Staphylococcus epidermidis bacteriocin A37 kills natural competitors with a unique mechanism of action.

Autor:	Puls JS; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany., Winnerling B; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany.; German Center for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany., Power JJ; Interfaculty Institute of Microbiology and Infection Medicine, Department of Infection Biology, University of Tübingen, 72076 Tübingen, Germany., Krüger AM; Clausius Institute of Physical and Theoretical Chemistry, University of Bonn, 53115 Bonn, Germany., Brajtenbach D; Clausius Institute of Physical and Theoretical Chemistry, University of Bonn, 53115 Bonn, Germany., Johnson M; Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Bilici K; Interfaculty Institute of Microbiology and Infection Medicine, Department of Infection Biology, University of Tübingen, 72076 Tübingen, Germany., Camus L; Interfaculty Institute of Microbiology and Infection Medicine, Department of Infection Biology, University of Tübingen, 72076 Tübingen, Germany., Fließwasser T; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany.; German Center for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany., Schneider T; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany.; German Center for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany., Sahl HG; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany., Ghosal D; Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Kubitscheck U; Clausius Institute of Physical and Theoretical Chemistry, University of Bonn, 53115 Bonn, Germany., Heilbronner S; Interfaculty Institute of Microbiology and Infection Medicine, Department of Infection Biology, University of Tübingen, 72076 Tübingen, Germany.; German Centre for Infection Research (DZIF), Partner Site Tübingen, 72076 Tübingen, Germany.; Present address: Faculty of Biology, Microbiology, Ludwig-Maximilians-University of Munich, 82152 München, Germany., Grein F; Institute for Pharmaceutical Microbiology, University Hospital Bonn, University of Bonn, 53115 Bonn, Germany.; German Center for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany.
Jazyk:	angličtina
Zdroj:	The ISME journal [ISME J] 2024 Jan 08; Vol. 18 (1).
DOI:	10.1093/ismejo/wrae044
Abstrakt:	Many bacteria produce antimicrobial compounds such as lantibiotics to gain advantage in the competitive natural environments of microbiomes. Epilancins constitute an until now underexplored family of lantibiotics with an unknown ecological role and unresolved mode of action. We discovered production of an epilancin in the nasal isolate Staphylococcus epidermidis A37. Using bioinformatic tools, we found that epilancins are frequently encoded within staphylococcal genomes, highlighting their ecological relevance. We demonstrate that production of epilancin A37 contributes to Staphylococcus epidermidis competition specifically against natural corynebacterial competitors. Combining microbiological approaches with quantitative in vivo and in vitro fluorescence microscopy and cryo-electron tomography, we show that A37 enters the corynebacterial cytoplasm through a partially transmembrane-potential-driven uptake without impairing the cell membrane function. Upon intracellular aggregation, A37 induces the formation of intracellular membrane vesicles, which are heavily loaded with the compound and are essential for the antibacterial activity of the epilancin. Our work sheds light on the ecological role of epilancins for staphylococci mediated by a mode of action previously unknown for lantibiotics. (© The Author(s) 2024. Published by Oxford University Press on behalf of the International Society for Microbial Ecology.)
Databáze:	MEDLINE
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