A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems.

2.50
Hdl Handle:
http://hdl.handle.net/10033/338723
Title:
A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems.
Authors:
Halbedel, Sven; Reiss, Swantje; Hahn, Birgit; Albrecht, Dirk; Mannala, Gopala Krishna; Chakraborty, Trinad; Hain, Torsten; Engelmann, Susanne; Flieger, Antje
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.
Citation:
A systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems. 2014, 13 (11):3063-81 Mol. Cell Proteomics
Journal:
Molecular & cellular proteomics : MCP
Issue Date:
Nov-2014
URI:
http://hdl.handle.net/10033/338723
DOI:
10.1074/mcp.M114.041327
PubMed ID:
25056936
Type:
Article
Language:
en
ISSN:
1535-9484
Appears in Collections:
publications of the research group Microbial Proteomics (MPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorHalbedel, Svenen
dc.contributor.authorReiss, Swantjeen
dc.contributor.authorHahn, Birgiten
dc.contributor.authorAlbrecht, Dirken
dc.contributor.authorMannala, Gopala Krishnaen
dc.contributor.authorChakraborty, Trinaden
dc.contributor.authorHain, Torstenen
dc.contributor.authorEngelmann, Susanneen
dc.contributor.authorFlieger, Antjeen
dc.date.accessioned2015-01-23T13:11:06Z-
dc.date.available2015-01-23T13:11:06Z-
dc.date.issued2014-11-
dc.identifier.citationA systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems. 2014, 13 (11):3063-81 Mol. Cell Proteomicsen
dc.identifier.issn1535-9484-
dc.identifier.pmid25056936-
dc.identifier.doi10.1074/mcp.M114.041327-
dc.identifier.urihttp://hdl.handle.net/10033/338723-
dc.description.abstractListeria 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.en
dc.language.isoenen
dc.titleA systematic proteomic analysis of Listeria monocytogenes house-keeping protein secretion systems.en
dc.typeArticleen
dc.identifier.journalMolecular & cellular proteomics : MCPen

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