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Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium
Quorum sensing (QS) is a density-dependent mechanism allowing bacteria to synchronize their physiological activities, mediated by a wide range of signaling molecules including N-acyl-homoserine lactones (AHLs). Production of AHL has been identified in various marine strains of Proteobacteria. Howeve...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5479921/ https://www.ncbi.nlm.nih.gov/pubmed/28690598 http://dx.doi.org/10.3389/fmicb.2017.01152 |
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author | Doberva, Margot Stien, Didier Sorres, Jonathan Hue, Nathalie Sanchez-Ferandin, Sophie Eparvier, Véronique Ferandin, Yoan Lebaron, Philippe Lami, Raphaël |
author_facet | Doberva, Margot Stien, Didier Sorres, Jonathan Hue, Nathalie Sanchez-Ferandin, Sophie Eparvier, Véronique Ferandin, Yoan Lebaron, Philippe Lami, Raphaël |
author_sort | Doberva, Margot |
collection | PubMed |
description | Quorum sensing (QS) is a density-dependent mechanism allowing bacteria to synchronize their physiological activities, mediated by a wide range of signaling molecules including N-acyl-homoserine lactones (AHLs). Production of AHL has been identified in various marine strains of Proteobacteria. However, the chemical diversity of these molecules still needs to be further explored. In this study, we examined the diversity of AHLs produced by strain MOLA 401, a marine Alphaproteobacterium that belongs to the ubiquitous Rhodobacteraceae family. We combined an original biosensors-based guided screening of extract microfractions with liquid chromatography coupled to mass spectrometry (MS), High Resolution MS/MS and Nuclear Magnetic Resonance. This approach revealed the unsuspected capacity of a single Rhodobacteraceae strain to synthesize 20 different compounds, which are most likely AHLs. Also, some of these AHLs possessed original features that have never been previously observed, including long (up to 19 carbons) and poly-hydroxylated acyl side chains, revealing new molecular adaptations of QS to planktonic life and a larger molecular diversity than expected of molecules involved in cell–cell signaling within a single strain. |
format | Online Article Text |
id | pubmed-5479921 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54799212017-07-07 Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium Doberva, Margot Stien, Didier Sorres, Jonathan Hue, Nathalie Sanchez-Ferandin, Sophie Eparvier, Véronique Ferandin, Yoan Lebaron, Philippe Lami, Raphaël Front Microbiol Microbiology Quorum sensing (QS) is a density-dependent mechanism allowing bacteria to synchronize their physiological activities, mediated by a wide range of signaling molecules including N-acyl-homoserine lactones (AHLs). Production of AHL has been identified in various marine strains of Proteobacteria. However, the chemical diversity of these molecules still needs to be further explored. In this study, we examined the diversity of AHLs produced by strain MOLA 401, a marine Alphaproteobacterium that belongs to the ubiquitous Rhodobacteraceae family. We combined an original biosensors-based guided screening of extract microfractions with liquid chromatography coupled to mass spectrometry (MS), High Resolution MS/MS and Nuclear Magnetic Resonance. This approach revealed the unsuspected capacity of a single Rhodobacteraceae strain to synthesize 20 different compounds, which are most likely AHLs. Also, some of these AHLs possessed original features that have never been previously observed, including long (up to 19 carbons) and poly-hydroxylated acyl side chains, revealing new molecular adaptations of QS to planktonic life and a larger molecular diversity than expected of molecules involved in cell–cell signaling within a single strain. Frontiers Media S.A. 2017-06-22 /pmc/articles/PMC5479921/ /pubmed/28690598 http://dx.doi.org/10.3389/fmicb.2017.01152 Text en Copyright © 2017 Doberva, Stien, Sorres, Hue, Sanchez-Ferandin, Eparvier, Ferandin, Lebaron and Lami. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Doberva, Margot Stien, Didier Sorres, Jonathan Hue, Nathalie Sanchez-Ferandin, Sophie Eparvier, Véronique Ferandin, Yoan Lebaron, Philippe Lami, Raphaël Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title | Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title_full | Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title_fullStr | Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title_full_unstemmed | Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title_short | Large Diversity and Original Structures of Acyl-Homoserine Lactones in Strain MOLA 401, a Marine Rhodobacteraceae Bacterium |
title_sort | large diversity and original structures of acyl-homoserine lactones in strain mola 401, a marine rhodobacteraceae bacterium |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5479921/ https://www.ncbi.nlm.nih.gov/pubmed/28690598 http://dx.doi.org/10.3389/fmicb.2017.01152 |
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