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The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri
Outer membrane phospholipase A (OMPLA) is an enzyme located in the outer membrane of Gram-negative bacteria. OMPLA exhibits broad substrate specificity, and some of its substrates are located in the cellular envelope. Generally, the enzymatic activity can only be induced by perturbation of the cell...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5043575/ https://www.ncbi.nlm.nih.gov/pubmed/27655730 http://dx.doi.org/10.1098/rsob.160073 |
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author | Wang, Xia Jiang, Feng Zheng, Jianhua Chen, Lihong Dong, Jie Sun, Lilian Zhu, Yafang Liu, Bo Yang, Jian Yang, Guowei Jin, Qi |
author_facet | Wang, Xia Jiang, Feng Zheng, Jianhua Chen, Lihong Dong, Jie Sun, Lilian Zhu, Yafang Liu, Bo Yang, Jian Yang, Guowei Jin, Qi |
author_sort | Wang, Xia |
collection | PubMed |
description | Outer membrane phospholipase A (OMPLA) is an enzyme located in the outer membrane of Gram-negative bacteria. OMPLA exhibits broad substrate specificity, and some of its substrates are located in the cellular envelope. Generally, the enzymatic activity can only be induced by perturbation of the cell envelope integrity through diverse methods. Although OMPLA has been thoroughly studied as a membrane protein in Escherichia coli and is constitutively expressed in many other bacterial pathogens, little is known regarding the functions of OMPLA during the process of bacterial infection. In this study, the proteomic and transcriptomic data indicated that OMPLA in Shigella flexneri, termed PldA, both stabilizes the bacterial membrane and is involved in bacterial infection under ordinary culture conditions. A series of physiological assays substantiated the disorganization of the bacterial outer membrane and the periplasmic space in the ΔpldA mutant strain. Furthermore, the ΔpldA mutant strain showed decreased levels of type III secretion system expression, contributing to the reduced internalization efficiency in host cells. The results of this study support that PldA, which is widespread across Gram-negative bacteria, is an important factor for the bacterial life cycle, particularly in human pathogens. |
format | Online Article Text |
id | pubmed-5043575 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-50435752016-10-05 The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri Wang, Xia Jiang, Feng Zheng, Jianhua Chen, Lihong Dong, Jie Sun, Lilian Zhu, Yafang Liu, Bo Yang, Jian Yang, Guowei Jin, Qi Open Biol Research Outer membrane phospholipase A (OMPLA) is an enzyme located in the outer membrane of Gram-negative bacteria. OMPLA exhibits broad substrate specificity, and some of its substrates are located in the cellular envelope. Generally, the enzymatic activity can only be induced by perturbation of the cell envelope integrity through diverse methods. Although OMPLA has been thoroughly studied as a membrane protein in Escherichia coli and is constitutively expressed in many other bacterial pathogens, little is known regarding the functions of OMPLA during the process of bacterial infection. In this study, the proteomic and transcriptomic data indicated that OMPLA in Shigella flexneri, termed PldA, both stabilizes the bacterial membrane and is involved in bacterial infection under ordinary culture conditions. A series of physiological assays substantiated the disorganization of the bacterial outer membrane and the periplasmic space in the ΔpldA mutant strain. Furthermore, the ΔpldA mutant strain showed decreased levels of type III secretion system expression, contributing to the reduced internalization efficiency in host cells. The results of this study support that PldA, which is widespread across Gram-negative bacteria, is an important factor for the bacterial life cycle, particularly in human pathogens. The Royal Society 2016-09-21 /pmc/articles/PMC5043575/ /pubmed/27655730 http://dx.doi.org/10.1098/rsob.160073 Text en © 2016 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Research Wang, Xia Jiang, Feng Zheng, Jianhua Chen, Lihong Dong, Jie Sun, Lilian Zhu, Yafang Liu, Bo Yang, Jian Yang, Guowei Jin, Qi The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title | The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title_full | The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title_fullStr | The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title_full_unstemmed | The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title_short | The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri |
title_sort | outer membrane phospholipase a is essential for membrane integrity and type iii secretion in shigella flexneri |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5043575/ https://www.ncbi.nlm.nih.gov/pubmed/27655730 http://dx.doi.org/10.1098/rsob.160073 |
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