Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown
Authors
Crouch, Lucy I.
Liberato, Marcelo V.
Urbanowicz, Paulina A.
Baslé, Arnaud
Lamb, Christopher A.
Stewart, Christopher J.
Cooke, Katie
Doona, Mary
Needham, Stephanie
Brady, Richard R.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2020-12-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
Attribution 3.0 United States
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
Full Citation
Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown, L. I. Crouch, M. V. Liberato, P. A. Urbanowicz, A. Baslé, C. A. Lamb, C. Stewart, K. Cooke, M. Doona, S. Needham, R. R. Brady, J. E. Berrington, K. Madunic, P. Chater, F. Zhang, R. J. Linhardt, D. I. R. Spencer, D. N. Bolam, Nature Communications, 11, 4017, 2020.
Abstract
The thick mucus layer of the gut provides a barrier to infiltration of the underlying epithelia by both the normal microbiota and enteric pathogens. Some members of the microbiota utilise mucin glycoproteins as a nutrient source, but a detailed understanding of the mechanisms used to breakdown these complex macromolecules is lacking. Here we describe the discovery and characterisation of endo-acting enzymes from prominent mucin-degrading bacteria that target the polyLacNAc structures within oligosaccharide side chains of both animal and human mucins. These O-glycanases are part of the large and diverse glycoside hydrolase 16 (GH16) family and are often lipoproteins, indicating that they are surface located and thus likely involved in the initial step in mucin breakdown. These data provide a significant advance in our knowledge of the mechanism of mucin breakdown by the normal microbiota. Furthermore, we also demonstrate the potential use of these enzymes as tools to explore changes in O-glycan structure in a number of intestinal disease states.
Description
Nature Communications, 11, 4017
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Nature
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Nature Communications
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Nature Communications
https://harc.rpi.edu/
Access
Open Access
CC BY — Creative Commons Attribution
CC BY — Creative Commons Attribution