Formyl peptide receptor-mediated proinflammatory consequences of peptide deformylase inhibition in Staphylococcus aureus |
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| Authors: | Diana Mader Marie-Joséphe Rabiet Francois Boulay Andreas Peschel |
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| Affiliation: | 1. Cellular and Molecular Microbiology Division, Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Elfriede-Aulhorn-Straße 6, 72076 Tübingen, Germany;2. CEA, DSV, iRTSV, Laboratoire Biochimie et Biophysique des Systèmes Intégrés, 17 rue des Martyrs, Grenoble F-38054, France;3. CNRS, UMR 5092, Grenoble F-38054, France;4. Université Joseph Fourier, Grenoble, F-38000, France;1. Infection Biology, Interfaculty Institute for Microbiology and Infection Medicine Tübingen (IMIT), University of Tübingen, Auf der Morgenstelle 28, 72076 Tübingen, Germany;1. State Key Laboratory of Organic-Inorganic Composites, Beijing University of Chemical Technology, Beijing 100029, China;2. Research Center of the Ministry of Education for High Gravity Engineering & Technology, Beijing University of Chemical Technology, Beijing 100029, China;3. General Research Institute for Nonferrous Metals, Beijing 100088, China;4. Department of Materials Science and Engineering, University of WA, Seattle, WA 98195, USA;1. Division of Allergy, Immunology and Rheumatology, Department of Pediatrics, University of North Carolina School of Medicine, Chapel Hill, NC;2. Section of Allergy, Immunology, Pulmonary, Critical Care, and Sleep Medicine, University of Wisconsin School of Medicine and Public Health, Madison, Wis;1. Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kracow, Poland;2. NanoTechnas–Center of Nanotechnology and Materials Science, Faculty of Chemistry, Vilnius University, Naugarduko St. 24, LT-03225 Vilnius, Lithuania;3. Laboratory of NanoBioTechnology, Institute of Semiconductor Physics, State Research Institute Centre for Physical and Technological Sciences, A. Gostauto g. 11, LT-01108 Vilnius, Lithuania;4. Department of Physical Chemistry, Faculty of Chemistry, Vilnius University, Naugarduko St. 24, LT-03225 Vilnius, Lithuania;1. Department of Cell Biology and Histology, Faculty of Biology, Campus Regional de Excelencia Internacional “Campus Mare Nostrum”, University of Murcia, 30100, Murcia, Spain;2. Department of Physical Chemistry, Faculty of Chemistry, Campus Regional de Excelencia Internacional “Campus Mare Nostrum”, University of Murcia, 30100, Murcia, Spain;1. Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India;2. RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan;3. Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan;4. RIKEN Systems and Structural Biology Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan;5. Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan |
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| Abstract: | The biosynthesis of proteins with N-terminal formylated methionine residues and subsequent protein deformylation are unique and invariant bacterial processes. They are exploited by the capacity of the human innate immune system to sense formylated peptides (FPs) and targeted by the deformylation-blocking antibiotic actinonin. We show that human polymorphonuclear leukocytes respond via the formyl peptide receptor (FPR) with increased calcium ion fluxes, chemotactic migration, IL-8 release, and CD11b upregulation to the human pathogen Staphylococcus aureus upon actinonin treatment. These data underscore the crucial role of bacterial FPs in innate immunity and indicate that deformylase inhibition may have considerable proinflammatory consequences. |
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