Skip to Main content Skip to Navigation
Journal articles

The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan

Abstract : Despite the 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 in response 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 in its structure, but no reports exist supportings this assumption. Herein, using [MS2] 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 identified found that the mycobacterial protein GlfH1 (Rv3096), which protein exhibits an 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 the a first step towards understanding the remodeling of mycobacterial AG.
Complete list of metadata

Cited literature [58 references]  Display  Hide  Download
Contributor : Laurent Kremer Connect in order to contact the contributor
Submitted on : Monday, June 15, 2020 - 4:36:55 PM
Last modification on : Wednesday, March 23, 2022 - 3:51:28 PM


 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document




Lin Shen, Albertus Viljoen, Sydney Villaume, Maju Joe, Iman Halloum, et al.. The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, pp.jbc.RA119.011817. ⟨10.1074/jbc.RA119.011817⟩. ⟨inserm-02495154⟩



Record views