Polyketide synthase (PKS) reduces fusion of Legionella pneumophila-containing vacuoles with lysosomes and contributes to bacterial competitiveness during infection

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dc.contributor.authorShevchuk, Olga
dc.contributor.authorPaegelow, Dennis
dc.contributor.authorRasch, Janine
dc.contributor.authorDöhrmann, Simon
dc.contributor.authorGünther, Gabriele
dc.contributor.authorHoppe, Julia
dc.contributor.authorSteinert, Michael
dc.contributor.authorÜnal, Can Murat
dc.contributor.authorBronietzki, Marc
dc.contributor.authorGutierrez, Maximiliano Gabriel
dc.date.accessioned2021-01-08T21:51:29Z
dc.date.available2021-01-08T21:51:29Z
dc.date.issued2014
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionUnal, Can/0000-0003-4710-9567; Gutierrez, Maximiliano/0000-0003-3199-0337en_US
dc.descriptionWOS:000347023400027en_US
dc.descriptionPubMed: 25218702en_US
dc.description.abstractL. pneumophila-containing vacuoles (LCVs) exclude endocytic and lysosomal markers in human macrophages and protozoa. We screened a L. pneumophila mini-Tn10 transposon library for mutants, which fail to inhibit the fusion of LCVs with lysosomes by loading of the lysosomal compartment with colloidal iron dextran, mechanical lysis of infected host cells, and magnetic isolation of LCVs that have fused with lysosomes. In silico analysis of the mutated genes, D. discoideum plaque assays and infection assays in protozoa and U937 macrophage-like cells identified well established as well as novel putative L. pneumophila virulence factors. Promising candidates were further analyzed for their colocalization with lysosomes in host cells using fluorescence microscopy. This approach corroborated that the O-methyltransferase, PilY1, TPR-containing protein and polyketide synthase (PKS) of L pneumophila interfere with lysosomal degradation. Competitive infections in protozoa and macrophages revealed that the identified PKS contributes to the biological fitness of pneumophila strains and may explain their prevalence in the epidemiology of Legionnaires' disease. (C) 2014 Elsevier GmbH. All rights reserved.
dc.description.sponsorshipGerman research society, DFGGerman Research Foundation (DFG) [STE838/6-1]
dc.description.sponsorshipFinancial support for this study was provided by the German research society, DFG (grant STE838/6-1). Barbara Schulz is greatly acknowledged for critical reading of the manuscript.
dc.identifier.doi10.1016/j.ijmm.2014.08.010
dc.identifier.endpage1181en_US
dc.identifier.issn1438-4221
dc.identifier.issn1618-0607
dc.identifier.issue8en_US
dc.identifier.scopus2-s2.0-84977814244
dc.identifier.scopusqualityQ2
dc.identifier.startpage1169en_US
dc.identifier.urihttp://doi.org/10.1016/j.ijmm.2014.08.010
dc.identifier.urihttps://hdl.handle.net/20.500.12846/300
dc.identifier.volume304en_US
dc.identifier.wosWOS:000347023400027
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorÜnal, Can Murat
dc.language.isoen
dc.publisherElsevier Gmbh, Urban & Fischer Verlag
dc.relation.ispartofInternational Journal Of Medical Microbiology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectLegionellaen_US
dc.subjectVirulenceen_US
dc.subjectTransposon Mutantsen_US
dc.subjectFitnessen_US
dc.subjectPksen_US
dc.titlePolyketide synthase (PKS) reduces fusion of Legionella pneumophila-containing vacuoles with lysosomes and contributes to bacterial competitiveness during infection
dc.typeArticle

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