Identification of d-arabinan-degrading enzymes in mycobacteria
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s41467-023-37839-5.pdf
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Published version
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1.82 MB
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Author(s)
Al-Jourani, Omar
Benedict, Samuel T
Ross, Jennifer
Layton, Abigail J
van der Peet, Phillip
Marando, Victoria M
Bailey, Nicholas P
Heunis, Tiaan
Manion, Joseph
Mensitieri, Francesca
Date Issued
April 19, 2023
Journal
Nature Communications
Publisher
Springer Science and Business Media LLC
Citation
Al-Jourani, O., Benedict, S.T., Ross, J. et al. Identification of d-arabinan-degrading enzymes in mycobacteria. Nat Commun 14, 2233 (2023).
Version
Final published version
Abstract
Bacterial cell growth and division require the coordinated action of enzymes that synthesize and degrade cell wall polymers. Here, we identify enzymes that cleave the d-arabinan core of arabinogalactan, an unusual component of the cell wall of Mycobacterium tuberculosis and other mycobacteria. We screened 14 human gut-derived Bacteroidetes for arabinogalactan-degrading activities and identified four families of glycoside hydrolases with activity against the d-arabinan or d-galactan components of arabinogalactan. Using one of these isolates with exo-d-galactofuranosidase activity, we generated enriched d-arabinan and used it to identify a strain of Dysgonomonas gadei as a d-arabinan degrader. This enabled the discovery of endo- and exo-acting enzymes that cleave d-arabinan, including members of the DUF2961 family (GH172) and a family of glycoside hydrolases (DUF4185/GH183) that display endo-d-arabinofuranase activity and are conserved in mycobacteria and other microbes. Mycobacterial genomes encode two conserved endo-d-arabinanases with different preferences for the d-arabinan-containing cell wall components arabinogalactan and lipoarabinomannan, suggesting they are important for cell wall modification and/or degradation. The discovery of these enzymes will support future studies into the structure and function of the mycobacterial cell wall.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1038/s41467-023-37839-5
