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N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels
N-acetyl glucosamine, the monomer of chitin, is an abundant source of carbon and nitrogen in nature as it is the main component and breakdown product of many structural polymers. Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in orde...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4993992/ https://www.ncbi.nlm.nih.gov/pubmed/27602027 http://dx.doi.org/10.3389/fmicb.2016.01313 |
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author | Kimyon, Önder Ulutürk, Zehra İ. Nizalapur, Shashidhar Lee, Matthew Kutty, Samuel K. Beckmann, Sabrina Kumar, Naresh Manefield, Mike |
author_facet | Kimyon, Önder Ulutürk, Zehra İ. Nizalapur, Shashidhar Lee, Matthew Kutty, Samuel K. Beckmann, Sabrina Kumar, Naresh Manefield, Mike |
author_sort | Kimyon, Önder |
collection | PubMed |
description | N-acetyl glucosamine, the monomer of chitin, is an abundant source of carbon and nitrogen in nature as it is the main component and breakdown product of many structural polymers. Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in order to catalyze the cleavage of chitin polymers into water soluble N-acetyl-D-glucosamine (NAG) monomers. In this study, the impact of NAG on QS activities of LuxR, LasR, and CviR regulated gene expression was investigated by examining the effect of NAG on QS regulated green fluorescent protein (GFP), violacein and extracellular chitinase expression. It was discovered that NAG inhibits AHL dependent gene transcription in AHL reporter strains within the range of 50–80% reduction at low millimolar concentrations (0.25–5 mM). Evidence is presented supporting a role for both competitive inhibition at the AHL binding site of LuxR type transcriptional regulators and catabolite repression. Further, this study shows that NAG down-regulates CviR induced violacein production while simultaneously up-regulating CviR dependent extracellular enzymes, suggesting that an unknown NAG dependent regulatory component influences phenotype expression. The quorum sensing inhibiting activity of NAG also adds to the list of compounds with known quorum sensing inhibiting activities. |
format | Online Article Text |
id | pubmed-4993992 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49939922016-09-06 N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels Kimyon, Önder Ulutürk, Zehra İ. Nizalapur, Shashidhar Lee, Matthew Kutty, Samuel K. Beckmann, Sabrina Kumar, Naresh Manefield, Mike Front Microbiol Microbiology N-acetyl glucosamine, the monomer of chitin, is an abundant source of carbon and nitrogen in nature as it is the main component and breakdown product of many structural polymers. Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in order to catalyze the cleavage of chitin polymers into water soluble N-acetyl-D-glucosamine (NAG) monomers. In this study, the impact of NAG on QS activities of LuxR, LasR, and CviR regulated gene expression was investigated by examining the effect of NAG on QS regulated green fluorescent protein (GFP), violacein and extracellular chitinase expression. It was discovered that NAG inhibits AHL dependent gene transcription in AHL reporter strains within the range of 50–80% reduction at low millimolar concentrations (0.25–5 mM). Evidence is presented supporting a role for both competitive inhibition at the AHL binding site of LuxR type transcriptional regulators and catabolite repression. Further, this study shows that NAG down-regulates CviR induced violacein production while simultaneously up-regulating CviR dependent extracellular enzymes, suggesting that an unknown NAG dependent regulatory component influences phenotype expression. The quorum sensing inhibiting activity of NAG also adds to the list of compounds with known quorum sensing inhibiting activities. Frontiers Media S.A. 2016-08-23 /pmc/articles/PMC4993992/ /pubmed/27602027 http://dx.doi.org/10.3389/fmicb.2016.01313 Text en Copyright © 2016 Kimyon, Ulutürk, Nizalapur, Lee, Kutty, Beckmann, Kumar and Manefield. 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 Kimyon, Önder Ulutürk, Zehra İ. Nizalapur, Shashidhar Lee, Matthew Kutty, Samuel K. Beckmann, Sabrina Kumar, Naresh Manefield, Mike N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title | N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title_full | N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title_fullStr | N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title_full_unstemmed | N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title_short | N-Acetylglucosamine Inhibits LuxR, LasR and CviR Based Quorum Sensing Regulated Gene Expression Levels |
title_sort | n-acetylglucosamine inhibits luxr, lasr and cvir based quorum sensing regulated gene expression levels |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4993992/ https://www.ncbi.nlm.nih.gov/pubmed/27602027 http://dx.doi.org/10.3389/fmicb.2016.01313 |
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