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Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus
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dc.contributor.author | Owen, C. David | |
dc.contributor.author | Tailford, Louise E | |
dc.contributor.author | Monaco, Serena | |
dc.contributor.author | Šuligoj, Tanja | |
dc.contributor.author | Vaux, Laura | |
dc.contributor.author | Lallement, Romane | |
dc.contributor.author | Khedri, Zahra | |
dc.contributor.author | Yu, Hai | |
dc.contributor.author | Lecointe, Karine | |
dc.contributor.author | Walshaw, John | |
dc.contributor.author | Tribolo, Sandra | |
dc.contributor.author | Horrex, Marc | |
dc.contributor.author | Bell, Andrew | |
dc.contributor.author | Chen, Xi | |
dc.contributor.author | Taylor, Garry L | |
dc.contributor.author | Varki, Ajit | |
dc.contributor.author | Angulo, Jesus | |
dc.contributor.author | Juge, Nathalie | |
dc.date.accessioned | 2018-01-05T10:30:11Z | |
dc.date.available | 2018-01-05T10:30:11Z | |
dc.date.issued | 2017-12-19 | |
dc.identifier.citation | Owen , C D , Tailford , L E , Monaco , S , Šuligoj , T , Vaux , L , Lallement , R , Khedri , Z , Yu , H , Lecointe , K , Walshaw , J , Tribolo , S , Horrex , M , Bell , A , Chen , X , Taylor , G L , Varki , A , Angulo , J & Juge , N 2017 , ' Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus ' , Nature Communications , vol. 8 , 2196 , pp. 1-15 . https://doi.org/10.1038/s41467-017-02109-8 | en |
dc.identifier.issn | 2041-1723 | |
dc.identifier.other | PURE: 251880416 | |
dc.identifier.other | PURE UUID: 78871d25-1993-416e-b5c0-210de180b284 | |
dc.identifier.other | PubMed: 29259165 | |
dc.identifier.other | PubMedCentral: PMC5736709 | |
dc.identifier.other | Scopus: 85038615602 | |
dc.identifier.other | ORCID: /0000-0001-9486-566X/work/60428044 | |
dc.identifier.other | WOS: 000418336800001 | |
dc.identifier.uri | https://hdl.handle.net/10023/12436 | |
dc.description | The authors gratefully acknowledge the support of the Biotechnology and Biological Sciences Research Council (BBSRC), this research was funded by the BBSRC Institute Strategic Programme for The Gut Health and Food Safety (BB/J004529/1), the BB/F016778/1 grant, and by the US National Institutes of Health (NIH) of grant R01HD065122 (to X.C.) and R01GM32373 (to A.V.). S.M. and J.A. acknowledge a postgraduate studentship and financial support from the School of Pharmacy of the University of East Anglia. | en |
dc.description.abstract | Ruminococcus gnavus is a human gut symbiont wherein the ability to degrade mucins is mediated by an intramolecular trans-sialidase (RgNanH). RgNanH comprises a GH33 catalytic domain and a sialic acid-binding carbohydrate-binding module (CBM40). Here we used glycan arrays, STD NMR, X-ray crystallography, mutagenesis and binding assays to determine the structure and function of RgNanH_CBM40 (RgCBM40). RgCBM40 displays the canonical CBM40 β-sandwich fold and broad specificity towards sialoglycans with millimolar binding affinity towards α2,3- or α2,6-sialyllactose. RgCBM40 binds to mucus produced by goblet cells and to purified mucins, providing direct evidence for a CBM40 as a novel bacterial mucus adhesin. Bioinformatics data show that RgCBM40 canonical type domains are widespread among Firmicutes. Furthermore, binding of R. gnavus ATCC 29149 to intestinal mucus is sialic acid mediated. Together, this study reveals novel features of CBMs which may contribute to the biogeography of symbiotic bacteria in the gut. | |
dc.format.extent | 15 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nature Communications | en |
dc.rights | © The Author(s) 2017. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. | en |
dc.subject | R Medicine | en |
dc.subject | QH301 Biology | en |
dc.subject | QD Chemistry | en |
dc.subject | DAS | en |
dc.subject.lcc | R | en |
dc.subject.lcc | QH301 | en |
dc.subject.lcc | QD | en |
dc.title | Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus | en |
dc.type | Journal article | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. Office of the Principal | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1038/s41467-017-02109-8 | |
dc.description.status | Peer reviewed | en |
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