Mycoplasma bovis (M. bovis) is a small bacterium that lacks a cell wall. M. bovis infection can result in chronic pneumonia and polyarthritis syndrome (CPPS), otitis media, conjunctivitis, and meningitis in feedlot cattle and mastitis in dairy cattle. To gain more understanding of the mechanism of M. bovis and host interaction, this study focused on P48, an important membrane protein involved in M. bovis adhesion, proliferation and virulence. In this study, exogenous P48 protein was introduced to explore its function in embryonic bovine lung (EBL) cells by recombinant vector and protein purification. We found that M. bovis infection inhibited EBL cells growth and enhanced apoptosis. Both intracellular and extracellular P48 protein treatment also induce apoptosis. Moreover, P48 activates endoplasmic reticulum (ER) stress response via increasing ER stress markers expression. To further explore the underlying mechanism, we performed inhibition experiments using ER stress inhibitor 4-PBA and specific siRNA interference against GRP78, and found that P48 protein modulated EBL cells apoptosis in an ER stress signaling-dependent manner. This study provided more data to further understand M. bovis infection mechanism and develop effective anti-mycoplasma strategy.
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