Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces

We report the isolation of N-acyl homoserine lactone-producing Enterobacter sp. isolate T1-1 from the posterior dorsal surfaces of the tongue of a healthy individual. Spent supernatants extract from Enterobacter sp. isolate T1-1 activated the biosensor Agrobacterium tumefaciens NTL4(pZLR4), suggesti...

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Autores principales: Yin, Wai-Fong, Purmal, Kathiravan, Chin, Shenyang, Chan, Xin-Yue, Chan, Kok-Gan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3522914/
https://www.ncbi.nlm.nih.gov/pubmed/23202161
http://dx.doi.org/10.3390/s121114307
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author Yin, Wai-Fong
Purmal, Kathiravan
Chin, Shenyang
Chan, Xin-Yue
Chan, Kok-Gan
author_facet Yin, Wai-Fong
Purmal, Kathiravan
Chin, Shenyang
Chan, Xin-Yue
Chan, Kok-Gan
author_sort Yin, Wai-Fong
collection PubMed
description We report the isolation of N-acyl homoserine lactone-producing Enterobacter sp. isolate T1-1 from the posterior dorsal surfaces of the tongue of a healthy individual. Spent supernatants extract from Enterobacter sp. isolate T1-1 activated the biosensor Agrobacterium tumefaciens NTL4(pZLR4), suggesting production of long chain AHLs by these isolates. High resolution mass spectrometry analysis of these extracts confirmed that Enterobacter sp. isolate T1-1 produced a long chain N-acyl homoserine lactone, namely N-dodecanoyl-homoserine lactone (C12-HSL). To the best of our knowledge, this is the first isolation of Enterobacter sp., strain T1-1 from the posterior dorsal surface of the human tongue and N-acyl homoserine lactones production by this bacterium.
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spelling pubmed-35229142013-01-09 Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces Yin, Wai-Fong Purmal, Kathiravan Chin, Shenyang Chan, Xin-Yue Chan, Kok-Gan Sensors (Basel) Article We report the isolation of N-acyl homoserine lactone-producing Enterobacter sp. isolate T1-1 from the posterior dorsal surfaces of the tongue of a healthy individual. Spent supernatants extract from Enterobacter sp. isolate T1-1 activated the biosensor Agrobacterium tumefaciens NTL4(pZLR4), suggesting production of long chain AHLs by these isolates. High resolution mass spectrometry analysis of these extracts confirmed that Enterobacter sp. isolate T1-1 produced a long chain N-acyl homoserine lactone, namely N-dodecanoyl-homoserine lactone (C12-HSL). To the best of our knowledge, this is the first isolation of Enterobacter sp., strain T1-1 from the posterior dorsal surface of the human tongue and N-acyl homoserine lactones production by this bacterium. Molecular Diversity Preservation International (MDPI) 2012-10-24 /pmc/articles/PMC3522914/ /pubmed/23202161 http://dx.doi.org/10.3390/s121114307 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Yin, Wai-Fong
Purmal, Kathiravan
Chin, Shenyang
Chan, Xin-Yue
Chan, Kok-Gan
Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title_full Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title_fullStr Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title_full_unstemmed Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title_short Long Chain N-acyl Homoserine Lactone Production by Enterobacter sp. Isolated from Human Tongue Surfaces
title_sort long chain n-acyl homoserine lactone production by enterobacter sp. isolated from human tongue surfaces
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3522914/
https://www.ncbi.nlm.nih.gov/pubmed/23202161
http://dx.doi.org/10.3390/s121114307
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