Cargando…
Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae
Enolase is an evolutionarily conserved enzyme involved in the processes of glycolysis and gluconeogenesis. Mycoplasma hyopneumoniae belongs to Mycoplasma, whose species are wall-less and among the smallest self-replicating bacteria, and is an important colonizing respiratory pathogen in the pig indu...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6585157/ https://www.ncbi.nlm.nih.gov/pubmed/31263685 http://dx.doi.org/10.3389/fcimb.2019.00209 |
_version_ | 1783428653033455616 |
---|---|
author | Chen, Rong Yu, Yanfei Feng, Zhixin Gan, Rong Xie, Xing Zhang, Zhenzhen Xie, Qingyun Wang, Weiwu Ran, Tingting Zhang, Wei Xiong, Qiyan Shao, Guoqing |
author_facet | Chen, Rong Yu, Yanfei Feng, Zhixin Gan, Rong Xie, Xing Zhang, Zhenzhen Xie, Qingyun Wang, Weiwu Ran, Tingting Zhang, Wei Xiong, Qiyan Shao, Guoqing |
author_sort | Chen, Rong |
collection | PubMed |
description | Enolase is an evolutionarily conserved enzyme involved in the processes of glycolysis and gluconeogenesis. Mycoplasma hyopneumoniae belongs to Mycoplasma, whose species are wall-less and among the smallest self-replicating bacteria, and is an important colonizing respiratory pathogen in the pig industry worldwide. Mycoplasma hyopneumoniae enolase (Mhp Eno) expression is significantly increased after infection and was previously found to be a virulence factor candidate. Our studies show that Mhp Eno is a cell surface-localized protein that can adhere to swine tracheal epithelial cells (STECs). Adhesion to STECs can be specifically inhibited by an Mhp Eno antibody. Mhp Eno can recognize and interact with plasminogen with high affinity. Here, the first crystal structure of the mycoplasmal enolase from Mycoplasma hyopneumoniae was determined. The structure showed unique features of Mhp Eno in the S3/H1, H6/S6, H7/H8, and H13 regions. All of these regions were longer than those of other enolases and were exposed on the Mhp Eno surface, making them accessible to host molecules. These results show that Mhp Eno has specific structural characteristics and acts as a multifunctional adhesin on the Mycoplasma hyopneumoniae cell surface. |
format | Online Article Text |
id | pubmed-6585157 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-65851572019-07-01 Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae Chen, Rong Yu, Yanfei Feng, Zhixin Gan, Rong Xie, Xing Zhang, Zhenzhen Xie, Qingyun Wang, Weiwu Ran, Tingting Zhang, Wei Xiong, Qiyan Shao, Guoqing Front Cell Infect Microbiol Cellular and Infection Microbiology Enolase is an evolutionarily conserved enzyme involved in the processes of glycolysis and gluconeogenesis. Mycoplasma hyopneumoniae belongs to Mycoplasma, whose species are wall-less and among the smallest self-replicating bacteria, and is an important colonizing respiratory pathogen in the pig industry worldwide. Mycoplasma hyopneumoniae enolase (Mhp Eno) expression is significantly increased after infection and was previously found to be a virulence factor candidate. Our studies show that Mhp Eno is a cell surface-localized protein that can adhere to swine tracheal epithelial cells (STECs). Adhesion to STECs can be specifically inhibited by an Mhp Eno antibody. Mhp Eno can recognize and interact with plasminogen with high affinity. Here, the first crystal structure of the mycoplasmal enolase from Mycoplasma hyopneumoniae was determined. The structure showed unique features of Mhp Eno in the S3/H1, H6/S6, H7/H8, and H13 regions. All of these regions were longer than those of other enolases and were exposed on the Mhp Eno surface, making them accessible to host molecules. These results show that Mhp Eno has specific structural characteristics and acts as a multifunctional adhesin on the Mycoplasma hyopneumoniae cell surface. Frontiers Media S.A. 2019-06-13 /pmc/articles/PMC6585157/ /pubmed/31263685 http://dx.doi.org/10.3389/fcimb.2019.00209 Text en Copyright © 2019 Chen, Yu, Feng, Gan, Xie, Zhang, Xie, Wang, Ran, Zhang, Xiong and Shao. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cellular and Infection Microbiology Chen, Rong Yu, Yanfei Feng, Zhixin Gan, Rong Xie, Xing Zhang, Zhenzhen Xie, Qingyun Wang, Weiwu Ran, Tingting Zhang, Wei Xiong, Qiyan Shao, Guoqing Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title | Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title_full | Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title_fullStr | Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title_full_unstemmed | Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title_short | Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae |
title_sort | featured species-specific loops are found in the crystal structure of mhp eno, a cell surface adhesin from mycoplasma hyopneumoniae |
topic | Cellular and Infection Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6585157/ https://www.ncbi.nlm.nih.gov/pubmed/31263685 http://dx.doi.org/10.3389/fcimb.2019.00209 |
work_keys_str_mv | AT chenrong featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT yuyanfei featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT fengzhixin featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT ganrong featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT xiexing featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT zhangzhenzhen featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT xieqingyun featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT wangweiwu featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT rantingting featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT zhangwei featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT xiongqiyan featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae AT shaoguoqing featuredspeciesspecificloopsarefoundinthecrystalstructureofmhpenoacellsurfaceadhesinfrommycoplasmahyopneumoniae |