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Proteomic identification of secreted proteins of Propionibacterium acnes
BACKGROUND: The anaerobic Gram-positive bacterium Propionibacterium acnes is a human skin commensal that resides preferentially within sebaceous follicles; however, it also exhibits many traits of an opportunistic pathogen, playing roles in a variety of inflammatory diseases such as acne vulgaris. T...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3224659/ https://www.ncbi.nlm.nih.gov/pubmed/20799957 http://dx.doi.org/10.1186/1471-2180-10-230 |
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author | Holland, Carsten Mak, Tim N Zimny-Arndt, Ursula Schmid, Monika Meyer, Thomas F Jungblut, Peter R Brüggemann, Holger |
author_facet | Holland, Carsten Mak, Tim N Zimny-Arndt, Ursula Schmid, Monika Meyer, Thomas F Jungblut, Peter R Brüggemann, Holger |
author_sort | Holland, Carsten |
collection | PubMed |
description | BACKGROUND: The anaerobic Gram-positive bacterium Propionibacterium acnes is a human skin commensal that resides preferentially within sebaceous follicles; however, it also exhibits many traits of an opportunistic pathogen, playing roles in a variety of inflammatory diseases such as acne vulgaris. To date, the underlying disease-causing mechanisms remain ill-defined and knowledge of P. acnes virulence factors remains scarce. Here, we identified proteins secreted during anaerobic cultivation of a range of skin and clinical P. acnes isolates, spanning the four known phylogenetic groups. RESULTS: Culture supernatant proteins of P. acnes were separated by two-dimensional electrophoresis (2-DE) and all Coomassie-stained spots were subsequently identified by MALDI mass spectrometry (MALDI-MS). A set of 20 proteins was secreted in the mid-exponential growth phase by the majority of strains tested. Functional annotation revealed that many of these common proteins possess degrading activities, including glycoside hydrolases with similarities to endoglycoceramidase, β-N-acetylglucosaminidase and muramidase; esterases such as lysophospholipase and triacylglycerol lipase; and several proteases. Other secreted factors included Christie-Atkins-Munch-Petersen (CAMP) factors, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and several hypothetical proteins, a few of which are unique to P. acnes. Strain-specific differences were apparent, mostly in the secretion of putative adhesins, whose genes exhibit variable phase variation-like sequence signatures. CONCLUSIONS: Our proteomic investigations have revealed that the P. acnes secretome harbors several proteins likely to play a role in host-tissue degradation and inflammation. Despite a large overlap between the secretomes of all four P. acnes phylotypes, distinct differences between predicted host-tissue interacting proteins were identified, providing potential insight into the differential virulence properties of P. acnes isolates. Thus, our data presents a rich resource for guiding much-needed investigations on P. acnes virulence factors and host interacting properties. |
format | Online Article Text |
id | pubmed-3224659 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-32246592011-11-28 Proteomic identification of secreted proteins of Propionibacterium acnes Holland, Carsten Mak, Tim N Zimny-Arndt, Ursula Schmid, Monika Meyer, Thomas F Jungblut, Peter R Brüggemann, Holger BMC Microbiol Research Article BACKGROUND: The anaerobic Gram-positive bacterium Propionibacterium acnes is a human skin commensal that resides preferentially within sebaceous follicles; however, it also exhibits many traits of an opportunistic pathogen, playing roles in a variety of inflammatory diseases such as acne vulgaris. To date, the underlying disease-causing mechanisms remain ill-defined and knowledge of P. acnes virulence factors remains scarce. Here, we identified proteins secreted during anaerobic cultivation of a range of skin and clinical P. acnes isolates, spanning the four known phylogenetic groups. RESULTS: Culture supernatant proteins of P. acnes were separated by two-dimensional electrophoresis (2-DE) and all Coomassie-stained spots were subsequently identified by MALDI mass spectrometry (MALDI-MS). A set of 20 proteins was secreted in the mid-exponential growth phase by the majority of strains tested. Functional annotation revealed that many of these common proteins possess degrading activities, including glycoside hydrolases with similarities to endoglycoceramidase, β-N-acetylglucosaminidase and muramidase; esterases such as lysophospholipase and triacylglycerol lipase; and several proteases. Other secreted factors included Christie-Atkins-Munch-Petersen (CAMP) factors, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and several hypothetical proteins, a few of which are unique to P. acnes. Strain-specific differences were apparent, mostly in the secretion of putative adhesins, whose genes exhibit variable phase variation-like sequence signatures. CONCLUSIONS: Our proteomic investigations have revealed that the P. acnes secretome harbors several proteins likely to play a role in host-tissue degradation and inflammation. Despite a large overlap between the secretomes of all four P. acnes phylotypes, distinct differences between predicted host-tissue interacting proteins were identified, providing potential insight into the differential virulence properties of P. acnes isolates. Thus, our data presents a rich resource for guiding much-needed investigations on P. acnes virulence factors and host interacting properties. BioMed Central 2010-08-27 /pmc/articles/PMC3224659/ /pubmed/20799957 http://dx.doi.org/10.1186/1471-2180-10-230 Text en Copyright ©2010 Holland 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. |
spellingShingle | Research Article Holland, Carsten Mak, Tim N Zimny-Arndt, Ursula Schmid, Monika Meyer, Thomas F Jungblut, Peter R Brüggemann, Holger Proteomic identification of secreted proteins of Propionibacterium acnes |
title | Proteomic identification of secreted proteins of Propionibacterium acnes |
title_full | Proteomic identification of secreted proteins of Propionibacterium acnes |
title_fullStr | Proteomic identification of secreted proteins of Propionibacterium acnes |
title_full_unstemmed | Proteomic identification of secreted proteins of Propionibacterium acnes |
title_short | Proteomic identification of secreted proteins of Propionibacterium acnes |
title_sort | proteomic identification of secreted proteins of propionibacterium acnes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3224659/ https://www.ncbi.nlm.nih.gov/pubmed/20799957 http://dx.doi.org/10.1186/1471-2180-10-230 |
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