The endogenous galactofuranosidase GlfH1 ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan
Auteur(s) :
Shen, Lin [Auteur]
Viljoen, Albertus [Auteur]
Villaume, Sydney [Auteur]
Joe, Maju [Auteur]
Halloum, Iman [Auteur]
Chêne, Loïc [Auteur]
Méry, Alexandre [Auteur]
Fabre, Emeline [Auteur]
Takegawa, Kaoru [Auteur]
Lowary, Todd L. [Auteur]
Vincent, Stéphane P. [Auteur]
Kremer, Laurent [Auteur]
Guérardel, Yann [Auteur]
Mariller, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Viljoen, Albertus [Auteur]
Villaume, Sydney [Auteur]
Joe, Maju [Auteur]
Halloum, Iman [Auteur]
Chêne, Loïc [Auteur]
Méry, Alexandre [Auteur]
Fabre, Emeline [Auteur]
Takegawa, Kaoru [Auteur]
Lowary, Todd L. [Auteur]
Vincent, Stéphane P. [Auteur]
Kremer, Laurent [Auteur]
Guérardel, Yann [Auteur]
Mariller, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Journal of Biological Chemistry
Nom court de la revue :
J. Biol. Chem.
Numéro :
295
Pagination :
5110-5123
Éditeur :
American Society for Biochemistry & Molecular Biology (ASBMB)
Date de publication :
2020-02-27
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
Despite impressive progress made over the past 20 years in our understanding of mycolylarabinogalactan-peptidoglycan (mAGP) biogenesis, the mechanisms by which the tubercle bacillus Mycobacterium tuberculosis adapts its ...
Lire la suite >Despite impressive progress made over the past 20 years in our understanding of mycolylarabinogalactan-peptidoglycan (mAGP) biogenesis, the mechanisms by which the tubercle bacillus Mycobacterium tuberculosis adapts its cell wall structure and composition to various environmental conditions, especially during infection, remain poorly understood. Being the central portion of the mAGP complex, arabinogalactan (AG) is believed to be the constituent of the mycobacterial cell envelope that undergoes the least structural changes, but no reports exist supporting this assumption. Herein, using recombinantly expressed mycobacterial protein, bioinformatics analyses, and kinetic and biochemical assays, we demonstrate that the AG can be remodeled by a mycobacterial endogenous enzyme. In particular, we found that the mycobacterial GlfH1 (Rv3096) protein exhibits exo-β-d-galactofuranose hydrolase activity and is capable of hydrolyzing the galactan chain of AG by recurrent cleavage of the terminal β-(1,5) and β-(1,6)-Galf linkages. The characterization of this galactosidase represents a first step toward understanding the remodeling of mycobacterial AG.Lire moins >
Lire la suite >Despite impressive progress made over the past 20 years in our understanding of mycolylarabinogalactan-peptidoglycan (mAGP) biogenesis, the mechanisms by which the tubercle bacillus Mycobacterium tuberculosis adapts its cell wall structure and composition to various environmental conditions, especially during infection, remain poorly understood. Being the central portion of the mAGP complex, arabinogalactan (AG) is believed to be the constituent of the mycobacterial cell envelope that undergoes the least structural changes, but no reports exist supporting this assumption. Herein, using recombinantly expressed mycobacterial protein, bioinformatics analyses, and kinetic and biochemical assays, we demonstrate that the AG can be remodeled by a mycobacterial endogenous enzyme. In particular, we found that the mycobacterial GlfH1 (Rv3096) protein exhibits exo-β-d-galactofuranose hydrolase activity and is capable of hydrolyzing the galactan chain of AG by recurrent cleavage of the terminal β-(1,5) and β-(1,6)-Galf linkages. The characterization of this galactosidase represents a first step toward understanding the remodeling of mycobacterial AG.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Glycobiologie structurale des interactions hôtes-pathogènes
Date de dépôt :
2020-11-23T12:18:29Z