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Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection
Author(s) -
Pan Qiao,
Xu Qingyuan,
Liu Tong,
Zhang Yujuan,
Xin Jiuqing
Publication year - 2022
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14963
Subject(s) - mycoplasma hyopneumoniae , biology , microbiology and biotechnology , unfolded protein response , endoplasmic reticulum
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.