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Background Mycoplasma hyopneumoniae  ( M. hyopneumoniae ) is the etiological agent of enzootic pneumonia, a highly infectious swine respiratory disease that distributed worldwide. The pathogenesis and virulence factors of  M. hyopneumoniae  are not fully clarified. As an important virulence factor of bacteria, nicotinamide adenine dinucleotide (NADH) oxidase (NOX) participates in host-pathogen interaction, however, the function of NOX involved in the pathogenesis of  M. hyopneumoniae  is not clear. Results In this study, significant differences in NOX transcription expression levels among different strains of  M. hyopneumoniae  differed in virulence were identified ,  suggesting that NOX may be correlated with  M. hyopneumoniae  virulence. The  nox  gene of  M. hyopneumoniae  was cloned and expressed in  Escherichia coli , and polyclonal antibodies against recombinant NOX (rNOX) were prepared. We confirmed the enzymatic activity of rNOX based on its capacity to oxidize NADH to NAD + . Flow cytometry analysis demonstrated the surface localization of NOX, and subcellular localization analysis further demonstrated that NOX exists in both the cytoplasm and cell membrane. rNOX was depicted to mediate adhesion to immortalized porcine bronchial epithelial cells (hTERT-PBECs). Pre-neutralizing  M. hyopneumoniae  with anti-rNOX antibody resulted in a more than 55% reduction in the adhesion rate of high- and low-virulence  M. hyopneumoniae  strains to hTERT-PBECs. Moreover, a significant difference appeared in the decline in CCU 50  titer between virulent (168) and virulence-attenuated (168L) strains. NOX not only recognized and interacted with host fibronectin but also induced cellular oxidative stress and apoptosis in hTERT-PBECs. The release of lactate dehydrogenase by NOX in hTERT-PBECs was positively correlated with the virulence of  M. hyopneumoniae  strains. Conclusions NOX is considered to be a potential virulence factor of  M. hyopneumoniae  and may play a significant role in mediating its pathogenesis.

NADH oxidase of Mycoplasma hyopneumoniae functions as a potential mediator of virulence