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Temperature-regulated expression of outer membrane proteins in Shigella flexneri
BACKGROUND: Bacteria exist widely in a diversity of natural environments. In order to survive adverse conditions such as nutrient depletion, biochemical and biological disturbances, and high temperature, bacteria have developed a wide variety of coping mechanisms. Temperature is one of the most impo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029548/ https://www.ncbi.nlm.nih.gov/pubmed/24330657 http://dx.doi.org/10.1186/1757-4749-5-38 |
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author | Harikrishnan, Hemavathy Ismail, Asma Banga Singh, Kirnpal-Kaur |
author_facet | Harikrishnan, Hemavathy Ismail, Asma Banga Singh, Kirnpal-Kaur |
author_sort | Harikrishnan, Hemavathy |
collection | PubMed |
description | BACKGROUND: Bacteria exist widely in a diversity of natural environments. In order to survive adverse conditions such as nutrient depletion, biochemical and biological disturbances, and high temperature, bacteria have developed a wide variety of coping mechanisms. Temperature is one of the most important factors that can enhance the expression of microbial proteins. This study was conducted to investigate how outer membrane proteins (OMPs) of the bacterium Shigella flexneri respond to stress, especially during fever when the host’s body temperature is elevated. METHODS: OMPs of S. flexneri ATCC 12022 and clinical isolate SH057 were extracted from an overnight culture grown at 37, 38.5, and 40°C. Comparisons of the expressed proteins under the different growth conditions were based on equal numbers of bacterial cells loaded in the SDS-PAGE gels. Separated proteins were stained with Coomassie brilliant blue. Selected proteins showing increased expression at 38.5 and 40°C were characterized by performing MALDI-ToF-ToF. RESULTS: Different degrees of expression were demonstrated for different proteins expressed at 37°C compared to 38.5 and 40°C. The proteins with molecular sizes of 18.4, 25.6, and 57.0 kDa showed increased expression level at increasing temperature and were identified as Dps, WrbA, and PepA, respectively. CONCLUSION: This study revealed that strains of S. flexneri respond at the proteomic level during stress caused by elevated temperature by decreasing the expression of proteins, maintaining the level of important proteins, or enhancing the levels of proteins presumably involved in survival and virulence. |
format | Online Article Text |
id | pubmed-4029548 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-40295482014-05-22 Temperature-regulated expression of outer membrane proteins in Shigella flexneri Harikrishnan, Hemavathy Ismail, Asma Banga Singh, Kirnpal-Kaur Gut Pathog Research BACKGROUND: Bacteria exist widely in a diversity of natural environments. In order to survive adverse conditions such as nutrient depletion, biochemical and biological disturbances, and high temperature, bacteria have developed a wide variety of coping mechanisms. Temperature is one of the most important factors that can enhance the expression of microbial proteins. This study was conducted to investigate how outer membrane proteins (OMPs) of the bacterium Shigella flexneri respond to stress, especially during fever when the host’s body temperature is elevated. METHODS: OMPs of S. flexneri ATCC 12022 and clinical isolate SH057 were extracted from an overnight culture grown at 37, 38.5, and 40°C. Comparisons of the expressed proteins under the different growth conditions were based on equal numbers of bacterial cells loaded in the SDS-PAGE gels. Separated proteins were stained with Coomassie brilliant blue. Selected proteins showing increased expression at 38.5 and 40°C were characterized by performing MALDI-ToF-ToF. RESULTS: Different degrees of expression were demonstrated for different proteins expressed at 37°C compared to 38.5 and 40°C. The proteins with molecular sizes of 18.4, 25.6, and 57.0 kDa showed increased expression level at increasing temperature and were identified as Dps, WrbA, and PepA, respectively. CONCLUSION: This study revealed that strains of S. flexneri respond at the proteomic level during stress caused by elevated temperature by decreasing the expression of proteins, maintaining the level of important proteins, or enhancing the levels of proteins presumably involved in survival and virulence. BioMed Central 2013-12-11 /pmc/articles/PMC4029548/ /pubmed/24330657 http://dx.doi.org/10.1186/1757-4749-5-38 Text en Copyright © 2013 Harikrishnan et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Harikrishnan, Hemavathy Ismail, Asma Banga Singh, Kirnpal-Kaur Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title | Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_full | Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_fullStr | Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_full_unstemmed | Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_short | Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_sort | temperature-regulated expression of outer membrane proteins in shigella flexneri |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029548/ https://www.ncbi.nlm.nih.gov/pubmed/24330657 http://dx.doi.org/10.1186/1757-4749-5-38 |
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