The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.

T2R38 has been shown to be a specific bacterial detector implicated in innate immune defense mechanism of human upper airway. Several clinical studies have demonstrated that this receptor is associated with the development of chronic rhinosinusitis (CRS). T2R38 was previously reported to bind to hom...

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Main Authors: Christophe Verbeurgt, Alex Veithen, Sébastien Carlot, Maxime Tarabichi, Jacques E Dumont, Sergio Hassid, Pierre Chatelain
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5597121?pdf=render
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author Christophe Verbeurgt
Alex Veithen
Sébastien Carlot
Maxime Tarabichi
Jacques E Dumont
Sergio Hassid
Pierre Chatelain
author_facet Christophe Verbeurgt
Alex Veithen
Sébastien Carlot
Maxime Tarabichi
Jacques E Dumont
Sergio Hassid
Pierre Chatelain
author_sort Christophe Verbeurgt
collection DOAJ
description T2R38 has been shown to be a specific bacterial detector implicated in innate immune defense mechanism of human upper airway. Several clinical studies have demonstrated that this receptor is associated with the development of chronic rhinosinusitis (CRS). T2R38 was previously reported to bind to homoserine lactones (HSL), quorum sensing molecules specific of Pseudomonas Aeruginosa and other gram negative species. Nevertheless, these bacteria are not the major pathogens found in CRS. Here we report on the identification of bacterial metabolites acting as new agonists of T2R38 based on a single cell calcium imaging study. Two quorum sensing molecules (Agr D1 thiolactone from Staphylococcus Aureus and CSP-1 from Streptococcus Pneumoniae) and a list of 32 bacterial metabolites from pathogens frequently implicated in CRS were tested. First, we observed that HSL failed to activate T2R38 in our experimental system, but that the dimethylsulfoxide (DMSO), used as a solvent for these lactones may, by itself, account for the agonistic effect previously described. Secondly, we showed that both Agr D1 thiolactone and CSP-1 are inactive but that at least 7 bacterial metabolites (acetone, 2-butanone, 2-pentanone, 2-methylpropanal, dimethyl disulfide, methylmercaptan, γ-butyrolactone) are able to specifically trigger this receptor. T2R38 is thus much more broadly tuned for bacterial compounds than previously thought.
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spelling doaj.art-ed08c05c466b4d7781f3b0b8940f609d2022-12-21T22:58:50ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01129e018130210.1371/journal.pone.0181302The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.Christophe VerbeurgtAlex VeithenSébastien CarlotMaxime TarabichiJacques E DumontSergio HassidPierre ChatelainT2R38 has been shown to be a specific bacterial detector implicated in innate immune defense mechanism of human upper airway. Several clinical studies have demonstrated that this receptor is associated with the development of chronic rhinosinusitis (CRS). T2R38 was previously reported to bind to homoserine lactones (HSL), quorum sensing molecules specific of Pseudomonas Aeruginosa and other gram negative species. Nevertheless, these bacteria are not the major pathogens found in CRS. Here we report on the identification of bacterial metabolites acting as new agonists of T2R38 based on a single cell calcium imaging study. Two quorum sensing molecules (Agr D1 thiolactone from Staphylococcus Aureus and CSP-1 from Streptococcus Pneumoniae) and a list of 32 bacterial metabolites from pathogens frequently implicated in CRS were tested. First, we observed that HSL failed to activate T2R38 in our experimental system, but that the dimethylsulfoxide (DMSO), used as a solvent for these lactones may, by itself, account for the agonistic effect previously described. Secondly, we showed that both Agr D1 thiolactone and CSP-1 are inactive but that at least 7 bacterial metabolites (acetone, 2-butanone, 2-pentanone, 2-methylpropanal, dimethyl disulfide, methylmercaptan, γ-butyrolactone) are able to specifically trigger this receptor. T2R38 is thus much more broadly tuned for bacterial compounds than previously thought.http://europepmc.org/articles/PMC5597121?pdf=render
spellingShingle Christophe Verbeurgt
Alex Veithen
Sébastien Carlot
Maxime Tarabichi
Jacques E Dumont
Sergio Hassid
Pierre Chatelain
The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
PLoS ONE
title The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
title_full The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
title_fullStr The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
title_full_unstemmed The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
title_short The human bitter taste receptor T2R38 is broadly tuned for bacterial compounds.
title_sort human bitter taste receptor t2r38 is broadly tuned for bacterial compounds
url http://europepmc.org/articles/PMC5597121?pdf=render
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