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Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader

The human gut microbiota plays a central role in intestinal health and disease. Yet, many of its bacterial constituents are functionally still largely unexplored. A crucial prerequisite for bacterial survival and proliferation is the creation and/or exploitation of an own niche. For many bacterial s...

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Autores principales: van Muijlwijk, Guus H., van Mierlo, Guido, Jansen, Pascal W.T.C., Vermeulen, Michiel, Bleumink-Pluym, Nancy M.C., Palm, Noah W., van Putten, Jos P.M., de Zoete, Marcel R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8409761/
https://www.ncbi.nlm.nih.gov/pubmed/34455931
http://dx.doi.org/10.1080/19490976.2021.1966278
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author van Muijlwijk, Guus H.
van Mierlo, Guido
Jansen, Pascal W.T.C.
Vermeulen, Michiel
Bleumink-Pluym, Nancy M.C.
Palm, Noah W.
van Putten, Jos P.M.
de Zoete, Marcel R.
author_facet van Muijlwijk, Guus H.
van Mierlo, Guido
Jansen, Pascal W.T.C.
Vermeulen, Michiel
Bleumink-Pluym, Nancy M.C.
Palm, Noah W.
van Putten, Jos P.M.
de Zoete, Marcel R.
author_sort van Muijlwijk, Guus H.
collection PubMed
description The human gut microbiota plays a central role in intestinal health and disease. Yet, many of its bacterial constituents are functionally still largely unexplored. A crucial prerequisite for bacterial survival and proliferation is the creation and/or exploitation of an own niche. For many bacterial species that are linked to human disease, the inner mucus layer was found to be an important niche. Allobaculum mucolyticum is a newly identified, IBD-associated species that is thought be closely associated with the host epithelium. To explore how this bacterium is able to effectively colonize this niche, we screened its genome for factors that may contribute to mucosal colonization. Up to 60 genes encoding putative Carbohydrate Active Enzymes (CAZymes) were identified in the genome of A. mucolyticum. Mass spectrometry revealed 49 CAZymes of which 26 were significantly enriched in its secretome. Functional assays demonstrated the presence of CAZyme activity in A. mucolyticum conditioned medium, degradation of human mucin O-glycans, and utilization of liberated non-terminal monosaccharides for bacterial growth. The results support a model in which sialidases and fucosidases remove terminal O-glycan sugars enabling subsequent degradation and utilization of carbohydrates for A. mucolyticum growth. A. mucolyticum CAZyme secretion may thus facilitate bacterial colonization and degradation of the mucus layer and may pose an interesting target for future therapeutic intervention.
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spelling pubmed-84097612021-09-02 Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader van Muijlwijk, Guus H. van Mierlo, Guido Jansen, Pascal W.T.C. Vermeulen, Michiel Bleumink-Pluym, Nancy M.C. Palm, Noah W. van Putten, Jos P.M. de Zoete, Marcel R. Gut Microbes Research Paper The human gut microbiota plays a central role in intestinal health and disease. Yet, many of its bacterial constituents are functionally still largely unexplored. A crucial prerequisite for bacterial survival and proliferation is the creation and/or exploitation of an own niche. For many bacterial species that are linked to human disease, the inner mucus layer was found to be an important niche. Allobaculum mucolyticum is a newly identified, IBD-associated species that is thought be closely associated with the host epithelium. To explore how this bacterium is able to effectively colonize this niche, we screened its genome for factors that may contribute to mucosal colonization. Up to 60 genes encoding putative Carbohydrate Active Enzymes (CAZymes) were identified in the genome of A. mucolyticum. Mass spectrometry revealed 49 CAZymes of which 26 were significantly enriched in its secretome. Functional assays demonstrated the presence of CAZyme activity in A. mucolyticum conditioned medium, degradation of human mucin O-glycans, and utilization of liberated non-terminal monosaccharides for bacterial growth. The results support a model in which sialidases and fucosidases remove terminal O-glycan sugars enabling subsequent degradation and utilization of carbohydrates for A. mucolyticum growth. A. mucolyticum CAZyme secretion may thus facilitate bacterial colonization and degradation of the mucus layer and may pose an interesting target for future therapeutic intervention. Taylor & Francis 2021-08-30 /pmc/articles/PMC8409761/ /pubmed/34455931 http://dx.doi.org/10.1080/19490976.2021.1966278 Text en © 2021 The Author(s). Published with license by Taylor & Francis Group, LLC. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Paper
van Muijlwijk, Guus H.
van Mierlo, Guido
Jansen, Pascal W.T.C.
Vermeulen, Michiel
Bleumink-Pluym, Nancy M.C.
Palm, Noah W.
van Putten, Jos P.M.
de Zoete, Marcel R.
Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title_full Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title_fullStr Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title_full_unstemmed Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title_short Identification of Allobaculum mucolyticum as a novel human intestinal mucin degrader
title_sort identification of allobaculum mucolyticum as a novel human intestinal mucin degrader
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8409761/
https://www.ncbi.nlm.nih.gov/pubmed/34455931
http://dx.doi.org/10.1080/19490976.2021.1966278
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