ArticleNature communications2023
Identification of D-arabinan-degrading enzymes in mycobacteria.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
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- A Type VII-secreted toxin enables inter-mycobacterial competition.Nature communications · 2026Article
- Strategies for GH functional annotation: toward harmonized and predictive CAZymology.Biotechnology for biofuels and bioproducts · 2026Article
- Ribosome Biogenesis and Translational Control in Skeletal Muscle Atrophy and Hypertrophy: Mechanisms and Therapeutic Perspectives.Biomolecules · 2026Review
- In vivo manipulation of human gut Bacteroides fitness by abiotic oligosaccharides.Nature chemical biology · 2025Article
- Mutations in Gordonia amarae mycolic acid biosynthetic pathway confer resistance to Patescibacteria parasite Mycosynbacter amalyticus.Nature communications · 2025Article
- Lignocellulose adaptation drives polysaccharide biosynthesis inFrontiers in fungal biology · 2025Article
- Analysis of complete genomes of Mycobacterium tuberculosis sublineage 2.1 (Proto-Beijing) revealed the presence of three pe_pgrs3-pe_pgrs4-like genes.Scientific reports · 2024Article
- Crystal structure of β-d-galactofuranosidase from Streptomyces sp. JHA19 in complex with an inhibitor provides insights into substrate specificity.FEBS letters · 2024Article
- The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth.Nature communications · 2024Article
- Chemical biology tools to probe bacterial glycans.Current opinion in chemical biology · 2024Review
- The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth.bioRxiv : the preprint server for biology · 2023Article
- Collected Thoughts on Mycobacterial Lipoarabinomannan, a Cell Envelope Lipoglycan.Pathogens (Basel, Switzerland) · 2023Review
- Identification and characterization of endo-α-, exo-α-, and exo-β-D-arabinofuranosidases degrading lipoarabinomannan and arabinogalactan of mycobacteria.Nature communications · 2023Article
Corrections and comments
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Authors and funding
26 authors at 9 institutions in 5 countries.
Funding
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.
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