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Links between type III secretion and extracytoplasmic stress responses in Yersinia
The cell envelope of pathogenic bacteria is a barrier against host environmental conditions and immunity molecules, as well as the site where many virulence factors are assembled. Extracytoplasmic stress responses (ESRs) have evolved to help maintain its integrity in conditions where it might be com...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467454/ https://www.ncbi.nlm.nih.gov/pubmed/23087910 http://dx.doi.org/10.3389/fcimb.2012.00125 |
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author | Flores-Kim, Josué Darwin, Andrew J. |
author_facet | Flores-Kim, Josué Darwin, Andrew J. |
author_sort | Flores-Kim, Josué |
collection | PubMed |
description | The cell envelope of pathogenic bacteria is a barrier against host environmental conditions and immunity molecules, as well as the site where many virulence factors are assembled. Extracytoplasmic stress responses (ESRs) have evolved to help maintain its integrity in conditions where it might be compromised. These ESRs also have important links to the production of envelope-associated virulence systems by the bacteria themselves. One such virulence factor is the type III secretion system (T3SS), the first example of which was provided by the pathogenic Yersinia. This article reviews the reported links between four different ESRs and T3SS function in Yersinia. Components of three of these ESRs affect the function and/or regulation of two different T3SSs. The response regulator of the Rcs ESR is involved in positive regulation of the Ysa-Ysp T3SS found in the highly pathogenic 1B biogroup of Y. enterocolitica. Conversely, the response regulator of the Y. pseudotuberculosis Cpx ESR can down-regulate production of the Ysc-Yop T3SS, and at least one other envelope virulence factor (invasin), by direct repression. Also in Y. pseudotuberculosis, there is some evidence suggesting that an intact RpoE ESR might be important for normal Yersinia outer proteins (Yop) production and secretion. Besides these regulatory links between ESRs and T3SSs, perhaps the most striking connection between T3SS function and an ESR is that between the phage shock protein (Psp) and Ysc-Yop systems of Y. enterocolitica. The Psp response does not affect the regulation or function of the Ysc-Yop system. Instead, Ysc-Yop T3SS production induces the Psp system, which then mitigates T3SS-induced envelope stress. Consequently, the Y. enterocolitica Psp system is essential when the Ysc-Yop T3SS is produced. |
format | Online Article Text |
id | pubmed-3467454 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-34674542012-10-19 Links between type III secretion and extracytoplasmic stress responses in Yersinia Flores-Kim, Josué Darwin, Andrew J. Front Cell Infect Microbiol Microbiology The cell envelope of pathogenic bacteria is a barrier against host environmental conditions and immunity molecules, as well as the site where many virulence factors are assembled. Extracytoplasmic stress responses (ESRs) have evolved to help maintain its integrity in conditions where it might be compromised. These ESRs also have important links to the production of envelope-associated virulence systems by the bacteria themselves. One such virulence factor is the type III secretion system (T3SS), the first example of which was provided by the pathogenic Yersinia. This article reviews the reported links between four different ESRs and T3SS function in Yersinia. Components of three of these ESRs affect the function and/or regulation of two different T3SSs. The response regulator of the Rcs ESR is involved in positive regulation of the Ysa-Ysp T3SS found in the highly pathogenic 1B biogroup of Y. enterocolitica. Conversely, the response regulator of the Y. pseudotuberculosis Cpx ESR can down-regulate production of the Ysc-Yop T3SS, and at least one other envelope virulence factor (invasin), by direct repression. Also in Y. pseudotuberculosis, there is some evidence suggesting that an intact RpoE ESR might be important for normal Yersinia outer proteins (Yop) production and secretion. Besides these regulatory links between ESRs and T3SSs, perhaps the most striking connection between T3SS function and an ESR is that between the phage shock protein (Psp) and Ysc-Yop systems of Y. enterocolitica. The Psp response does not affect the regulation or function of the Ysc-Yop system. Instead, Ysc-Yop T3SS production induces the Psp system, which then mitigates T3SS-induced envelope stress. Consequently, the Y. enterocolitica Psp system is essential when the Ysc-Yop T3SS is produced. Frontiers Media S.A. 2012-10-10 /pmc/articles/PMC3467454/ /pubmed/23087910 http://dx.doi.org/10.3389/fcimb.2012.00125 Text en Copyright © 2012 Flores-Kim and Darwin. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc. |
spellingShingle | Microbiology Flores-Kim, Josué Darwin, Andrew J. Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title | Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title_full | Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title_fullStr | Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title_full_unstemmed | Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title_short | Links between type III secretion and extracytoplasmic stress responses in Yersinia |
title_sort | links between type iii secretion and extracytoplasmic stress responses in yersinia |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467454/ https://www.ncbi.nlm.nih.gov/pubmed/23087910 http://dx.doi.org/10.3389/fcimb.2012.00125 |
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