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...
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my.usim-84372015-12-31T03:17:20Z Temperature-regulated expression of outer membrane proteins in Shigella flexneri Hemavathy, Harikrishnan, Kirnpal-Kaur Banga, Singh, Asma, Ismail, Dna-Binding Protein Escherichia-Coli Oxidative Stress Salmonella-Typhi Stationary-Phase Virulence Gene Dps Aminopeptidase Identification 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 degrees 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 degrees C were characterized by performing MALDI-ToF-ToF. Results: Different degrees of expression were demonstrated for different proteins expressed at 37 degrees C compared to 38.5 and 40 degrees 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. 2015-06-19T02:53:50Z 2015-06-19T02:53:50Z 2013 Article 1757-4749 http://ddms.usim.edu.my/handle/123456789/8437 http://download.springer.com/static/pdf/388/art%253A10.1186%252F1757-4749-5-38.pdf?originUrl=http%3A%2F%2Fgutpathogens.biomedcentral.com%2Farticle%2F10.1186%2F1757-4749-5-38&token2=exp=1451532097~acl=%2Fstatic%2Fpdf%2F388%2Fart%25253A10.1186%25252F1757-4749-5-38.pdf*~hmac=a40f19bee4d59b1440be2ebd406581c6b892ebce93bfe0a7a136d0129d7ff531 en_US Biomed Central Ltd |
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Dna-Binding Protein Escherichia-Coli Oxidative Stress Salmonella-Typhi Stationary-Phase Virulence Gene Dps Aminopeptidase Identification |
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Dna-Binding Protein Escherichia-Coli Oxidative Stress Salmonella-Typhi Stationary-Phase Virulence Gene Dps Aminopeptidase Identification Hemavathy, Harikrishnan, Kirnpal-Kaur Banga, Singh, Asma, Ismail, Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
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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 degrees 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 degrees C were characterized by performing MALDI-ToF-ToF. Results: Different degrees of expression were demonstrated for different proteins expressed at 37 degrees C compared to 38.5 and 40 degrees 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. |
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Article |
author |
Hemavathy, Harikrishnan, Kirnpal-Kaur Banga, Singh, Asma, Ismail, |
author_facet |
Hemavathy, Harikrishnan, Kirnpal-Kaur Banga, Singh, Asma, Ismail, |
author_sort |
Hemavathy, Harikrishnan, |
title |
Temperature-regulated expression of outer membrane proteins in Shigella flexneri |
title_short |
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_sort |
temperature-regulated expression of outer membrane proteins in shigella flexneri |
publisher |
Biomed Central Ltd |
publishDate |
2015 |
url |
http://ddms.usim.edu.my/handle/123456789/8437 http://download.springer.com/static/pdf/388/art%253A10.1186%252F1757-4749-5-38.pdf?originUrl=http%3A%2F%2Fgutpathogens.biomedcentral.com%2Farticle%2F10.1186%2F1757-4749-5-38&token2=exp=1451532097~acl=%2Fstatic%2Fpdf%2F388%2Fart%25253A10.1186%25252F1757-4749-5-38.pdf*~hmac=a40f19bee4d59b1440be2ebd406581c6b892ebce93bfe0a7a136d0129d7ff531 |
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1645152417538375680 |
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13.222552 |