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Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus

Author

Listed:
  • C. David Owen

    (University of St Andrews
    Harwell Science and Innovation Campus)

  • Louise E. Tailford

    (Quadram Institute Bioscience, Norwich Research Park)

  • Serena Monaco

    (University of East Anglia, Norwich Research Park)

  • Tanja Šuligoj

    (Quadram Institute Bioscience, Norwich Research Park)

  • Laura Vaux

    (Quadram Institute Bioscience, Norwich Research Park)

  • Romane Lallement

    (Quadram Institute Bioscience, Norwich Research Park)

  • Zahra Khedri

    (Departments of Medicine and Cellular and Molecular Medicine, UC San Diego
    Ajinomoto Althea Inc)

  • Hai Yu

    (University of California-Davis)

  • Karine Lecointe

    (Quadram Institute Bioscience, Norwich Research Park)

  • John Walshaw

    (Quadram Institute Bioscience, Norwich Research Park
    University of East Anglia)

  • Sandra Tribolo

    (Quadram Institute Bioscience, Norwich Research Park)

  • Marc Horrex

    (Quadram Institute Bioscience, Norwich Research Park)

  • Andrew Bell

    (Quadram Institute Bioscience, Norwich Research Park)

  • Xi Chen

    (University of California-Davis)

  • Gary L. Taylor

    (University of St Andrews)

  • Ajit Varki

    (Departments of Medicine and Cellular and Molecular Medicine, UC San Diego)

  • Jesus Angulo

    (University of East Anglia, Norwich Research Park)

  • Nathalie Juge

    (Quadram Institute Bioscience, Norwich Research Park)

Abstract

Ruminococcus gnavus is a human gut symbiont wherein the ability to degrade mucins is mediated by an intramolecular trans-sialidase (RgNanH). RgNanH comprises a GH33 catalytic domain and a sialic acid-binding carbohydrate-binding module (CBM40). Here we used glycan arrays, STD NMR, X-ray crystallography, mutagenesis and binding assays to determine the structure and function of RgNanH_CBM40 (RgCBM40). RgCBM40 displays the canonical CBM40 β-sandwich fold and broad specificity towards sialoglycans with millimolar binding affinity towards α2,3- or α2,6-sialyllactose. RgCBM40 binds to mucus produced by goblet cells and to purified mucins, providing direct evidence for a CBM40 as a novel bacterial mucus adhesin. Bioinformatics data show that RgCBM40 canonical type domains are widespread among Firmicutes. Furthermore, binding of R. gnavus ATCC 29149 to intestinal mucus is sialic acid mediated. Together, this study reveals novel features of CBMs which may contribute to the biogeography of symbiotic bacteria in the gut.

Suggested Citation

  • C. David Owen & Louise E. Tailford & Serena Monaco & Tanja Šuligoj & Laura Vaux & Romane Lallement & Zahra Khedri & Hai Yu & Karine Lecointe & John Walshaw & Sandra Tribolo & Marc Horrex & Andrew Bell, 2017. "Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus," Nature Communications, Nature, vol. 8(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02109-8
    DOI: 10.1038/s41467-017-02109-8
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    Cited by:

    1. 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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