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Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection
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 modu...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9542919/ https://www.ncbi.nlm.nih.gov/pubmed/35791781 http://dx.doi.org/10.1111/mmi.14963 |
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author | Pan, Qiao Xu, Qingyuan Liu, Tong Zhang, Yujuan Xin, Jiuqing |
author_facet | Pan, Qiao Xu, Qingyuan Liu, Tong Zhang, Yujuan Xin, Jiuqing |
author_sort | Pan, Qiao |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9542919 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95429192022-10-14 Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection Pan, Qiao Xu, Qingyuan Liu, Tong Zhang, Yujuan Xin, Jiuqing Mol Microbiol Research Articles 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. John Wiley and Sons Inc. 2022-07-16 2022-09 /pmc/articles/PMC9542919/ /pubmed/35791781 http://dx.doi.org/10.1111/mmi.14963 Text en © 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Research Articles Pan, Qiao Xu, Qingyuan Liu, Tong Zhang, Yujuan Xin, Jiuqing Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title |
Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title_full |
Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title_fullStr |
Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title_full_unstemmed |
Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title_short |
Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection |
title_sort | mycoplasma hyopneumoniae membrane protein mhp271 interacts with host upr protein grp78 to facilitate infection |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9542919/ https://www.ncbi.nlm.nih.gov/pubmed/35791781 http://dx.doi.org/10.1111/mmi.14963 |
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