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A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems.
Halbedel, Sven Reiss, Swantje Hahn, Birgit Albrecht, Dirk Mannala, Gopala Krishna Chakraborty, Trinad Hain, Torsten Engelmann, Susanne Flieger, Antje
Halbedel, Sven
Reiss, Swantje
Hahn, Birgit
Albrecht, Dirk
Mannala, Gopala Krishna
Chakraborty, Trinad
Hain, Torsten
Engelmann, Susanne
Flieger, Antje
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2014-11
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Abstract
Listeria monocytogenes is a firmicute bacterium causing serious infections in humans upon consumption of contaminated food. Most of its virulence factors are secretory proteins either released to the medium or attached to the bacterial surface. L. monocytogenes encodes at least six different protein secretion pathways. Although great efforts have been made in the past to predict secretory proteins and their secretion routes using bioinformatics, experimental evidence is lacking for most secretion systems. Therefore, we constructed mutants in the main housekeeping protein secretion systems, which are the Sec-dependent transport, the YidC membrane insertases SpoIIIJ and YqjG, as well as the twin-arginine pathway, and analyzed their secretion and virulence defects. Our results demonstrate that Sec-dependent secretion and membrane insertion of proteins via YidC proteins are essential for viability of L. monocytogenes. Depletion of SecA or YidC activity severely affected protein secretion, whereas loss of the Tat-pathway was without any effect on secretion, viability, and virulence. Two-dimensional gel electrophoresis combined with protein identification by mass spectrometry revealed that secretion of many virulence factors and of enzymes synthesizing and degrading the cell wall depends on the SecA route. This finding was confirmed by SecA inhibition experiments using sodium azide. Analysis of secretion of substrates typically dependent on the accessory SecA2 ATPase in wild type and azide resistant mutants of L. monocytogenes revealed for the first time that SecA2-dependent protein secretion also requires the ATPase activity of the house-keeping SecA protein.
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A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems. 2014, 13 (11):3063-81 Mol. Cell Proteomics
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en
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1535-9484