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Identification of D-arabinan-degrading enzymes in mycobacteria

Lookup NU author(s): Omar Al-Jourani, Dr Jenn RossORCiD, Dr Nick Bailey, Dr Tiaan Heunis, Joseph Manion, Francesca Mensitieri, Dr Javier Abellon-RuizORCiD, Sophia Oram, Lauren Parsons, Dr Arnaud Basle, Professor Matthias TrostORCiD, Professor Robert HirtORCiD, Dr Elisabeth Lowe

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 2023. The Author(s).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.


Publication metadata

Author(s): Al-Jourani O, Benedict ST, Ross J, Layton AJ, van der Peet P, Marando VM, Bailey NP, Heunis T, Manion J, Mensitieri F, Franklin A, Abellon-Ruiz J, Oram SL, Parsons L, Cartmell A, Wright GSA, Basle A, Trost M, Henrissat B, Munoz-Munoz J, Hirt RP, Kiessling LL, Lovering AL, Williams SJ, Lowe EC, Moynihan PJ

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2023

Volume: 14

Issue: 1

Online publication date: 19/04/2023

Acceptance date: 31/03/2023

Date deposited: 15/05/2023

ISSN (electronic): 2041-1723

Publisher: Nature Publishing Group

URL: https://doi.org/10.1038/s41467-023-37839-5

DOI: 10.1038/s41467-023-37839-5

PubMed id: 37076525


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Funding

Funder referenceFunder name
209437/Z/17/Z
322820European Commission
DP210100233
BB/M011186/1
BB/S010122/1
BBSRCIAA-1544084
DO210100235
R01 Al-126592
RGS\R2\202228
RGS\R2\212050
NNF20SA0067193
NNF22OC0077058
NNF22SA0077601
SBF005\1065
U01GM125288
SBF006\1048

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