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dc.contributor.authorTailford, Louise E.
dc.contributor.authorOwen, C. David
dc.contributor.authorWalshaw, John
dc.contributor.authorCrost, Emmanuelle H.
dc.contributor.authorHardy-Goddard, Jemma
dc.contributor.authorLe Gall, Gwenaelle
dc.contributor.authorde Vos, Willem M.
dc.contributor.authorTaylor, Garry L.
dc.contributor.authorJuge, Nathalie
dc.date.accessioned2015-08-21T15:40:01Z
dc.date.available2015-08-21T15:40:01Z
dc.date.issued2015-07-08
dc.identifier.citationTailford , L E , Owen , C D , Walshaw , J , Crost , E H , Hardy-Goddard , J , Le Gall , G , de Vos , W M , Taylor , G L & Juge , N 2015 , ' Discovery of intramolecular trans- sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation ' , Nature Communications , vol. 6 , 7624 . https://doi.org/10.1038/ncomms8624en
dc.identifier.issn2041-1723
dc.identifier.otherPURE: 211299588
dc.identifier.otherPURE UUID: 8ff6eeec-a1e9-4b4e-a597-245aa7cb7a70
dc.identifier.otherWOS: 000358857000017
dc.identifier.otherScopus: 84946936348
dc.identifier.otherORCID: /0000-0001-9486-566X/work/60428034
dc.identifier.otherWOS: 000358857000017
dc.identifier.urihttp://hdl.handle.net/10023/7310
dc.descriptionThe authors acknowledge the support of the Biotechnology and Biological Sciences Research Council (BBSRC), this research was partly funded by the BBSRC Institute Strategic Programme for The Gut Health and Food Safety (BB/J004529/1) and by the BB/L008602/1 BBSRC-responsive mode grant. We also acknowledge support from the EU FP7 TORNADO programme. The research of WMdV was supported by the Academy of Finland, European Research Council and the Netherlands Organization for Scientific Research.en
dc.description.abstractThe gastrointestinal mucus layer is colonized by a dense community of microbes catabolizing dietary and host carbohydrates during their expansion in the gut. Alterations in mucosal carbohydrate availability impact on the composition of microbial species. Ruminococcus gnavus is a commensal anaerobe present in the gastrointestinal tract of >90% of humans and overrepresented in inflammatory bowel diseases (IBD). Using a combination of genomics, enzymology and crystallography, we show that the mucin-degrader R. gnavus ATCC 29149 strain produces an intramolecular trans-sialidase (IT-sialidase) that cleaves off terminal α2-3-linked sialic acid from glycoproteins, releasing 2,7-anhydro-Neu5Ac instead of sialic acid. Evidence of IT-sialidases in human metagenomes indicates that this enzyme occurs in healthy subjects but is more prevalent in IBD metagenomes. Our results uncover a previously unrecognized enzymatic activity in the gut microbiota, which may contribute to the adaptation of intestinal bacteria to the mucosal environment in health and disease.
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofNature Communicationsen
dc.rightsCopyright 2015 the Authors. This work is licensed under a Creative Commons Attribution 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 to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/en
dc.subjectInflammatory bowel-diseasesen
dc.subjectSialic-aciden
dc.subjectStreptococcus-pneumoniaeen
dc.subjectEntric pathogensen
dc.subjectCrystal-structureen
dc.subjectMucus layersen
dc.subjectMucinen
dc.subjectBacteriaen
dc.subjectSpecificityen
dc.subjectMetabolismen
dc.subjectR Medicineen
dc.subjectBDCen
dc.subjectR2Cen
dc.subject.lccRen
dc.titleDiscovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptationen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Office of the Principalen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1038/ncomms8624
dc.description.statusPeer revieweden


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