The LacdiNAc-Specific Adhesin LabA Mediates ...
Document type :
Article dans une revue scientifique
DOI :
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Title :
The LacdiNAc-Specific Adhesin LabA Mediates Adhesion of Helicobacter pylori to Human Gastric Mucosa
Author(s) :
Rossez, Yannick [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gosset, Pierre [Auteur]
Institut Catholique de Lille [ICL]
Boneca, Ivo G. [Auteur]
Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall [BGPB]
Magalhães, Ana [Auteur]
Instituto de Patologia e Imunologia Molecular da Universidade do Porto [IPATIMUP]
Ecobichon, Chantal [Auteur]
Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall [BGPB]
Reis, Celso A. [Auteur]
Instituto de Patologia e Imunologia Molecular da Universidade do Porto [IPATIMUP]
Cieniewski, Caroline [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Joncquel, Marie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leonard, Renaud [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Maes, Emmanuel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Sperandio, Brice [Auteur]
Pathogénie Microbienne Moléculaire
Slomianny, Christian [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Sansonetti, Philippe J. [Auteur]
Pathogénie Microbienne Moléculaire
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Masselot, Catherine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gosset, Pierre [Auteur]
Institut Catholique de Lille [ICL]
Boneca, Ivo G. [Auteur]
Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall [BGPB]
Magalhães, Ana [Auteur]
Instituto de Patologia e Imunologia Molecular da Universidade do Porto [IPATIMUP]
Ecobichon, Chantal [Auteur]
Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall [BGPB]
Reis, Celso A. [Auteur]
Instituto de Patologia e Imunologia Molecular da Universidade do Porto [IPATIMUP]
Cieniewski, Caroline [Auteur]

Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Joncquel, Marie [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leonard, Renaud [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Maes, Emmanuel [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Sperandio, Brice [Auteur]
Pathogénie Microbienne Moléculaire
Slomianny, Christian [Auteur]

Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Sansonetti, Philippe J. [Auteur]
Pathogénie Microbienne Moléculaire
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Masselot, Catherine [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
The Journal of infectious diseases
Volume number :
210
Pages :
1286-1295
Publication date :
2014-10-15
ISSN :
0022-1899
English keyword(s) :
lacdiNAc
Amino Acid Sequence
Humans
Mice, Inbred C57BL
Molecular Sequence Data
Rats
tropism
Adhesins, Bacterial
Gastric Mucosa
Rats, Sprague-Dawley
Bacterial Adhesion
Animals
gastric mucins
Helicobacter pylori
Protein Binding
Mice
Adhesin
Gene Expression Regulation, Bacterial
Amino Acid Sequence
Humans
Mice, Inbred C57BL
Molecular Sequence Data
Rats
tropism
Adhesins, Bacterial
Gastric Mucosa
Rats, Sprague-Dawley
Bacterial Adhesion
Animals
gastric mucins
Helicobacter pylori
Protein Binding
Mice
Adhesin
Gene Expression Regulation, Bacterial
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Adhesion of Helicobacter pylori to the gastric mucosa is a necessary prerequisite for the pathogenesis of H. pylori–related diseases. In this study, we investigated the GalNAcβ1-4GlcNAc motif (also known as N,N’-diacetyl ...
Show more >Adhesion of Helicobacter pylori to the gastric mucosa is a necessary prerequisite for the pathogenesis of H. pylori–related diseases. In this study, we investigated the GalNAcβ1-4GlcNAc motif (also known as N,N’-diacetyllactosediamine [lacdiNAc]) carried by MUC5AC gastric mucins as the target for bacterial binding to the human gastric mucosa. The expression of LacdiNAc carried by gastric mucins was correlated with H. pylori localization, and all strains tested adhered significantly to this motif. Proteomic analysis and mutant construction allowed the identification of a yet uncharacterized bacterial adhesin, LabA, which specifically recognizes lacdiNAc. These findings unravel a target of adhesion for H. pylori in addition to moieties recognized by the well-characterized adhesins BabA and SabA. Localization of the LabA target, restricted to the gastric mucosa, suggests a plausible explanation for the tissue tropism of these bacteria. These results pave the way for the development of alternative strategies against H. pylori infection, using adherence inhibitors.Show less >
Show more >Adhesion of Helicobacter pylori to the gastric mucosa is a necessary prerequisite for the pathogenesis of H. pylori–related diseases. In this study, we investigated the GalNAcβ1-4GlcNAc motif (also known as N,N’-diacetyllactosediamine [lacdiNAc]) carried by MUC5AC gastric mucins as the target for bacterial binding to the human gastric mucosa. The expression of LacdiNAc carried by gastric mucins was correlated with H. pylori localization, and all strains tested adhered significantly to this motif. Proteomic analysis and mutant construction allowed the identification of a yet uncharacterized bacterial adhesin, LabA, which specifically recognizes lacdiNAc. These findings unravel a target of adhesion for H. pylori in addition to moieties recognized by the well-characterized adhesins BabA and SabA. Localization of the LabA target, restricted to the gastric mucosa, suggests a plausible explanation for the tissue tropism of these bacteria. These results pave the way for the development of alternative strategies against H. pylori infection, using adherence inhibitors.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Inserm
Université de Lille
Inserm
Université de Lille
Collections :
Research team(s) :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Génétique des enveloppes bactériennes
Génétique des enveloppes bactériennes
Submission date :
2020-02-12T15:44:38Z
2021-04-22T07:14:19Z
2021-04-22T07:27:00Z
2021-04-22T07:14:19Z
2021-04-22T07:27:00Z