RadA, a MSCRAMM Adhesin of the Dominant Symbiote Ruminococcus gnavus E1, Binds Human Immunoglobulins and Intestinal Mucins

Adhesion to the digestive mucosa is considered a key factor for bacterial persistence within the gut. In this study, we show that Ruminococcus gnavus E1 can express the radA gene, which encodes an adhesin of the MSCRAMMs family, only when it colonizes the gut. T...

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Autores principales:	Marc Maresca, Radia Alatou, Ange Pujol, Cendrine Nicoletti, Josette Perrier, Thierry Giardina, Gwenola Simon, Vincent Méjean, Michel Fons
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	<i>Ruminococcus gnavus</i> adhesin bacterial Ig-like domain collagen mucus mucin Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/402272ee27af48f49faa015e90d9db36
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spelling	oai:doaj.org-article:402272ee27af48f49faa015e90d9db362021-11-25T16:52:48ZRadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins10.3390/biom111116132218-273Xhttps://doaj.org/article/402272ee27af48f49faa015e90d9db362021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1613https://doaj.org/toc/2218-273XAdhesion to the digestive mucosa is considered a key factor for bacterial persistence within the gut. In this study, we show that <i>Ruminococcus gnavus</i> E1 can express the <i>radA</i> gene, which encodes an adhesin of the MSCRAMMs family, only when it colonizes the gut. The RadA N-terminal region contains an all-β bacterial Ig-like domain known to interact with collagens. We observed that it preferentially binds human immunoglobulins (IgA and IgG) and intestinal mucins. Using deglycosylated substrates, we also showed that the RadA N-terminal region recognizes two different types of motifs, the protein backbone of human IgG and the glycan structure of mucins. Finally, competition assays with lectins and free monosaccharides identified Galactose and N-Acetyl-Galactosamine motifs as specific targets for the binding of RadA to mucins and the surface of human epithelial cells.Marc MarescaRadia AlatouAnge PujolCendrine NicolettiJosette PerrierThierry GiardinaGwenola SimonVincent MéjeanMichel FonsMDPI AGarticle<i>Ruminococcus gnavus</i>adhesinbacterial Ig-like domaincollagenmucusmucinMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1613, p 1613 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	<i>Ruminococcus gnavus</i> adhesin bacterial Ig-like domain collagen mucus mucin Microbiology QR1-502
spellingShingle	<i>Ruminococcus gnavus</i> adhesin bacterial Ig-like domain collagen mucus mucin Microbiology QR1-502 Marc Maresca Radia Alatou Ange Pujol Cendrine Nicoletti Josette Perrier Thierry Giardina Gwenola Simon Vincent Méjean Michel Fons RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
description	Adhesion to the digestive mucosa is considered a key factor for bacterial persistence within the gut. In this study, we show that <i>Ruminococcus gnavus</i> E1 can express the <i>radA</i> gene, which encodes an adhesin of the MSCRAMMs family, only when it colonizes the gut. The RadA N-terminal region contains an all-β bacterial Ig-like domain known to interact with collagens. We observed that it preferentially binds human immunoglobulins (IgA and IgG) and intestinal mucins. Using deglycosylated substrates, we also showed that the RadA N-terminal region recognizes two different types of motifs, the protein backbone of human IgG and the glycan structure of mucins. Finally, competition assays with lectins and free monosaccharides identified Galactose and N-Acetyl-Galactosamine motifs as specific targets for the binding of RadA to mucins and the surface of human epithelial cells.
format	article
author	Marc Maresca Radia Alatou Ange Pujol Cendrine Nicoletti Josette Perrier Thierry Giardina Gwenola Simon Vincent Méjean Michel Fons
author_facet	Marc Maresca Radia Alatou Ange Pujol Cendrine Nicoletti Josette Perrier Thierry Giardina Gwenola Simon Vincent Méjean Michel Fons
author_sort	Marc Maresca
title	RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
title_short	RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
title_full	RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
title_fullStr	RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
title_full_unstemmed	RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins
title_sort	rada, a mscramm adhesin of the dominant symbiote <i>ruminococcus gnavus</i> e1, binds human immunoglobulins and intestinal mucins
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/402272ee27af48f49faa015e90d9db36
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RadA, a MSCRAMM Adhesin of the Dominant Symbiote <i>Ruminococcus gnavus</i> E1, Binds Human Immunoglobulins and Intestinal Mucins

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