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

• DOI: 10.1186/s13567-018-0610-2
• Publication Date: 2018-11-19T13:29:04Z
• Authors: Yanfei Yu; Maojun Liu; Lizhong Hua; Mingjun Qiu; Wei Zhang; Yanna Wei; Yuan Gan; Zhixin Feng; Guoqing Shao; Qiyan Xiong
• Keywords: Mycoplasma hyopneumoniae

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 relative abundance of proteins in virulent 168 (F107) and attenuated 168L (F380) M. strains identify virulence-associated by two-dimensional electrophoresis (2-DE). Seven were found be ≥ 1.5-fold more abundant 168, protein–protein interaction network analysis revealed all seven interact with factors. Unexpectedly, six these are encoded core rather than accessory genomic elements. The most differentially seven, fructose-1,6-bisphosphate aldolase (FBA), was successfully cloned, expressed purified. Flow cytometry demonstrated surface localisation FBA, recombinant FBA (rFBA) mediated adhesion swine tracheal epithelial cells (STEC), anti-rFBA sera decreased adherence STEC. Surface plasmon resonance showed rFBA bound fibronectin a moderately strong KD 469 nM. results demonstrate gene expression contributes hyopneumoniae, moonlights as adhesin, mediating binding host via fibronectin.