期刊
ELIFE
卷 3, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.03080
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资金
- MRC [MC_UP_A025_1013, MC_U105184332] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1013, MC_U105184332] Funding Source: researchfish
- Wellcome Trust [096570/Z/11/Z] Funding Source: researchfish
- Medical Research Council [MC_U105184332, MC_UP_A025_1013] Funding Source: Medline
- Wellcome Trust [100993/Z/13/Z, WT096570, 100993] Funding Source: Medline
Malaria inflicts an enormous burden on global human health. The emergence of parasite resistance to front-line drugs has prompted a renewed focus on the repositioning of clinically approved drugs as potential anti-malarial therapies. Antibiotics that inhibit protein translation are promising candidates for repositioning. We have solved the cryo-EM structure of the cytoplasmic ribosome from the human malaria parasite, Plasmodium falciparum, in complex with emetine at 3.2 angstrom resolution. Emetine is an anti-protozoan drug used in the treatment of ameobiasis that also displays potent anti-malarial activity. Emetine interacts with the E-site of the ribosomal small subunit and shares a similar binding site with the antibiotic pactamycin, thereby delivering its therapeutic effect by blocking mRNA/tRNA translocation. As the first cryo-EM structure that visualizes an antibiotic bound to any ribosome at atomic resolution, this establishes cryo-EM as a powerful tool for screening and guiding the design of drugs that target parasite translation machinery.
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