Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89083
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dc.contributor.authorSeviour, Thomasen
dc.contributor.authorHansen, Susan Hoveen
dc.contributor.authorYang, Liangen
dc.contributor.authorYau, Yin Hoeen
dc.contributor.authorWang, Victor Bochuanen
dc.contributor.authorStenvang, Marcel R.en
dc.contributor.authorChristiansen, Gunnaen
dc.contributor.authorMarsili, Enricoen
dc.contributor.authorGivskov, Michaelen
dc.contributor.authorChen, Yicaien
dc.contributor.authorOtzen, Daniel E.en
dc.contributor.authorNielsen, Per Halkjæren
dc.contributor.authorGeifman-Shochat, Susanaen
dc.contributor.authorKjelleberg, Staffanen
dc.contributor.authorDueholm, Morten S.en
dc.date.accessioned2018-09-20T03:59:16Zen
dc.date.accessioned2019-12-06T17:17:28Z-
dc.date.available2018-09-20T03:59:16Zen
dc.date.available2019-12-06T17:17:28Z-
dc.date.issued2015en
dc.identifier.citationSeviour, T., Hansen, S. H., Yang, L., Yau, Y. H., Wang, V. B., Stenvang, M. R., . . . Dueholm, M. S. (2015). Functional amyloids keep quorum-sensing molecules in check. Journal of Biological Chemistry, 290(10), 6457-6469. doi:10.1074/jbc.M114.613810en
dc.identifier.issn0021-9258en
dc.identifier.urihttps://hdl.handle.net/10356/89083-
dc.description.abstractThe mechanism by which extracellular metabolites, including redox mediators and quorum-sensing signaling molecules, traffic through the extracellular matrix of biofilms is poorly explored. We hypothesize that functional amyloids, abundant in natural biofilms and possessing hydrophobic domains, retain these metabolites. Using surface plasmon resonance, we demonstrate that the quorum-sensing (QS) molecules, 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-L-homoserine lactone, and the redox mediator pyocyanin bind with transient affinity to functional amyloids from Pseudomonas (Fap). Their high hydrophobicity predisposes them to signal-amyloid interactions, but specific interactions also play a role. Transient interactions allow for rapid association and dissociation kinetics, which make the QS molecules bioavailable and at the same time secure within the extracellular matrix as a consequence of serial bindings. Retention of the QS molecules was confirmed using Pseudomonas aeruginosa PAO1-based 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-L-homoserine lactone reporter assays, showing that Fap fibrils pretreated with the QS molecules activate the reporters even after sequential washes. Pyocyanin retention was validated by electrochemical analysis of pyocyanin-pretreated Fap fibrils subjected to the same washing process. Results suggest that QS molecule-amyloid interactions are probably important in the turbulent environments commonly encountered in natural habitats.en
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent13 p.en
dc.language.isoenen
dc.relation.ispartofseriesJournal of Biological Chemistryen
dc.rights© 2015 by The American Society for Biochemistry and Molecular Biology, Inc. This paper was published in Journal of Biological Chemistry and is made available as an electronic reprint (preprint) with permission of The American Society for Biochemistry and Molecular Biology, Inc. The published version is available at: [http://dx.doi.org/10.1074/jbc.M114.613810]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.en
dc.subjectBiofilmen
dc.subjectDRNTU::Science::Biological sciencesen
dc.subjectAmyloiden
dc.titleFunctional amyloids keep quorum-sensing molecules in checken
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science & Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.organizationSingapore Centre for Environmental Life Sciences Engineeringen
dc.contributor.researchEnergy Research Institute @NTUen
dc.identifier.doi10.1074/jbc.M114.613810en
dc.description.versionPublished versionen
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