DOI: 10.7554/elife.03080. Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine

Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine

10.7554/elife.03080

Crossref journal-article

eLife Sciences Publications, Ltd

eLife (4374)

Abstract

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.

Bibliography

Wong, W., Bai, X., Brown, A., Fernandez, I. S., Hanssen, E., Condron, M., Tan, Y. H., Baum, J., & Scheres, S. H. (2014). Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. ELife, 3. CLOCKSS.

Authors 9

Wilson Wong (first)
Xiao-chen Bai (additional)
Alan Brown (additional)
Israel S Fernandez (additional)
Eric Hanssen (additional)
Melanie Condron (additional)
Yan Hong Tan (additional)
Jake Baum (additional)
Sjors HW Scheres (additional)

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Dates

Type	When
Created	11 years, 2 months ago (June 9, 2014, 11:29 a.m.)
Deposited	1 year, 10 months ago (Oct. 11, 2023, 8:45 p.m.)
Indexed	21 hours, 59 minutes ago (Aug. 21, 2025, 1:01 p.m.)
Issued	11 years, 2 months ago (June 9, 2014)
Published	11 years, 2 months ago (June 9, 2014)
Published Online	11 years, 2 months ago (June 9, 2014)

Funders 18

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Human Frontier Science Program 10.13039/501100000854
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BibTeX

@article{Wong_2014, title={Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine}, volume={3}, ISSN={2050-084X}, url={http://dx.doi.org/10.7554/elife.03080}, DOI={10.7554/elife.03080}, journal={eLife}, publisher={eLife Sciences Publications, Ltd}, author={Wong, Wilson and Bai, Xiao-chen and Brown, Alan and Fernandez, Israel S and Hanssen, Eric and Condron, Melanie and Tan, Yan Hong and Baum, Jake and Scheres, Sjors HW}, year={2014}, month=jun }

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  "abstract": "<jats:p>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 \u00c5 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.</jats:p>",
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  "title": "Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine",
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