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Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown

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

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 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.


Publication metadata

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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Funding

Funder referenceFunder name
BB/M029018/1Biotechnology and Biological Sciences Research Council (BBSRC)

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