Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum

Abstract 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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	S. Duboux, M. Golliard, J. A. Muller, G. Bergonzelli, C. J. Bolten, A. Mercenier, M. Kleerebezem
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f9dd18896a8341ad9ec15256cceb5fc2
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:f9dd18896a8341ad9ec15256cceb5fc2
record_format	dspace
spelling	oai:doaj.org-article:f9dd18896a8341ad9ec15256cceb5fc22021-12-02T13:27:04ZCarbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum10.1038/s41598-021-86740-y2045-2322https://doaj.org/article/f9dd18896a8341ad9ec15256cceb5fc22021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86740-yhttps://doaj.org/toc/2045-2322Abstract 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.S. DubouxM. GolliardJ. A. MullerG. BergonzelliC. J. BoltenA. MercenierM. KleerebezemNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q S. Duboux M. Golliard J. A. Muller G. Bergonzelli C. J. Bolten A. Mercenier M. Kleerebezem Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum
description	Abstract 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	article
author	S. Duboux M. Golliard J. A. Muller G. Bergonzelli C. J. Bolten A. Mercenier M. Kleerebezem
author_facet	S. Duboux M. Golliard J. A. Muller G. Bergonzelli C. J. Bolten A. Mercenier M. Kleerebezem
author_sort	S. Duboux
title	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_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_sort	carbohydrate-controlled serine protease inhibitor (serpin) production in bifidobacterium longum subsp. longum
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f9dd18896a8341ad9ec15256cceb5fc2
work_keys_str_mv	AT sduboux carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT mgolliard carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT jamuller carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT gbergonzelli carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT cjbolten carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT amercenier carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum AT mkleerebezem carbohydratecontrolledserineproteaseinhibitorserpinproductioninbifidobacteriumlongumsubsplongum
_version_	1718393069549649920

Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum

Ejemplares similares