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dc.creatorWu, Haiyanges
dc.creatorRebello, Osmondes
dc.creatorOwen, C. Davides
dc.creatorWalpole, Samueles
dc.creatorBennati Granier, Chloees
dc.creatorNdeh, Didieres
dc.creatorMonaco, Serenaes
dc.creatorAngulo Álvarez, Jesúses
dc.date.accessioned2021-03-03T11:29:05Z
dc.date.available2021-03-03T11:29:05Z
dc.date.issued2021
dc.identifier.citationWu, H., Rebello, O., Owen, C.D., Walpole, S., Bennati Granier, C., Ndeh, D.,...,Angulo Álvarez, J. (2021). Fucosidases from the human gut symbiont Ruminococcus gnavus. Cellular and Molecular Life Sciences, 78 (2), 675-693.
dc.identifier.issn1420-9071es
dc.identifier.urihttps://hdl.handle.net/11441/105599
dc.description.abstractThe availability and repartition of fucosylated glycans within the gastrointestinal tract contributes to the adaptation of gut bacteria species to ecological niches. To access this source of nutrients, gut bacteria encode α-l-fucosidases (fucosidases) which catalyze the hydrolysis of terminal α-l-fucosidic linkages. We determined the substrate and linkage specificities of fucosidases from the human gut symbiont Ruminococcus gnavus. Sequence similarity network identified strain-specific fucosidases in R. gnavus ATCC 29149 and E1 strains that were further validated enzymatically against a range of defined oligosaccharides and glycoconjugates. Using a combination of glycan microarrays, mass spectrometry, isothermal titration calorimetry, crystallographic and saturation transfer difference NMR approaches, we identified a fucosidase with the capacity to recognize sialic acid-terminated fucosylated glycans (sialyl Lewis X/A epitopes) and hydrolyze α1–3/4 fucosyl linkages in these substrates without the need to remove sialic acid. Molecular dynamics simulation and docking showed that 3′-Sialyl Lewis X (sLeX) could be accommodated within the binding site of the enzyme. This specificity may contribute to the adaptation of R. gnavus strains to the infant and adult gut and has potential applications in diagnostic glycomic assays for diabetes and certain cancers.es
dc.formatapplication/pdfes
dc.format.extent19 p.es
dc.language.isoenges
dc.publisherSpringeres
dc.relation.ispartofCellular and Molecular Life Sciences, 78 (2), 675-693.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectGut microbiotaes
dc.subjectGlycoside hydrolasees
dc.subjectMucuses
dc.subjectMucin glycosylationes
dc.subjectLewis epitopeses
dc.subjectAntennary fucosees
dc.titleFucosidases from the human gut symbiont Ruminococcus gnavuses
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Química orgánicaes
dc.relation.publisherversionhttps://doi.org/10.1007/s00018-020-03514-xes
dc.identifier.doi10.1007/s00018-020-03514-xes
dc.journaltitleCellular and Molecular Life Scienceses
dc.publication.volumen78es
dc.publication.issue2es
dc.publication.initialPage675es
dc.publication.endPage693es

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