ArticlePloS one2009
Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
- The peptidoglycan-binding domain regulates antimycobacterial activity of LysB by affecting its transportation and/or catalytic activity.Communications biology · 2026Article
- Expression and biochemical characterization of a patatin-like medium-chain esterase Rv1063c fromFrontiers in microbiology · 2026Article
- Discovery of anti-infective compounds againstFrontiers in microbiology · 2024Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- Current Therapy and Therapeutic Targets for Microsporidiosis.Frontiers in microbiology · 2022Review
- Total Synthesis of Tetrahydrolipstatin, Its Derivatives, and Evaluation of Their Ability to Potentiate Multiple Antibiotic Classes againstACS infectious diseases · 2021Article
- Rv3091, An Extracellular Patatin-Like Phospholipase inFrontiers in microbiology · 2020Article
- Biochemical and microbiological evaluation ofMedChemComm · 2019Article
- LipG a bifunctional phospholipase/thioesterase involved in mycobacterial envelope remodeling.Bioscience reports · 2018Article
- Characterization of Tetrahydrolipstatin and Stereoderivatives on the Inhibition of Essential Mycobacterium tuberculosis Lipid Esterases.Biochemistry · 2018Article
- Structural basis for lipid binding and mechanism of theThe Journal of biological chemistry · 2018Article
- A Screen for Protein-Protein Interactions in Live Mycobacteria Reveals a Functional Link between the Virulence-Associated Lipid Transporter LprG and the Mycolyltransferase Antigen 85A.ACS infectious diseases · 2017Article
- Small-Molecule Probes Reveal Esterases with Persistent Activity in Dormant and Reactivating Mycobacterium tuberculosis.ACS infectious diseases · 2016Article
- Effects of Lipid-Lowering Drugs on Vancomycin Susceptibility of Mycobacteria.Antimicrobial agents and chemotherapy · 2016Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Characterization of Rv0888, a Novel Extracellular Nuclease from Mycobacterium tuberculosis.Scientific reports · 2016Article
- Surface hydrolysis of sphingomyelin by the outer membrane protein Rv0888 supports replication of Mycobacterium tuberculosis in macrophages.Molecular microbiology · 2015Article
- Article
- Targeting lipid esterases in mycobacteria grown under different physiological conditions using activity-based profiling with tetrahydrolipstatin (THL).Molecular & cellular proteomics : MCP · 2014Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The cell wall of M. tuberculosis is central to its success as a pathogen. Mycolic acids are key components of this cell wall. The genes involved in joining the alpha and mero mycolates are located in a cluster, beginning with Rv3799c and extending at least until Rv3804c. The role of each enzyme encoded by these five genes is fairly well understood, except for Rv3802c. Rv3802 is one of seven putative cutinases encoded by the genome of M. tuberculosis. In phytopathogens, cutinases hydrolyze the waxy layer of plants, cutin. In a strictly mammalian pathogen, such as M. tuberculosis, it is likely that these proteins perform a different function. Of the seven, we chose to focus on Rv3802c because of its location in a mycolic acid synthesis gene cluster, its putative essentiality, its ubiquitous presence in actinomycetes, and its conservation in the minimal genome of Mycobacterium leprae. We expressed Rv3802 in Escherichia coli and purified the enzymatically active form. We probed its activities and inhibitors characterizing those relevant to its possible role in mycolic acid biosynthesis. In addition to its reported phospholipase A activity, Rv3802 has significant thioesterase activity, and it is inhibited by tetrahydrolipstatin (THL). THL is a described anti-tuberculous compound with an unknown mechanism, but it reportedly targets cell wall synthesis. Taken together, these data circumstantially support a role for Rv3802 in mycolic acid synthesis and, as the cell wall is integral to M. tuberculosis pathogenesis, identification of a novel cell wall enzyme and its inhibition has therapeutic and diagnostic implications.
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