ArticleInfection and immunity2012
LipC (Rv0220) is an immunogenic cell surface esterase of Mycobacterium tuberculosis.
Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- The cause-effect relation of tuberculosis on incidence of diabetes mellitus.Frontiers in cellular and infection microbiology · 2023Review
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- Article
- Rv0646c, an esterase from M. tuberculosis, up-regulates the host immune response in THP-1 macrophages cells.Molecular and cellular biochemistry · 2018Article
- Rv1288, a Two Domain, Cell Wall Anchored, Nutrient Stress Inducible Carboxyl-Esterase ofFrontiers in cellular and infection microbiology · 2018Article
- Ester-prodrugs of ethambutol control its antibacterial activity and provide rapid screening for mycobacterial hydrolase activity.Bioorganic & medicinal chemistry letters · 2017Article
- Evaluation of Rv0220, Rv2958c, Rv2994 and Rv3347c of Mycobacterium tuberculosis for serodiagnosis of tuberculosis.Microbial biotechnology · 2017Article
- Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Biochemistry · 2016Article
- Inactivation of MSMEG_0412 gene drastically affects surface related properties of Mycobacterium smegmatis.BMC microbiology · 2016Article
- Profiling Esterases in Mycobacterium tuberculosis Using Far-Red Fluorogenic Substrates.ACS chemical biology · 2016Article
- PE11, a PE/PPE family protein of Mycobacterium tuberculosis is involved in cell wall remodeling and virulence.Scientific reports · 2016Article
- Far-red fluorogenic probes for esterase and lipase detection.Chembiochem : a European journal of chemical biology · 2015Article
- Identification and Characterization of Lipase Activity and Immunogenicity of LipL from Mycobacterium tuberculosis.PloS one · 2015Article
- Molecular characterization of oxidative stress-inducible LipD of Mycobacterium tuberculosis H37Rv.Current microbiology · 2014Article
- Targeting lipid esterases in mycobacteria grown under different physiological conditions using activity-based profiling with tetrahydrolipstatin (THL).Molecular & cellular proteomics : MCP · 2014Article
- Development of a POC test for TB based on multiple immunodominant epitopes of M. tuberculosis specific cell-wall proteins.PloS one · 2014Article
- Characterization of an acid inducible lipase Rv3203 from Mycobacterium tuberculosis H37Rv.Molecular biology reports · 2014Article
- Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
We have reported previously the identification of novel proteins of Mycobacterium tuberculosis by the immunoscreening of an expression library of M. tuberculosis genomic DNA with sera obtained from M. tuberculosis-infected rabbits at 5 weeks postinfection. In this study, we report the further characterization of one of these antigens, LipC (Rv0220). LipC is annotated as a member of the Lip family based on the presence of the consensus motif "GXSXG" characteristic of esterases. Although predicted to be a cytoplasmic enzyme, we provide evidence that LipC is a cell surface protein that is present in both the cell wall and the capsule of M. tuberculosis. Consistent with this localization, LipC elicits strong humoral immune responses in both HIV-negative (HIV-) and HIV-positive (HIV+) tuberculosis (TB) patients. The absence of anti-LipC antibodies in sera from purified protein derivative-positive (PPD+) healthy subjects confirms its expression only during active M. tuberculosis infection. Epitope mapping of LipC identified 6 immunodominant epitopes, 5 of which map to the exposed surface of the modeled LipC protein. The recombinant LipC (rLipC) protein also elicits proinflammatory cytokine and chemokine responses from macrophages and pulmonary epithelial cells. rLipC can hydrolyze short-chain esters with the carbon chain containing 2 to 10 carbon atoms. Together, these studies demonstrate that LipC is a novel cell surface-associated esterase of M. tuberculosis that is highly immunogenic and elicits both antibodies and cytokines/chemokines.
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