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    Non-antibiotic quorum sensing inhibitors acting against N-acyl homoserine lactone synthase as druggable target

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    Chang_Scientific_Reports.pdf (2.037Mb)
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    Publication date
    2014-11
    Author
    Chang, Chien-Yi
    Krishnan, T.
    Wang, H.
    Chen, Y.
    Yin, W.
    Chong, Y.
    Tan, L.Y.
    Chong, T.M.
    Chan, K.
    Keyword
    N-acylhomoserine lactone (AHL); Non-antibiotic quorum sensing; Escherichia coli; QS-inhibiting agents
    Rights
    © 2014 The Authors. Reproduced in accordance with the publisher's selfarchiving policy. This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/
    Peer-Reviewed
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    Abstract
    N-acylhomoserine lactone (AHL)-based quorum sensing (QS) is important for the regulation of proteobacterial virulence determinants. Thus, the inhibition of AHL synthases offers non-antibiotics-based therapeutic potentials against QS-mediated bacterial infections. In this work, functional AHL synthases of Pseudomonas aeruginosa LasI and RhlI were heterologously expressed in an AHL-negative Escherichia coli followed by assessments on their AHLs production using AHL biosensors and high resolution liquid chromatography–mass spectrometry (LCMS). These AHL-producing E. coli served as tools for screening AHL synthase inhibitors. Based on a campaign of screening synthetic molecules and natural products using our approach, three strongest inhibitors namely are salicylic acid, tannic acid and trans-cinnamaldehyde have been identified. LCMS analysis further confirmed tannic acid and trans-cinnemaldehyde efficiently inhibited AHL production by RhlI. We further demonstrated the application of trans-cinnemaldehyde inhibiting Rhl QS system regulated pyocyanin production in P. aeruginosa up to 42.06%. Molecular docking analysis suggested that trans-cinnemaldehyde binds to the LasI and EsaI with known structures mainly interacting with their substrate binding sites. Our data suggested a new class of QS-inhibiting agents from natural products targeting AHL synthase and provided a potential approach for facilitating the discovery of anti-QS signal synthesis as basis of novel anti-infective approach.
    URI
    http://hdl.handle.net/10454/15066
    Version
    Published version
    Citation
    Chang C, Krishnan T, Wang H et al (2014) Non-antibiotic quorum sensing inhibitors acting against N-acyl homoserine lactone synthase as druggable target. Scientific Reports. 4:7245.
    Link to publisher’s version
    http://dx.doi.org/10.1038/srep07245
    Type
    Article
    Collections
    Life Sciences Publications

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