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

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, Xi Chen, Gary L. Taylor, Ajit Varki, Jesus Angulo and Nathalie Juge ()
Additional contact information
C. David Owen: University of St Andrews
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
Hai Yu: University of California-Davis
Karine Lecointe: Quadram Institute Bioscience, Norwich Research Park
John Walshaw: Quadram Institute Bioscience, Norwich Research Park
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

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-02109-8

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