ArticleNature communications2024
The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- A new role for lipoproteins LpqZ and FecB in orchestrating mycobacterial cell envelope biogenesis.mBio · 2026Article
- Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge.Cell reports · 2025Article
- Article
- Stopping Tuberculosis at the Gate: The Role ofVaccines · 2025Review
- Improving the bioconversion of phytosterols to 9α-hydroxy-4-androstene-3,17-dione by disruption of acyltransferase SucT and TmaT associated with the mycobacterial cell wall synthesis.World journal of microbiology & biotechnology · 2024Article
- Lipoarabinomannan mediates localized cell wall integrity during division in mycobacteria.Nature communications · 2024Article
Corrections and comments
- Erratum issued
- Update of
Authors and funding
18 authors.
Funding
Abstract
Mycobacterial glycolipids are important cell envelope structures that drive host-pathogen interactions. Arguably, the most important are lipoarabinomannan (LAM) and its precursor, lipomannan (LM), which are trafficked from the bacterium to the host via unknown mechanisms. Arabinomannan is thought to be a capsular derivative of these molecules, lacking a lipid anchor. However, the mechanism by which this material is generated has yet to be elucidated. Here, we describe the identification of a glycoside hydrolase family 76 enzyme that we term LamH (Rv0365c in Mycobacterium tuberculosis) which specifically cleaves α-1,6-mannoside linkages within LM and LAM, driving its export to the capsule releasing its phosphatidyl-myo-inositol mannoside lipid anchor. Unexpectedly, we found that the catalytic activity of this enzyme is important for efficient exit from stationary phase cultures, potentially implicating arabinomannan as a signal for growth phase transition. Finally, we demonstrate that LamH is important for M. tuberculosis survival in macrophages.
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