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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorCrouch, Lucy I.
dc.contributor.authorLiberato, Marcelo V.
dc.contributor.authorUrbanowicz, Paulina A.
dc.contributor.authorBaslé, Arnaud
dc.contributor.authorLamb, Christopher A.
dc.contributor.authorStewart, Christopher J.
dc.contributor.authorCooke, Katie
dc.contributor.authorDoona, Mary
dc.contributor.authorNeedham, Stephanie
dc.contributor.authorBrady, Richard R.
dc.contributor.authorBerrington, Janet E.
dc.contributor.authorMadunic, Katarina
dc.contributor.authorWuhrer, Manfred
dc.contributor.authorChater, Peter
dc.contributor.authorPearson, Jeffery P.
dc.contributor.authorGlowacki, Robert
dc.contributor.authorMartens, Eric C.
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSpencer, Daniel I.R.
dc.contributor.authorBolam, David N.
dc.date2020
dc.date.accessioned2022-06-21T15:35:23Z
dc.date.available2022-06-21T15:35:23Z
dc.date.issued2020-12-01
dc.identifier.citationProminent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown, L. I. Crouch, M. V. Liberato, P. A. Urbanowicz, A. Baslé, C. A. Lamb, C. Stewart, K. Cooke, M. Doona, S. Needham, R. R. Brady, J. E. Berrington, K. Madunic, P. Chater, F. Zhang, R. J. Linhardt, D. I. R. Spencer, D. N. Bolam, Nature Communications, 11, 4017, 2020.
dc.identifier.issn20411723
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5052
dc.identifier.urihttps://doi.org/10.1038/s41467-020-17847-5
dc.descriptionNature Communications, 11, 4017
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractThe thick mucus layer of the gut provides a barrier to infiltration of the underlying epithelia by both the normal microbiota and enteric pathogens. Some members of the microbiota utilise mucin glycoproteins as a nutrient source, but a detailed understanding of the mechanisms used to breakdown these complex macromolecules is lacking. Here we describe the discovery and characterisation of endo-acting enzymes from prominent mucin-degrading bacteria that target the polyLacNAc structures within oligosaccharide side chains of both animal and human mucins. These O-glycanases are part of the large and diverse glycoside hydrolase 16 (GH16) family and are often lipoproteins, indicating that they are surface located and thus likely involved in the initial step in mucin breakdown. These data provide a significant advance in our knowledge of the mechanism of mucin breakdown by the normal microbiota. Furthermore, we also demonstrate the potential use of these enzymes as tools to explore changes in O-glycan structure in a number of intestinal disease states.
dc.languageen_US
dc.language.isoENG
dc.publisherNature
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofNature Communications
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleProminent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdownen_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1038/s41467-020-17847-5
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.volume11


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Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution