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Plasmodium dihydrofolate reductase is a second enzyme target for the antimalarial action of triclosan

Journal article
Authors E. Bilsland
L. van Vliet
K. Williams
J. Feltham
Marta Carrasco
W. L. Fotoran
E. F. G. Cubillos
G. Wunderlich
Morten Grötli
F. Hollfelder
V. Jackson
R. D. King
S. G. Oliver
Published in Scientific Reports
Volume 8
ISSN 2045-2322
Publication year 2018
Published at Department of Chemistry and Molecular Biology
Language en
Links doi.org/10.1038/s41598-018-19549-x
Keywords carrier protein reductase, saccharomyces-cerevisiae, crystal-structure, liver-stage, falciparum, malaria, inhibition, resistance, derivatives, discovery, Science & Technology - Other Topics
Subject categories Microbiology, Immunology

Abstract

Malaria, caused by parasites of the genus Plasmodium, leads to over half a million deaths per year, 90% of which are caused by Plasmodium falciparum. P. vivax usually causes milder forms of malaria; however, P. vivax can remain dormant in the livers of infected patients for weeks or years before re-emerging in a new bout of the disease. The only drugs available that target all stages of the parasite can lead to severe side effects in patients with glucose-6-phosphate dehydrogenase (G6PD) deficiency; hence, there is an urgent need to develop new drugs active against blood and liver stages of the parasite. Different groups have demonstrated that triclosan, a common antibacterial agent, targets the Plasmodium liver enzyme enoyl reductase. Here, we provide 4 independent lines of evidence demonstrating that triclosan specifically targets both wild-type and pyrimethamine-resistant P. falciparum and P. vivax dihydrofolate reductases, classic targets for the blood stage of the parasite. This makes triclosan an exciting candidate for further development as a dual specificity antimalarial, which could target both liver and blood stages of the parasite.

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