The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan

Lin Shen, Albertus Viljoen, Sydney Villaume, Maju Joe, Iman Halloum, Loic P. Chene, Alexandre Méry, Emeline Fabre, Kaoru Takegawa, Todd L. Lowary, Stéphane P. Vincent, Laurent Kremer, Yann Guérardel, Christophe Mariller

Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs


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 themAGPcomplex, 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 theAGcan 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.

langue originaleAnglais
Pages (de - à)5110-5123
Nombre de pages14
journalJournal of Biological Chemistry
Numéro de publication15
Les DOIs
Etat de la publicationPublié - 10 avr. 2020

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