ArticleThe Journal of biological chemistry2013
Exposure to a cutinase-like serine esterase triggers rapid lysis of multiple mycobacterial species.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 16 citations in OpenAlex.
- Fluorescence-Quenched Mycoloyl-Arabinofuranoside Analogs: Fluorogenic Probes for Mycobacterial Outer Membrane-Degrading Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- Review
- Exploring the molecular properties and bactericidal potential of Lysin B from mycobacteriophage WXIN.BMC microbiology · 2026Article
- Targeting intracellular nontuberculous mycobacteria andMicrobiology spectrum · 2024Article
- Intrapulmonary Treatment with Mycobacteriophage LysB Rapidly Reduces Mycobacterium abscessus Burden.Antimicrobial agents and chemotherapy · 2023Article
- Chemical Reporters for Bacterial Glycans: Development and Applications.Chemical reviews · 2022Review
- Trehalose Recycling Promotes Energy-Efficient Biosynthesis of the Mycobacterial Cell Envelope.mBio · 2021Article
- The role of chemoenzymatic synthesis in advancing trehalose analogues as tools for combatting bacterial pathogens.Chemical communications (Cambridge, England) · 2020Article
- A FRET-Based Fluorogenic Trehalose Dimycolate Analogue for Probing Mycomembrane-Remodeling Enzymes of Mycobacteria.ACS omega · 2019Article
- A hydrolase of trehalose dimycolate induces nutrient influx and stress sensitivity to balance intracellular growth of Mycobacterium tuberculosis.Cell host & microbe · 2014Article
- Free mycolic acid accumulation in the cell wall of the mce1 operon mutant strain of Mycobacterium tuberculosis.Journal of microbiology (Seoul, Korea) · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Mycobacteria are shaped by a thick envelope made of an array of uniquely structured lipids and polysaccharides. However, the spatial organization of these molecules remains unclear. Here, we show that exposure to an esterase from Mycobacterium smegmatis (Msmeg_1529), hydrolyzing the ester linkage of trehalose dimycolate in vitro, triggers rapid and efficient lysis of Mycobacterium tuberculosis, Mycobacterium bovis BCG, and Mycobacterium marinum. Exposure to the esterase immediately releases free mycolic acids, while concomitantly depleting trehalose mycolates. Moreover, lysis could be competitively inhibited by an excess of purified trehalose dimycolate and was abolished by a S124A mutation affecting the catalytic activity of the esterase. These findings are consistent with an indispensable structural role of trehalose mycolates in the architectural design of the exposed surface of the mycobacterial envelope. Importantly, we also demonstrate that the esterase-mediated rapid lysis of M. tuberculosis significantly improves its detection in paucibacillary samples.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.