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 and Nathalie Juge ()
Additional contact information
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
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
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

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms8624 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8624

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8624

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().