Structural highlights
Publication Abstract from PubMedRuminococcus 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 beta-sandwich fold and broad specificity towards sialoglycans with millimolar binding affinity towards alpha2,3- or alpha2,6-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. Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus.,Owen CD, Tailford LE, Monaco S, Suligoj T, Vaux L, Lallement R, Khedri Z, Yu H, Lecointe K, Walshaw J, Tribolo S, Horrex M, Bell A, Chen X, Taylor GL, Varki A, Angulo J, Juge N Nat Commun. 2017 Dec 19;8(1):2196. doi: 10.1038/s41467-017-02109-8. PMID:29259165[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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