Glycosylate and move! The glycosyltransferase ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Glycosylate and move! The glycosyltransferase Maf is involved in bacterial flagella formation
Auteur(s) :
Sulzenbacher, Gerlind [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Roig-Zamboni, Véronique [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Lebrun, Régine [Auteur]
Plateforme Protéomique [Marseille]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Murat, Dorothée [Auteur]
Laboratoire de chimie bactérienne [LCB]
Mansuelle, Pascal [Auteur]
Plateforme Protéomique [Marseille]
Yamakawa, Nao [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Qian, Xin-Xin [Auteur]
Laboratoire de chimie bactérienne [LCB]
Vincentelli, Renaud [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Bourne, Yves [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Wu, Long-Fei [Auteur]
Laboratoire de chimie bactérienne [LCB]
Alberto, François [Auteur]
Laboratoire de chimie bactérienne [LCB]
Architecture et fonction des macromolécules biologiques [AFMB]
Roig-Zamboni, Véronique [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Lebrun, Régine [Auteur]
Plateforme Protéomique [Marseille]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Murat, Dorothée [Auteur]
Laboratoire de chimie bactérienne [LCB]
Mansuelle, Pascal [Auteur]
Plateforme Protéomique [Marseille]
Yamakawa, Nao [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Qian, Xin-Xin [Auteur]
Laboratoire de chimie bactérienne [LCB]
Vincentelli, Renaud [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Bourne, Yves [Auteur]
Architecture et fonction des macromolécules biologiques [AFMB]
Wu, Long-Fei [Auteur]
Laboratoire de chimie bactérienne [LCB]
Alberto, François [Auteur]
Laboratoire de chimie bactérienne [LCB]
Titre de la revue :
Environmental Microbiology
Nom court de la revue :
Environ. Microbiol.
Numéro :
20
Pagination :
228-240
Date de publication :
2018-01
ISSN :
1462-2920
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
The flagella of various Gram-negative bacteria are decorated with diverse glycan structures, amongst them nonulosonic acids related to the sialic acid family. Although nonulosonic sugar biosynthesis pathways have been ...
Lire la suite >The flagella of various Gram-negative bacteria are decorated with diverse glycan structures, amongst them nonulosonic acids related to the sialic acid family. Although nonulosonic sugar biosynthesis pathways have been dissected in various pathogens, the enzymes transferring the sugars onto flagellin are still poorly characterized. The deletion of genes coding for motility associated factors (Mafs) found in many pathogenic strains systematically gives rise to nonflagellated bacteria lacking specific nonulosonic sugars on the flagellins, therefore, relating Maf function to flagellin glycosylation and bacterial motility. We investigated the role of Maf from our model organism, Magnetospirillum magneticum AMB-1, in the glycosylation and formation of the flagellum. Deletion of the gene amb0685 coding for Maf produced a nonflagellated bacterium where the flagellin was still produced but no longer glycosylated. Our X-ray structure analysis revealed that the central domain of Maf exhibits similarity to sialyltransferases from Campylobacter jejuni. Glycan analysis suggested that the nonulosonic carbohydrate structure transferred is pseudaminic acid or a very close derivative. This work describes the importance of glycosylation in the formation of the bacterial flagellum and provides the first structural model for a member of a new bacterial glycosyltransferase family involved in nonulosonic acids transfer onto flagellins.Lire moins >
Lire la suite >The flagella of various Gram-negative bacteria are decorated with diverse glycan structures, amongst them nonulosonic acids related to the sialic acid family. Although nonulosonic sugar biosynthesis pathways have been dissected in various pathogens, the enzymes transferring the sugars onto flagellin are still poorly characterized. The deletion of genes coding for motility associated factors (Mafs) found in many pathogenic strains systematically gives rise to nonflagellated bacteria lacking specific nonulosonic sugars on the flagellins, therefore, relating Maf function to flagellin glycosylation and bacterial motility. We investigated the role of Maf from our model organism, Magnetospirillum magneticum AMB-1, in the glycosylation and formation of the flagellum. Deletion of the gene amb0685 coding for Maf produced a nonflagellated bacterium where the flagellin was still produced but no longer glycosylated. Our X-ray structure analysis revealed that the central domain of Maf exhibits similarity to sialyltransferases from Campylobacter jejuni. Glycan analysis suggested that the nonulosonic carbohydrate structure transferred is pseudaminic acid or a very close derivative. This work describes the importance of glycosylation in the formation of the bacterial flagellum and provides the first structural model for a member of a new bacterial glycosyltransferase family involved in nonulosonic acids transfer onto flagellins.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Projet ANR :
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Chemical Glycobiology
Date de dépôt :
2020-02-12T15:11:06Z
2021-05-07T10:08:47Z
2021-05-07T10:08:47Z