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- W2685204875 abstract "Capreomycin is a second-line drug for multiple drug-resistant (MDR) tuberculosis (TB). However, along with the increase use in clinic, the therapeutic efficiency of capreomycin is decreasing. To better understand TB drug-resistance to capreomycin, we have done research to identify molecular target of capreomycin. An established L12-L10 interaction assay was used to evaluate the activity of capreomycin. And Mycobacterium smegmatis was used as the model bacterial of Mycobacterium tuberculosis. L12 and L10 overexpressing strains were constructed. Translation inhibition by capreomycin was assessed by using an in vitro cell-free translation system supplied with ribosomes from mycobacterium smegmatis as well as a luciferase reporter. we demonstrate that capreomycin inhibits L12-L10 interaction using an established L12-L10 interaction assay. It provoked our interest to further investigate the compound. Our observation that overexpression of L12 and/or L10 in mycobacterium smegmatis increases the MIC of capreomycin indicates that L12 and L10 are likely the targets. We further found that both EF-G-dependent GTPase activity and ribosome-mediated protein synthesis were inhibited by capreomycin. We speculated that the disruption of L12-L10 interaction by capreomycin impairs EF-G-dependent GTPase activity and protein synthesis subsequently. Moreover, capreomycin inhibits the growth of mycobacterium smegmatis through bactericidal effect. Interestingly, the bactericidal effect of capreomycin is restrained when protein synthesis is blocked. All the results suggest that capreomycin seems to inhibit TB through interrupting L12-L10 interaction. This finding might provide novel clues for anti-TB drug discovery and clinical use." @default.
- W2685204875 created "2017-06-30" @default.
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- W2685204875 date "2017-08-01" @default.
- W2685204875 modified "2023-10-18" @default.
- W2685204875 title "The Anti-Tuberculosis Antibiotic Capreomycin Inhibits Protein Synthesis Through Disrupting Interaction Between Tibosomal Proteins L12 and L10" @default.
- W2685204875 doi "https://doi.org/10.1016/j.clinthera.2017.05.076" @default.
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