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Lookup NU author(s): Dr Lucy Crouch, Dr Arnaud Basle, Professor Chris LambORCiD, Professor Christopher StewartORCiD, Kate Cooke, Mary Doona, Dr Stephanie Needham, Richard Brady, Professor Janet Berrington, Dr Peter Chater, Professor Jeffrey Pearson, Dr David Bolam
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2020, The Author(s).The 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.
Author(s): Crouch LI, Liberato MV, Urbanowicz PA, Basle A, Lamb CA, Stewart CJ, Cooke K, Doona M, Needham S, Brady RR, Berrington JE, Madunic K, Wuhrer M, Chater P, Pearson JP, Glowacki R, Martens EC, Zhang F, Linhardt RJ, Spencer DIR, Bolam DN
Publication type: Article
Publication status: Published
Journal: Nature Communications
Year: 2020
Volume: 11
Issue: 1
Online publication date: 11/08/2020
Acceptance date: 21/07/2020
Date deposited: 26/08/2020
ISSN (electronic): 2041-1723
Publisher: Nature Research
URL: https://doi.org/10.1038/s41467-020-17847-5
DOI: 10.1038/s41467-020-17847-5
PubMed id: 32782292
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