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The unfolded protein response (UPR) plays a crucial role in  Mycoplasma hyopneumoniae  ( M. hyopneumoniae ) pathogenesis. We previously demonstrated that  M. hyopneumoniae  interferes with the host UPR to foster bacterial adhesion and infection. However, the underlying molecular mechanism of this UPR modulation is unclear. Here, we report that  M. hyopneumoniae  membrane protein Mhp271 interacts with host GRP78, a master regulator of UPR localized to the porcine tracheal epithelial cells (PTECs) surface. The interaction of Mhp271 with GRP78 reduces the porcine beta‐defensin 2 (PBD‐2) production, thereby facilitating  M. hyopneumoniae  adherence and infection. Furthermore, the R1‐2 repeat region of Mhp271 is crucial for GRP78 binding and the regulation of PBD‐2 expression. Intriguingly, a coimmunoprecipitation (Co‐IP) assay and molecular docking prediction indicated that the ATP, rather than the substrate‐binding domain of GRP78, is targeted by Mhp271 R1‐2. Overall, our findings identify host GRP78 as a target for  M. hyopneumoniae  Mhp271 modulating the host UPR to facilitate  M. hyopneumoniae  adherence and infection.

Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection