2.50
Hdl Handle:
http://hdl.handle.net/10033/19559
Title:
Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes.
Authors:
Baumgärtner, Maja; Kärst, Uwe; Gerstel, Birgit; Loessner, Martin; Wehland, Jürgen; Jänsch, Lothar ( 0000-0002-5655-1181 )
Abstract:
Lipoprotein anchoring in bacteria is mediated by the prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the transfer of a diacylglyceryl moiety to the prospective N-terminal cysteine of the mature lipoprotein. Deletion of the lgt gene in the gram-positive pathogen Listeria monocytogenes (i) impairs intracellular growth of the bacterium in different eukaryotic cell lines and (ii) leads to increased release of lipoproteins into the culture supernatant. Comparative extracellular proteome analyses of the EGDe wild-type strain and the Delta lgt mutant provided systematic insight into the relative expression of lipoproteins. Twenty-six of the 68 predicted lipoproteins were specifically released into the extracellular proteome of the Delta lgt strain, and this proved that deletion of lgt is an excellent approach for experimental verification of listerial lipoproteins. Consequently, we generated Delta lgt Delta prfA double mutants to detect lipoproteins belonging to the main virulence regulon that is controlled by PrfA. Overall, we identified three lipoproteins whose extracellular levels are regulated and one lipoprotein that is posttranslationally modified depending on PrfA. It is noteworthy that in contrast to previous studies of Escherichia coli, we unambiguously demonstrated that lipidation by Lgt is not a prerequisite for activity of the lipoprotein-specific signal peptidase II (Lsp) in Listeria.
Affiliation:
Department of Cell Biology, Helmholtz Centre for Infection Research (HZI), D-38124 Braunschweig, Germany.
Citation:
Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes. 2007, 189 (2):313-24 J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
Jan-2007
URI:
http://hdl.handle.net/10033/19559
DOI:
10.1128/JB.00976-06
PubMed ID:
17041050
Type:
Article
Language:
en
ISSN:
0021-9193
Appears in Collections:
Publications of RG Cellular Proteome Research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorBaumgärtner, Majaen
dc.contributor.authorKärst, Uween
dc.contributor.authorGerstel, Birgiten
dc.contributor.authorLoessner, Martinen
dc.contributor.authorWehland, Jürgenen
dc.contributor.authorJänsch, Lotharen
dc.date.accessioned2008-03-03T15:44:11Zen
dc.date.available2008-03-03T15:44:11Zen
dc.date.issued2007-01en
dc.identifier.citationInactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes. 2007, 189 (2):313-24 J. Bacteriol.en
dc.identifier.issn0021-9193en
dc.identifier.pmid17041050en
dc.identifier.doi10.1128/JB.00976-06en
dc.identifier.urihttp://hdl.handle.net/10033/19559en
dc.description.abstractLipoprotein anchoring in bacteria is mediated by the prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the transfer of a diacylglyceryl moiety to the prospective N-terminal cysteine of the mature lipoprotein. Deletion of the lgt gene in the gram-positive pathogen Listeria monocytogenes (i) impairs intracellular growth of the bacterium in different eukaryotic cell lines and (ii) leads to increased release of lipoproteins into the culture supernatant. Comparative extracellular proteome analyses of the EGDe wild-type strain and the Delta lgt mutant provided systematic insight into the relative expression of lipoproteins. Twenty-six of the 68 predicted lipoproteins were specifically released into the extracellular proteome of the Delta lgt strain, and this proved that deletion of lgt is an excellent approach for experimental verification of listerial lipoproteins. Consequently, we generated Delta lgt Delta prfA double mutants to detect lipoproteins belonging to the main virulence regulon that is controlled by PrfA. Overall, we identified three lipoproteins whose extracellular levels are regulated and one lipoprotein that is posttranslationally modified depending on PrfA. It is noteworthy that in contrast to previous studies of Escherichia coli, we unambiguously demonstrated that lipidation by Lgt is not a prerequisite for activity of the lipoprotein-specific signal peptidase II (Lsp) in Listeria.en
dc.language.isoenen
dc.subject.mesh3T3 Cellsen
dc.subject.meshAnimalsen
dc.subject.meshAspartic Endopeptidasesen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCaco-2 Cellsen
dc.subject.meshComputational Biologyen
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen
dc.subject.meshGene Deletionen
dc.subject.meshGene Expression Regulation, Bacterialen
dc.subject.meshHumansen
dc.subject.meshLipoproteinsen
dc.subject.meshListeria monocytogenesen
dc.subject.meshMiceen
dc.subject.meshMicroscopy, Fluorescenceen
dc.subject.meshMutationen
dc.subject.meshOperonen
dc.subject.meshPeptide Termination Factorsen
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshTransferasesen
dc.subject.meshVirulenceen
dc.titleInactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes.en
dc.typeArticleen
dc.contributor.departmentDepartment of Cell Biology, Helmholtz Centre for Infection Research (HZI), D-38124 Braunschweig, Germany.en
dc.identifier.journalJournal of bacteriologyen

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