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Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum
The Serine Protease Inhibitor (serpin) protein has been suggested to play a key role in the interaction of bifidobacteria with the host. By inhibiting intestinal serine proteases, it might allow bifidobacteria to reside in specific gut niches. In inflammatory diseases where serine proteases contribu...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8012564/ https://www.ncbi.nlm.nih.gov/pubmed/33790385 http://dx.doi.org/10.1038/s41598-021-86740-y |
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author | Duboux, S. Golliard, M. Muller, J. A. Bergonzelli, G. Bolten, C. J. Mercenier, A. Kleerebezem, M. |
author_facet | Duboux, S. Golliard, M. Muller, J. A. Bergonzelli, G. Bolten, C. J. Mercenier, A. Kleerebezem, M. |
author_sort | Duboux, S. |
collection | PubMed |
description | The Serine Protease Inhibitor (serpin) protein has been suggested to play a key role in the interaction of bifidobacteria with the host. By inhibiting intestinal serine proteases, it might allow bifidobacteria to reside in specific gut niches. In inflammatory diseases where serine proteases contribute to the innate defense mechanism of the host, serpin may dampen the damaging effects of inflammation. In view of the beneficial roles of this protein, it is important to understand how its production is regulated. Here we demonstrate that Bifidobacterium longum NCC 2705 serpin production is tightly regulated by carbohydrates. Galactose and fructose increase the production of this protein while glucose prevents it, suggesting the involvement of catabolite repression. We identified that di- and oligosaccharides containing galactose (GOS) and fructose (FOS) moieties, including the human milk oligosaccharide Lacto-N-tetraose (LNT), are able to activate serpin production. Moreover, we show that the carbohydrate mediated regulation is conserved within B. longum subsp. longum strains but not in other bifidobacterial taxons harboring the serpin coding gene, highlighting that the serpin regulation circuits are not only species- but also subspecies- specific. Our work demonstrates that environmental conditions can modulate expression of an important effector molecule of B. longum, having potential important implications for probiotic manufacturing and supporting the postulated role of serpin in the ability of bifidobacteria to colonize the intestinal tract. |
format | Online Article Text |
id | pubmed-8012564 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-80125642021-04-01 Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum Duboux, S. Golliard, M. Muller, J. A. Bergonzelli, G. Bolten, C. J. Mercenier, A. Kleerebezem, M. Sci Rep Article The Serine Protease Inhibitor (serpin) protein has been suggested to play a key role in the interaction of bifidobacteria with the host. By inhibiting intestinal serine proteases, it might allow bifidobacteria to reside in specific gut niches. In inflammatory diseases where serine proteases contribute to the innate defense mechanism of the host, serpin may dampen the damaging effects of inflammation. In view of the beneficial roles of this protein, it is important to understand how its production is regulated. Here we demonstrate that Bifidobacterium longum NCC 2705 serpin production is tightly regulated by carbohydrates. Galactose and fructose increase the production of this protein while glucose prevents it, suggesting the involvement of catabolite repression. We identified that di- and oligosaccharides containing galactose (GOS) and fructose (FOS) moieties, including the human milk oligosaccharide Lacto-N-tetraose (LNT), are able to activate serpin production. Moreover, we show that the carbohydrate mediated regulation is conserved within B. longum subsp. longum strains but not in other bifidobacterial taxons harboring the serpin coding gene, highlighting that the serpin regulation circuits are not only species- but also subspecies- specific. Our work demonstrates that environmental conditions can modulate expression of an important effector molecule of B. longum, having potential important implications for probiotic manufacturing and supporting the postulated role of serpin in the ability of bifidobacteria to colonize the intestinal tract. Nature Publishing Group UK 2021-03-31 /pmc/articles/PMC8012564/ /pubmed/33790385 http://dx.doi.org/10.1038/s41598-021-86740-y Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Duboux, S. Golliard, M. Muller, J. A. Bergonzelli, G. Bolten, C. J. Mercenier, A. Kleerebezem, M. Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title | Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title_full | Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title_fullStr | Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title_full_unstemmed | Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title_short | Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum |
title_sort | carbohydrate-controlled serine protease inhibitor (serpin) production in bifidobacterium longum subsp. longum |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8012564/ https://www.ncbi.nlm.nih.gov/pubmed/33790385 http://dx.doi.org/10.1038/s41598-021-86740-y |
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