ArticlePloS one2015
Identification and Characterization of Lipase Activity and Immunogenicity of LipL from Mycobacterium tuberculosis.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Identification of novel metagenomic lipases through integrated structural and sequence-based analysis.PeerJ · 2026Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- A Phagosomally Expressed Gene, rv0428c, of Mycobacterium tuberculosis Demonstrates Acetyl Transferase Activity and Plays a Protective Role Under Stress Conditions.The protein journal · 2022Article
- Purification and Optimization of Extracellular Lipase from a Novel StrainInternational journal of analytical chemistry · 2022Article
- Overexpression ofInternational journal of molecular sciences · 2021Article
- Butyryl/Caproyl-CoA:Acetate CoA-transferase: cloning, expression and characterization of the key enzyme involved in medium-chain fatty acid biosynthesis.Bioscience reports · 2021Article
- Rv3091, An Extracellular Patatin-Like Phospholipase inFrontiers in microbiology · 2020Article
- Article
- Investigations into Isoniazid TreatedJournal of pathogens · 2018Article
- Marine Metagenome as A Resource for Novel Enzymes.Genomics, proteomics & bioinformatics · 2015Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipids and lipid-metabolizing esterases/lipases are highly important for the mycobacterial life cycle and, possibly, for mycobacterial virulence. In this study, we expressed 10 members of the Lip family of Mycobacterium tuberculosis. Among the 10 proteins, LipL displayed a significantly high enzymatic activity for the hydrolysis of long-chain lipids. The optimal temperature for the lipase activity of LipL was demonstrated to be 37°C, and the optimal pH was 8.0. The lipase active center was not the conserved motif G-x-S-x-G, but rather the S-x-x-K and GGG motifs, and the key catalytic amino acid residues were identified as G50, S88, and K91, as demonstrated through site-directed mutagenesis experiments. A three-dimensional modeling structure of LipL was constructed, which showed that the GGG motif was located in the surface of a pocket structure. Furthermore, the subcellular localization of LipL was demonstrated to be on the mycobacterial surface by Western blot analysis. Our results revealed that the LipL protein could induce a strong humoral immune response in humans and activate a CD8+ T cell-mediated response in mice. Overall, our study identified and characterized a novel lipase denoted LipL from M. tuberculosis, and demonstrated that LipL functions as an immunogen that activates both humoral and cell-mediated responses.
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