Characterization of the isoprenoid chain of coenzyme Q in Plasmodium falciparum

Little is known about isoprenoid biosynthesis in parasitic protozoa. The presence of dolichol and isoprenylated proteins has been detected in Plasmodium falciparum, but no studies are available about the biosynthesis of the isoprenic side chain attached to the benzoquinone ring of coenzyme Q. In the...

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Publicado: 2002
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v207_n1_p13_DeMacedo
http://hdl.handle.net/20.500.12110/paper_03781097_v207_n1_p13_DeMacedo
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Sumario:Little is known about isoprenoid biosynthesis in parasitic protozoa. The presence of dolichol and isoprenylated proteins has been detected in Plasmodium falciparum, but no studies are available about the biosynthesis of the isoprenic side chain attached to the benzoquinone ring of coenzyme Q. In the present study, using metabolic labelling with different intermediates, we demonstrated the presence of an active isoprenoid pathway for the biosynthesis of the isoprenic chain of coenzyme Q. Our results show that P. falciparum is able to synthesize different homologs (coenzyme Q8 and coenzyme Q9), depending on the given intermediate. Parasites treated with nerolidol at doses 2.2 times below the IC50 showed a decreased ability to synthesize the isoprenic chain attached to coenzyme Q at all intraerythrocytic stages. Treatment with nerolidol arrested development of the intraerythrocytic stages of the parasites, indicating that the drug may have an antimalarial potential. © 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.