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

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)
4 Downloads (Pure)


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.
Original languageEnglish
Article number7624
Number of pages12
JournalNature Communications
Publication statusPublished - 8 Jul 2015


  • Inflammatory bowel-diseases
  • Sialic-acid
  • Streptococcus-pneumoniae
  • Entric pathogens
  • Crystal-structure
  • Mucus layers
  • Mucin
  • Bacteria
  • Specificity
  • Metabolism


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