AhR sensing of bacterial pigments regulates antibacterial defence

Pedro Moura-Alves, Kellen Faé, Erica Houthuys, Anca Dorhoi, Annika Kreuchwig, Jens Furkert, Nicola Barison, Anne Diehl, Antje Munder, Patricia Constant, Tatsiana Skrahina, Ute Guhlich-Bornhof, Marion Klemm, Anne-Britta Koehler, Silke Bandermann, Christian Goosmann, Hans-Joachim Mollenkopf, Robert Hurwitz, Volker Brinkmann, Simon Fillatreau, Mamadou Daffe, Burkhard Tümmler, Michael Kolbe, Hartmut Oschkinat, Gerd Krause and Stefan H. E. Kaufmann ()
Additional contact information
Pedro Moura-Alves: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Kellen Faé: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Erica Houthuys: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Anca Dorhoi: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Annika Kreuchwig: Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
Jens Furkert: Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
Nicola Barison: Max Planck Institute for Infection Biology, Structural Systems Biology, Charitéplatz 1, 10117 Berlin, Germany
Anne Diehl: Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
Antje Munder: Clinical Research Group, Clinic for Pediatric Pneumology, Allergology and Neonatology, OE 6710, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany
Patricia Constant: Institute of Pharmacology and Structural Biology (IPBS), CNRS and University of Toulouse (Toulouse III), 205 Route de Narbonne, 31077, Toulouse cedex 04, Toulouse, France
Tatsiana Skrahina: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Ute Guhlich-Bornhof: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Marion Klemm: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Anne-Britta Koehler: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Silke Bandermann: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Christian Goosmann: Microscopy Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Hans-Joachim Mollenkopf: Microarray Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Robert Hurwitz: Protein Purification Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Volker Brinkmann: Microscopy Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany
Simon Fillatreau: German Rheumatism Research Centre Berlin (DRFZ), a Leibniz Institute, Charitéplatz 1, 10117 Berlin, Germany
Mamadou Daffe: Institute of Pharmacology and Structural Biology (IPBS), CNRS and University of Toulouse (Toulouse III), 205 Route de Narbonne, 31077, Toulouse cedex 04, Toulouse, France
Burkhard Tümmler: Clinical Research Group, Clinic for Pediatric Pneumology, Allergology and Neonatology, OE 6710, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany
Michael Kolbe: Max Planck Institute for Infection Biology, Structural Systems Biology, Charitéplatz 1, 10117 Berlin, Germany
Hartmut Oschkinat: Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
Gerd Krause: Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany
Stefan H. E. Kaufmann: Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany

Nature, 2014, vol. 512, issue 7515, 387-392

Abstract: Abstract The aryl hydrocarbon receptor (AhR) is a highly conserved ligand-dependent transcription factor that senses environmental toxins and endogenous ligands, thereby inducing detoxifying enzymes and modulating immune cell differentiation and responses. We hypothesized that AhR evolved to sense not only environmental pollutants but also microbial insults. We characterized bacterial pigmented virulence factors, namely the phenazines from Pseudomonas aeruginosa and the naphthoquinone phthiocol from Mycobacterium tuberculosis, as ligands of AhR. Upon ligand binding, AhR activation leads to virulence factor degradation and regulated cytokine and chemokine production. The relevance of AhR to host defence is underlined by heightened susceptibility of AhR-deficient mice to both P. aeruginosa and M. tuberculosis. Thus, we demonstrate that AhR senses distinct bacterial virulence factors and controls antibacterial responses, supporting a previously unidentified role for AhR as an intracellular pattern recognition receptor, and identify bacterial pigments as a new class of pathogen-associated molecular patterns.

Date: 2014
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DOI: 10.1038/nature13684

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