Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown
AuthorCrouch, 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.; Berrington, Janet E.; Madunic, Katarina; Wuhrer, Manfred; Chater, Peter; Pearson, Jeffery P.; Glowacki, Robert; Martens, Eric C.; Zhang, Fuming; Linhardt, Robert J.; Spencer, Daniel I.R.; Bolam, David N.
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationProminent 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.
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AbstractThe 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.;
DescriptionNature 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.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Nature Communications; https://harc.rpi.edu/;
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