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Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation

Author

Listed:
  • Louise E. Tailford

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park)

  • C. David Owen

    (Biomolecular Sciences Building, University of St Andrews)

  • John Walshaw

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park
    School of Computing Sciences, University of East Anglia)

  • Emmanuelle H. Crost

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park)

  • Jemma Hardy-Goddard

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park)

  • Gwenaelle Le Gall

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park)

  • Willem M. de Vos

    (Laboratory of Microbiology
    University of Helsinki)

  • Garry L. Taylor

    (Biomolecular Sciences Building, University of St Andrews)

  • Nathalie Juge

    (The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park)

Abstract

The gastrointestinal mucus layer is colonized by a dense community of microbes catabolizing dietary and host carbohydrates during their expansion in the gut. Alterations in mucosal carbohydrate availability impact on the composition of microbial species. Ruminococcus gnavus is a commensal anaerobe present in the gastrointestinal tract of >90% of humans and overrepresented in inflammatory bowel diseases (IBD). Using a combination of genomics, enzymology and crystallography, we show that the mucin-degrader R. gnavus ATCC 29149 strain produces an intramolecular trans-sialidase (IT-sialidase) that cleaves off terminal α2-3-linked sialic acid from glycoproteins, releasing 2,7-anhydro-Neu5Ac instead of sialic acid. Evidence of IT-sialidases in human metagenomes indicates that this enzyme occurs in healthy subjects but is more prevalent in IBD metagenomes. Our results uncover a previously unrecognized enzymatic activity in the gut microbiota, which may contribute to the adaptation of intestinal bacteria to the mucosal environment in health and disease.

Suggested Citation

  • Louise E. Tailford & C. David Owen & John Walshaw & Emmanuelle H. Crost & Jemma Hardy-Goddard & Gwenaelle Le Gall & Willem M. de Vos & Garry L. Taylor & Nathalie Juge, 2015. "Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation," Nature Communications, Nature, vol. 6(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8624
    DOI: 10.1038/ncomms8624
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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.

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