumoniae - genetics; Mycoplasma hyopneumoniae - pathogenicity; Physiological aspects; Pneumonia of Swine, Mycoplasmal - microbiology; Proteomics; Respiratory Mucosa - microbiology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - veterinary; Swine - microbiology; Trachea - microbiology; Veterinary research; Virulence; Virulence-associated Factors; Moonlighting Proteins; Mycoplasma Hyopneumoniae; Hyopneumoniae Strain; Hyopneumoniae Genome
• ISSN: 1297-9716; 0928-4249; 1297-9716
• DOI: 10.1186/s13567-018-0610-2

Mycoplasma hyopneumoniae is an important respiratory pathogen that causes great economic losses to the pig industry worldwide. Although some putative virulence factors have been reported, pathogenesis remains poorly understood. Herein, we evaluated the relative abundance of proteins in virulent 168 (F107) and attenuated 168L (F380) M. hyopneumoniae strains to identify virulence-associated factors by two-dimensional electrophoresis (2-DE). Seven proteins were found to be ≥ 1.5-fold more abundant in 168, and protein-protein interaction network analysis revealed that all seven interact with putative virulence factors. Unexpectedly, six of these virulence-associated proteins are encoded by core rather than accessory genomic elements. The most differentially abundant of the seven, fructose-1,6-bisphosphate aldolase (FBA), was successfully cloned, expressed and purified. Flow cytometry demonstrated the surface localisation of FBA, recombinant FBA (rFBA) mediated adhesion to swine tracheal epithelial cells (STEC), and anti-rFBA sera decreased adherence to STEC. Surface plasmon resonance showed that rFBA bound to fibronectin with a moderately strong K of 469 nM. The results demonstrate that core gene expression contributes to adhesion and virulence in M. hyopneumoniae, and FBA moonlights as an important adhesin, mediating binding to host cells via fibronectin.