The endogenous galactofuranosidase GlfH1 hydrolyzes mycobacterial arabinogalactan

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

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)5110-5123
Number of pages14
JournalJournal of Biological Chemistry
Issue number15
Publication statusPublished - Apr 10 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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