Tailford, Louise E., Owen, C. David, Walshaw, John, Crost, Emmanuelle H., Hardy-Goddard, Jemma, Le Gall, Gwenaelle ORCID: https://orcid.org/0000-0002-1379-2196, De Vos, Willem M., Taylor, Garry L. and Juge, Nathalie (2015) Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Nature Communications, 6. ISSN 2041-1723
Full text not available from this repository.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.
Item Type: | Article |
---|---|
Uncontrolled Keywords: | chemistry(all),biochemistry, genetics and molecular biology(all),physics and astronomy(all),sdg 3 - good health and well-being ,/dk/atira/pure/subjectarea/asjc/1600 |
Related URLs: | |
Depositing User: | LivePure Connector |
Date Deposited: | 26 Oct 2018 16:31 |
Last Modified: | 14 Dec 2023 02:55 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/68679 |
DOI: | 10.1038/ncomms8624 |
Actions (login required)
View Item |