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

研究成果: Contribution to journalArticle査読

5 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)5110-5123
ページ数14
ジャーナルJournal of Biological Chemistry
295
15
DOI
出版ステータス出版済み - 4 10 2020

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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