Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
AuthorWong, W; Bai, X-C; Brown, A; Fernandez, IS; Hanssen, E; Condron, M; Tan, YH; Baum, J; Scheres, SHW
PublisherELIFE SCIENCES PUBLICATIONS LTD
University of Melbourne Author/sTan, Yan Hong; BAUM, JACOB; Hanssen, Eric; Wong, Wilson; BAI, XIAOCHEN
Medicine, Dentistry & Health Sciences
Microbiology & Immunology
Melbourne Students & Learning
Document TypeJournal Article
CitationsWong, W., Bai, X. -C., Brown, A., Fernandez, I. S., Hanssen, E., Condron, M., Tan, Y. H., Baum, J. & Scheres, S. H. W. (2014). Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. ELIFE, 3 (3), https://doi.org/10.7554/eLife.03080.
Access StatusOpen Access
Open Access at PMChttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086275
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 Å 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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