Cargando…
SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins
The aim of this study was to explore the role of SecDF in protein secretion in Bacillus cereus ATCC 14579 by in-depth characterization of a markerless secDF knock out mutant. Deletion of secDF resulted in pleiotropic effects characterized by a moderately slower growth rate, aberrant cell morphology,...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118872/ https://www.ncbi.nlm.nih.gov/pubmed/25083861 http://dx.doi.org/10.1371/journal.pone.0103326 |
_version_ | 1782328897447133184 |
---|---|
author | Vörös, Aniko Simm, Roger Slamti, Leyla McKay, Matthew J. Hegna, Ida K. Nielsen-LeRoux, Christina Hassan, Karl A. Paulsen, Ian T. Lereclus, Didier Økstad, Ole Andreas Molloy, Mark P. Kolstø, Anne-Brit |
author_facet | Vörös, Aniko Simm, Roger Slamti, Leyla McKay, Matthew J. Hegna, Ida K. Nielsen-LeRoux, Christina Hassan, Karl A. Paulsen, Ian T. Lereclus, Didier Økstad, Ole Andreas Molloy, Mark P. Kolstø, Anne-Brit |
author_sort | Vörös, Aniko |
collection | PubMed |
description | The aim of this study was to explore the role of SecDF in protein secretion in Bacillus cereus ATCC 14579 by in-depth characterization of a markerless secDF knock out mutant. Deletion of secDF resulted in pleiotropic effects characterized by a moderately slower growth rate, aberrant cell morphology, enhanced susceptibility to xenobiotics, reduced virulence and motility. Most toxins, including food poisoning-associated enterotoxins Nhe, Hbl, and cytotoxin K, as well as phospholipase C were less abundant in the secretome of the ΔsecDF mutant as determined by label-free mass spectrometry. Global transcriptome studies revealed profound transcriptional changes upon deletion of secDF indicating cell envelope stress. Interestingly, the addition of glucose enhanced the described phenotypes. This study shows that SecDF is an important part of the Sec-translocase mediating efficient secretion of virulence factors in the Gram-positive opportunistic pathogen B. cereus, and further supports the notion that B. cereus enterotoxins are secreted by the Sec-system. |
format | Online Article Text |
id | pubmed-4118872 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-41188722014-08-04 SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins Vörös, Aniko Simm, Roger Slamti, Leyla McKay, Matthew J. Hegna, Ida K. Nielsen-LeRoux, Christina Hassan, Karl A. Paulsen, Ian T. Lereclus, Didier Økstad, Ole Andreas Molloy, Mark P. Kolstø, Anne-Brit PLoS One Research Article The aim of this study was to explore the role of SecDF in protein secretion in Bacillus cereus ATCC 14579 by in-depth characterization of a markerless secDF knock out mutant. Deletion of secDF resulted in pleiotropic effects characterized by a moderately slower growth rate, aberrant cell morphology, enhanced susceptibility to xenobiotics, reduced virulence and motility. Most toxins, including food poisoning-associated enterotoxins Nhe, Hbl, and cytotoxin K, as well as phospholipase C were less abundant in the secretome of the ΔsecDF mutant as determined by label-free mass spectrometry. Global transcriptome studies revealed profound transcriptional changes upon deletion of secDF indicating cell envelope stress. Interestingly, the addition of glucose enhanced the described phenotypes. This study shows that SecDF is an important part of the Sec-translocase mediating efficient secretion of virulence factors in the Gram-positive opportunistic pathogen B. cereus, and further supports the notion that B. cereus enterotoxins are secreted by the Sec-system. Public Library of Science 2014-08-01 /pmc/articles/PMC4118872/ /pubmed/25083861 http://dx.doi.org/10.1371/journal.pone.0103326 Text en © 2014 Vörös et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Vörös, Aniko Simm, Roger Slamti, Leyla McKay, Matthew J. Hegna, Ida K. Nielsen-LeRoux, Christina Hassan, Karl A. Paulsen, Ian T. Lereclus, Didier Økstad, Ole Andreas Molloy, Mark P. Kolstø, Anne-Brit SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title | SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title_full | SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title_fullStr | SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title_full_unstemmed | SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title_short | SecDF as Part of the Sec-Translocase Facilitates Efficient Secretion of Bacillus cereus Toxins and Cell Wall-Associated Proteins |
title_sort | secdf as part of the sec-translocase facilitates efficient secretion of bacillus cereus toxins and cell wall-associated proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118872/ https://www.ncbi.nlm.nih.gov/pubmed/25083861 http://dx.doi.org/10.1371/journal.pone.0103326 |
work_keys_str_mv | AT vorosaniko secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT simmroger secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT slamtileyla secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT mckaymatthewj secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT hegnaidak secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT nielsenlerouxchristina secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT hassankarla secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT paulseniant secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT lereclusdidier secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT økstadoleandreas secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT molloymarkp secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins AT kolstøannebrit secdfaspartofthesectranslocasefacilitatesefficientsecretionofbacilluscereustoxinsandcellwallassociatedproteins |