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  Proteomic identification of secreted proteins of Propionibacterium acnes

Holland, C., Mak, T. N., Zimny-Arndt, U., Schmid, M., Meyer, T. F., Jungblut, P. R., et al. (2010). Proteomic identification of secreted proteins of Propionibacterium acnes. BMC Microbiology, 10: 230.

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Genre: Journal Article
Alternative Title : BMC Microbiol.

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BMC_Microbiol_2010_10_230.pdf (Publisher version), 3MB
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© 2010 Holland et al; licensee BioMed Central Ltd. 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.
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Holland, Carsten1, Author              
Mak, Tim N.1, Author              
Zimny-Arndt, Ursula2, Author              
Schmid, Monika2, Author              
Meyer, Thomas F.1, Author              
Jungblut, Peter R.2, Author              
Brüggemann, Holger1, Author              
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1Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664147              
2Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664143              

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 Abstract: 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, beta-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.

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Language(s): eng - English
 Dates: 2010-08-27
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 529858
ISI: 000281804600001
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Title: BMC Microbiology
  Alternative Title : BMC Microbiol.
Source Genre: Journal
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Pages: - Volume / Issue: 10 Sequence Number: 230 Start / End Page: - Identifier: ISSN: 1471-2180