Identification of d-arabinan-degrading enzymes in mycobacteria

Omar Al-Jourani, Samuel T. Benedict, Jennifer Ross, Abigail J. Layton, Phillip Peet, Victoria M. Marando, Nicholas P. Bailey, Tiaan Heunis, Joseph Manion, Francesca Mensitieri, Aaron Franklin, Javier Abellon-Ruiz, Sophia L. Oram, Lauren Parsons, Alan Cartmell, Gareth S. A. Wright, Arnaud Baslé, Matthias Trost, Bernard Henrissat, Jose Munoz-Munoz, Robert P. Hirt, Laura L. Kiessling, Andrew L. Lovering, Spencer J. Williams, Elisabeth C. Lowe () and Patrick J. Moynihan ()
Additional contact information
Omar Al-Jourani: Newcastle University
Samuel T. Benedict: University of Birmingham
Jennifer Ross: Newcastle University
Abigail J. Layton: University of Birmingham
Phillip Peet: University of Melbourne, Parkville
Victoria M. Marando: Massachusetts Institute of Technology
Nicholas P. Bailey: Newcastle University
Tiaan Heunis: Newcastle University
Joseph Manion: Newcastle University
Francesca Mensitieri: Newcastle University
Aaron Franklin: University of Birmingham
Javier Abellon-Ruiz: Newcastle University
Sophia L. Oram: Newcastle University
Lauren Parsons: Newcastle University
Alan Cartmell: University of Liverpool
Gareth S. A. Wright: University of Essex
Arnaud Baslé: Newcastle University
Matthias Trost: Newcastle University
Bernard Henrissat: King Abdulaziz University
Jose Munoz-Munoz: Northumbria University
Robert P. Hirt: Newcastle University
Laura L. Kiessling: Massachusetts Institute of Technology
Andrew L. Lovering: University of Birmingham
Spencer J. Williams: University of Melbourne, Parkville
Elisabeth C. Lowe: Newcastle University
Patrick J. Moynihan: University of Birmingham

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-37839-5

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