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SecDF as part of the Sec-translocase facilitates efficient secretion of Bacillus cereus toxins and cell wall-associated proteins.

Identifieur interne : 003203 ( PubMed/Checkpoint ); précédent : 003202; suivant : 003204

SecDF as part of the Sec-translocase facilitates efficient secretion of Bacillus cereus toxins and cell wall-associated proteins.

Auteurs : Aniko Vörös [Norvège] ; Roger Simm [Norvège] ; Leyla Slamti [France] ; Matthew J. Mckay [Australie] ; Ida K. Hegna [Norvège] ; Christina Nielsen-Leroux [France] ; Karl A. Hassan [Australie] ; Ian T. Paulsen [Australie] ; Didier Lereclus [France] ; Ole Andreas Kstad [Norvège] ; Mark P. Molloy [Australie] ; Anne-Brit Kolst [Norvège]

Source :

RBID : pubmed:25083861

Descripteurs français

English descriptors

Abstract

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.

DOI: 10.1371/journal.pone.0103326
PubMed: 25083861


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pubmed:25083861

Le document en format XML

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<term>Bacterial Proteins (genetics)</term>
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<term>Bacillus cereus (ultrastructure)</term>
<term>Mutation</term>
<term>Papillons de nuit (microbiologie)</term>
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<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
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<term>Résistance bactérienne aux médicaments (génétique)</term>
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<term>Papillons de nuit</term>
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<term>Moths</term>
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<term>Xenobiotics</term>
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<term>Bacillus cereus</term>
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<term>Bacillus cereus</term>
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<term>Régulation de l'expression des gènes bactériens</term>
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<div type="abstract" xml:lang="en">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.</div>
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<pubmed>
<MedlineCitation Status="MEDLINE" Owner="NLM">
<PMID Version="1">25083861</PMID>
<DateCreated>
<Year>2014</Year>
<Month>08</Month>
<Day>02</Day>
</DateCreated>
<DateCompleted>
<Year>2015</Year>
<Month>04</Month>
<Day>23</Day>
</DateCompleted>
<DateRevised>
<Year>2017</Year>
<Month>02</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Electronic-eCollection">
<Journal>
<ISSN IssnType="Electronic">1932-6203</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>9</Volume>
<Issue>8</Issue>
<PubDate>
<Year>2014</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
<ISOAbbreviation>PLoS ONE</ISOAbbreviation>
</Journal>
<ArticleTitle>SecDF as part of the Sec-translocase facilitates efficient secretion of Bacillus cereus toxins and cell wall-associated proteins.</ArticleTitle>
<Pagination>
<MedlinePgn>e103326</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0103326</ELocationID>
<Abstract>
<AbstractText>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.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Vörös</LastName>
<ForeName>Aniko</ForeName>
<Initials>A</Initials>
<AffiliationInfo>
<Affiliation>Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Simm</LastName>
<ForeName>Roger</ForeName>
<Initials>R</Initials>
<AffiliationInfo>
<Affiliation>Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Slamti</LastName>
<ForeName>Leyla</ForeName>
<Initials>L</Initials>
<AffiliationInfo>
<Affiliation>INRA, UMR1319 Micalis, Domaine de La Minière, Guyancourt, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>McKay</LastName>
<ForeName>Matthew J</ForeName>
<Initials>MJ</Initials>
<AffiliationInfo>
<Affiliation>Australian Proteome Analysis Facility (APAF), Macquarie University, Sydney, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Hegna</LastName>
<ForeName>Ida K</ForeName>
<Initials>IK</Initials>
<AffiliationInfo>
<Affiliation>Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Nielsen-LeRoux</LastName>
<ForeName>Christina</ForeName>
<Initials>C</Initials>
<AffiliationInfo>
<Affiliation>INRA, UMR1319 Micalis, Domaine de La Minière, Guyancourt, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Hassan</LastName>
<ForeName>Karl A</ForeName>
<Initials>KA</Initials>
<AffiliationInfo>
<Affiliation>Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Paulsen</LastName>
<ForeName>Ian T</ForeName>
<Initials>IT</Initials>
<AffiliationInfo>
<Affiliation>Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Lereclus</LastName>
<ForeName>Didier</ForeName>
<Initials>D</Initials>
<AffiliationInfo>
<Affiliation>INRA, UMR1319 Micalis, Domaine de La Minière, Guyancourt, France; AgroParistech, UMR Micalis, Jouy-en-Josas, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Økstad</LastName>
<ForeName>Ole Andreas</ForeName>
<Initials>OA</Initials>
<AffiliationInfo>
<Affiliation>Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Molloy</LastName>
<ForeName>Mark P</ForeName>
<Initials>MP</Initials>
<AffiliationInfo>
<Affiliation>Australian Proteome Analysis Facility (APAF), Macquarie University, Sydney, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Kolstø</LastName>
<ForeName>Anne-Brit</ForeName>
<Initials>AB</Initials>
<AffiliationInfo>
<Affiliation>Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2014</Year>
<Month>08</Month>
<Day>01</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>United States</Country>
<MedlineTA>PLoS One</MedlineTA>
<NlmUniqueID>101285081</NlmUniqueID>
<ISSNLinking>1932-6203</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001427">Bacterial Toxins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D015262">Xenobiotics</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
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<PMID Version="1">20942974</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Genet. 2002 Dec;32 Suppl:509-14</RefSource>
<PMID Version="1">12454646</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>PLoS One. 2011;6(4):e18902</RefSource>
<PMID Version="1">21526150</PMID>
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