Chapter 27. Epithelial mucins and bacterial ...
Document type :
Partie d'ouvrage: Chapitre
Permalink :
Title :
Chapter 27. Epithelial mucins and bacterial adhesion
Author(s) :
Colomb, Florent [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Masselot, Catherine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Groux, Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Delannoy, Philippe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Masselot, Catherine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Groux, Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Delannoy, Philippe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Scientific editor(s) :
Pilar Rauter, Amelia
Lindhorst, Thisbe
Queneau, Yves
Lindhorst, Thisbe
Queneau, Yves
Book title :
Carbohydrate Chemistry : Volume 40
Volume number :
40
Pages :
596-623
Publisher :
Royal Society of Chemistry
Publication place :
Cambridge
Publication date :
2014
ISBN :
978-1-84973-965-8
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Mucins are high molecular weight glycoproteins characterized by highly O-glycosylated tandem repeat domains. Mucin-type O-glycans exhibit a variety of terminal sequences including histo-blood group antigens that serve as ...
Show more >Mucins are high molecular weight glycoproteins characterized by highly O-glycosylated tandem repeat domains. Mucin-type O-glycans exhibit a variety of terminal sequences including histo-blood group antigens that serve as counter receptors and participate in the adhesion and clearance of numerous bacteria including pathogens. In parallel, the pathological changes of mucin glycosylation modulate bacterial adhesion, often enhancing the adhesion of pathogenic bacteria. This review summarizes the current knowledge on the structure and biosynthesis of epithelial mucin O-glycans chains, the physio-pathological glycosylation repertoire of mucins and the role of mucin glycosylation in bacterial adhesion, focusing on the gastrointestinal tract and airway mucins.Show less >
Show more >Mucins are high molecular weight glycoproteins characterized by highly O-glycosylated tandem repeat domains. Mucin-type O-glycans exhibit a variety of terminal sequences including histo-blood group antigens that serve as counter receptors and participate in the adhesion and clearance of numerous bacteria including pathogens. In parallel, the pathological changes of mucin glycosylation modulate bacterial adhesion, often enhancing the adhesion of pathogenic bacteria. This review summarizes the current knowledge on the structure and biosynthesis of epithelial mucin O-glycans chains, the physio-pathological glycosylation repertoire of mucins and the role of mucin glycosylation in bacterial adhesion, focusing on the gastrointestinal tract and airway mucins.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Régulation de la glycosylation terminale
Génétique des enveloppes bactériennes
Génétique des enveloppes bactériennes
Submission date :
2020-02-12T15:44:39Z
2021-02-25T09:50:16Z
2021-02-25T09:50:16Z