The endogenous galactofuranosidase GlfH1 ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan
Author(s) :
Shen, Lin [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Viljoen, Albertus [Auteur]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Villaume, Sydney [Auteur]
Université de Namur [Namur] [UNamur]
Joe, Maju [Auteur]
University of Alberta
Halloum, Iman [Auteur]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Chêne, Loïc [Auteur]
Université de Namur [Namur] [UNamur]
Mery, Alexandre [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fabre, Emeline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Takegawa, Kaoru [Auteur]
Kyushu University
Lowary, Todd L. [Auteur]
University of Alberta
Vincent, Stéphane P. [Auteur]
Université de Namur [Namur] [UNamur]
Kremer, Laurent [Auteur]
Institut National de la Santé et de la Recherche Médicale [INSERM]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Mariller, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Viljoen, Albertus [Auteur]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Villaume, Sydney [Auteur]
Université de Namur [Namur] [UNamur]
Joe, Maju [Auteur]
University of Alberta
Halloum, Iman [Auteur]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Chêne, Loïc [Auteur]
Université de Namur [Namur] [UNamur]
Mery, Alexandre [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fabre, Emeline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Takegawa, Kaoru [Auteur]
Kyushu University
Lowary, Todd L. [Auteur]
University of Alberta
Vincent, Stéphane P. [Auteur]
Université de Namur [Namur] [UNamur]
Kremer, Laurent [Auteur]
Institut National de la Santé et de la Recherche Médicale [INSERM]
Institut de Recherche en Infectiologie de Montpellier [IRIM]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Mariller, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Journal of Biological Chemistry
Abbreviated title :
J. Biol. Chem.
Volume number :
295
Pages :
5110-5123
Publisher :
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication date :
2020-02-27
English keyword(s) :
Mycobacterium tuberculosis
mycobacteria
polysaccharide
glycosidas
galactofuranose
arabinogalactan
catabolism
cell envelope
galactofuranosidase
Rv3096
mycobacteria
polysaccharide
glycosidas
galactofuranose
arabinogalactan
catabolism
cell envelope
galactofuranosidase
Rv3096
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Glycobiologie structurale des interactions hôtes-pathogènes
Submission date :
2020-11-23T12:18:29Z
2020-11-23T16:28:32Z
2020-11-23T16:28:32Z
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