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

Author

Listed:
  • Lucy I. Crouch

    (Newcastle University
    University of Birmingham)

  • Marcelo V. Liberato

    (Universidade de Sorocaba, Programa de Processos Tecnológicos e Ambientais)

  • Paulina A. Urbanowicz

    (Ludger Ltd, Culham Science Centre)

  • Arnaud Baslé

    (Newcastle University)

  • Christopher A. Lamb

    (Newcastle upon Tyne Hospitals NHS Foundation Trust)

  • Christopher J. Stewart

    (Newcastle University)

  • Katie Cooke

    (Newcastle University)

  • Mary Doona

    (Newcastle upon Tyne Hospitals NHS Foundation Trust)

  • Stephanie Needham

    (Newcastle upon Tyne Hospitals NHS Foundation Trust)

  • Richard R. Brady

    (Newcastle upon Tyne Hospitals NHS Foundation Trust)

  • Janet E. Berrington

    (Royal Victoria Infirmary)

  • Katarina Madunic

    (Leiden University Medical Centre)

  • Manfred Wuhrer

    (Leiden University Medical Centre)

  • Peter Chater

    (Newcastle University)

  • Jeffery P. Pearson

    (Newcastle University)

  • Robert Glowacki

    (University of Michigan Medical School)

  • Eric C. Martens

    (University of Michigan Medical School)

  • Fuming Zhang

    (Rensselaer Polytechnic Institute)

  • Robert J. Linhardt

    (Rensselaer Polytechnic Institute)

  • Daniel I. R. Spencer

    (Ludger Ltd, Culham Science Centre)

  • David N. Bolam

    (Newcastle University)

Abstract

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.

Suggested Citation

  • Lucy I. Crouch & Marcelo V. Liberato & Paulina A. Urbanowicz & Arnaud Baslé & Christopher A. Lamb & Christopher J. Stewart & Katie Cooke & Mary Doona & Stephanie Needham & Richard R. Brady & Janet E. , 2020. "Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17847-5
    DOI: 10.1038/s41467-020-17847-5
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    Cited by:

    1. Janneke Elzinga & Yoshiki Narimatsu & Noortje Haan & Henrik Clausen & Willem M. Vos & Hanne L. P. Tytgat, 2024. "Binding of Akkermansia muciniphila to mucin is O-glycan specific," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    2. Bashar Shuoker & Michael J. Pichler & Chunsheng Jin & Hiroka Sakanaka & Haiyang Wu & Ana Martínez Gascueña & Jining Liu & Tine Sofie Nielsen & Jan Holgersson & Eva Nordberg Karlsson & Nathalie Juge & , 2023. "Sialidases and fucosidases of Akkermansia muciniphila are crucial for growth on mucin and nutrient sharing with mucus-associated gut bacteria," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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