Proteomic identification of secreted proteins of Propionibacterium acnes

BMC Microbiology
Carsten HollandHolger Brüggemann

Abstract

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. 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 (CA...Continue Reading

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Related Concepts

Acne Vulgaris
Bacterial Proteins
Propionibacterium acnes
2D Polyacrylamide Gel Electrophoresis
Determination, Sequence Homology
Protein Targeting
Proteomics
Beta-N-Acetylglucosaminidase
Electrophoresis, Gel, Two-Dimensional
Esterases

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