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Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155

BACKGROUND: The usually non-pathogenic soil bacterium Mycobacterium smegmatis is commonly used as a model mycobacterial organism because it is fast growing and shares many features with pathogenic mycobacteria. Proteomic studies of M. smegmatis can shed light on mechanisms of mycobacterial growth, c...

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Detalles Bibliográficos
Autores principales: He, Zhiguo, De Buck, Jeroen
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2867950/
https://www.ncbi.nlm.nih.gov/pubmed/20412585
http://dx.doi.org/10.1186/1471-2180-10-121
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author He, Zhiguo
De Buck, Jeroen
author_facet He, Zhiguo
De Buck, Jeroen
author_sort He, Zhiguo
collection PubMed
description BACKGROUND: The usually non-pathogenic soil bacterium Mycobacterium smegmatis is commonly used as a model mycobacterial organism because it is fast growing and shares many features with pathogenic mycobacteria. Proteomic studies of M. smegmatis can shed light on mechanisms of mycobacterial growth, complex lipid metabolism, interactions with the bacterial environment and provide a tractable system for antimycobacterial drug development. The cell wall proteins are particularly interesting in this respect. The aim of this study was to construct a reference protein map for these proteins in M. smegmatis. RESULTS: A proteomic analysis approach, based on one dimensional polyacrylamide gel electrophoresis and LC-MS/MS, was used to identify and characterize the cell wall associated proteins of M. smegmatis. An enzymatic cell surface shaving method was used to determine the surface-exposed proteins. As a result, a total of 390 cell wall proteins and 63 surface-exposed proteins were identified. Further analysis of the 390 cell wall proteins provided the theoretical molecular mass and pI distributions and determined that 26 proteins are shared with the surface-exposed proteome. Detailed information about functional classification, signal peptides and number of transmembrane domains are given next to discussing the identified transcriptional regulators, transport proteins and the proteins involved in lipid metabolism and cell division. CONCLUSION: In short, a comprehensive profile of the M. smegmatis cell wall subproteome is reported. The current research may help the identification of some valuable vaccine and drug target candidates and provide foundation for the future design of preventive, diagnostic, and therapeutic strategies against mycobacterial diseases.
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spelling pubmed-28679502010-05-12 Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155 He, Zhiguo De Buck, Jeroen BMC Microbiol Research article BACKGROUND: The usually non-pathogenic soil bacterium Mycobacterium smegmatis is commonly used as a model mycobacterial organism because it is fast growing and shares many features with pathogenic mycobacteria. Proteomic studies of M. smegmatis can shed light on mechanisms of mycobacterial growth, complex lipid metabolism, interactions with the bacterial environment and provide a tractable system for antimycobacterial drug development. The cell wall proteins are particularly interesting in this respect. The aim of this study was to construct a reference protein map for these proteins in M. smegmatis. RESULTS: A proteomic analysis approach, based on one dimensional polyacrylamide gel electrophoresis and LC-MS/MS, was used to identify and characterize the cell wall associated proteins of M. smegmatis. An enzymatic cell surface shaving method was used to determine the surface-exposed proteins. As a result, a total of 390 cell wall proteins and 63 surface-exposed proteins were identified. Further analysis of the 390 cell wall proteins provided the theoretical molecular mass and pI distributions and determined that 26 proteins are shared with the surface-exposed proteome. Detailed information about functional classification, signal peptides and number of transmembrane domains are given next to discussing the identified transcriptional regulators, transport proteins and the proteins involved in lipid metabolism and cell division. CONCLUSION: In short, a comprehensive profile of the M. smegmatis cell wall subproteome is reported. The current research may help the identification of some valuable vaccine and drug target candidates and provide foundation for the future design of preventive, diagnostic, and therapeutic strategies against mycobacterial diseases. BioMed Central 2010-04-22 /pmc/articles/PMC2867950/ /pubmed/20412585 http://dx.doi.org/10.1186/1471-2180-10-121 Text en Copyright ©2010 He and De Buck; 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.
spellingShingle Research article
He, Zhiguo
De Buck, Jeroen
Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title_full Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title_fullStr Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title_full_unstemmed Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title_short Cell wall proteome analysis of Mycobacterium smegmatis strain MC2 155
title_sort cell wall proteome analysis of mycobacterium smegmatis strain mc2 155
topic Research article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2867950/
https://www.ncbi.nlm.nih.gov/pubmed/20412585
http://dx.doi.org/10.1186/1471-2180-10-121
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