The Transcriptional Antiterminator RfaH Represses Biofilm Formation in Escherichia coli
Autor: | Jörg Hacker, Kai Michaelis, Karin Lindner, Paolo Landini, Christophe Beloin, Ulrich Dobrindt, Jean-Marc Ghigo |
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Přispěvatelé: | Génétique des Biofilms, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Bayerische Julius-Maximilians University, Swiss Federal Insitute of Aquatic Science and Technology [Dübendorf] (EAWAG), Fonds der Chemischen Industrie, Bayerische Forschungsstiftung, Fondation BNP Parisbas grants, We thank Jean-Claude Lazzaroni for help in constructing the LPS mutant in E. coli K-12 strains, Peter Owen for the gift of an Ag43 antiserum, and Shaynoor Dramsi for help with immunodetection experiments. We also thank Alexander J. B. Zehnder, Jennifer Leeds, Philippe Delepelaire, and Gábor Nagy for helpful discussions and critical reading of the manuscript. We thank Barbara Plaschke, Birgit Schellberg, and Teresa Colangelo for excellent technical assistance and Claude Lebos and Brigitte Arbeille (Laboratoire de Biologie Cellulaire et Microscopie Electronique, Tours, France) for preparation of the SEM micrographs., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2006 |
Předmět: |
Lipopolysaccharides
[SDV]Life Sciences [q-bio] Mutant MESH: Adhesins Escherichia coli MESH: Virulence medicine.disease_cause MESH: Down-Regulation Bacterial Adhesion MESH: Adhesins Bacterial/metabolism 0303 health sciences MESH: Escherichia coli/pathogenicity MESH: Gene Expression Regulation Bacterial Adhesins Escherichia coli Strain (chemistry) biology Virulence Escherichia coli Proteins MESH: Lipopolysaccharides/metabolism Enterobacteriaceae Phenotype MESH: Peptide Elongation Factors/physiology MESH: Escherichia coli/physiology MESH: Escherichia coli Proteins/physiology MESH: Peptide Elongation Factors/genetics Bacterial Outer Membrane Proteins MESH: Antigens Bacterial/metabolism MESH: Biofilms/growth & development Down-Regulation MESH: Escherichia coli/genetics Genetics and Molecular Biology Microbiology MESH: Escherichia coli Proteins/metabolism MESH: Trans-Activators/physiology 03 medical and health sciences MESH: Escherichia coli Proteins/genetics medicine Bacteriology Escherichia coli MESH: Bacterial Adhesion Adhesins Bacterial Molecular Biology 030304 developmental biology Antigens Bacterial MESH: Trans-Activators/genetics MESH: Bacterial Outer Membrane Proteins/metabolism 030306 microbiology Biofilm Gene Expression Regulation Bacterial biology.organism_classification Peptide Elongation Factors [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Biofilms Trans-Activators rpoS |
Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2006, 188 (4), pp.1316-1331. ⟨10.1128/JB.188.4.1316-1331.2006⟩ Journal of Bacteriology, 2006, 188 (4), pp.1316-1331. ⟨10.1128/JB.188.4.1316-1331.2006⟩ |
ISSN: | 0021-9193 1098-5530 |
DOI: | 10.1128/JB.188.4.1316-1331.2006⟩ |
Popis: | We investigated the influence of regulatory and pathogenicity island-associated factors (Hha, RpoS, LuxS, EvgA, RfaH, and tRNA 5 Leu ) on biofilm formation by uropathogenic Escherichia coli (UPEC) strain 536. Only inactivation of rfaH , which encodes a transcriptional antiterminator, resulted in increased initial adhesion and biofilm formation by E. coli 536. rfaH inactivation in nonpathogenic E. coli K-12 isolate MG1655 resulted in the same phenotype. Transcriptome analysis of wild-type strain 536 and an rfaH mutant of this strain revealed that deletion of rfaH correlated with increased expression of flu orthologs. flu encodes antigen 43 (Ag43), which mediates autoaggregation and biofilm formation. We confirmed that deletion of rfaH leads to increased levels of flu and flu -like transcripts in E. coli K-12 and UPEC. Supporting the hypothesis that RfaH represses biofilm formation through reduction of the Ag43 level, the increased-biofilm phenotype of E. coli MG1655 rfaH was reversed upon inactivation of flu . Deletion of the two flu orthologs, however, did not modify the behavior of mutant 536 rfaH . Our results demonstrate that the strong initial adhesion and biofilm formation capacities of strain MG1655 rfaH are mediated by both increased steady-state production of Ag43 and likely increased Ag43 presentation due to null rfaH -dependent lipopolysaccharide depletion. Although the roles of rfaH in the biofilm phenotype are different in UPEC strain 536 and K-12 strain MG1655, this study shows that RfaH, in addition to affecting the expression of bacterial virulence factors, also negatively controls expression and surface presentation of Ag43 and possibly another Ag43-independent factor(s) that mediates cell-cell interactions and biofilm formation. |
Databáze: | OpenAIRE |
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