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Papers In Press, published online ahead of print January 1, 2010
J. Lipid Res., doi:10.1194/jlr.M900166-JLR200

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Journal of Lipid Research, Vol. 51, 81-96, January 2010
Copyright © 2010 by American Society for Biochemistry and Molecular Biology

Rodent and nonrodent malaria parasites differ in their phospholipid metabolic pathways^[S]

Sandrine Déchamps^*, Marjorie Maynadier^*, Sharon Wein^*, Laila Gannoun-Zaki^*, Eric Maréchal^1, and Henri J. Vial^1,2,*

^* Dynamique des Interactions Membranaires Normales et Pathologiques, UMR 5235, Centre National de la Recherche Scientifique (CNRS) - Universite Montpellier II, cc 107, Place Eugene Bataillon, 34095 Montpellier Cedex 05, France
UMR 5168 CNRS-CEA-INRA-Universite Joseph Fourier, Institut de Recherches en Technologies et Sciences pour le Vivant, 17 avenue des Martyrs, 38058 Grenoble, France

² To whom correspondence should be addressed. e-mail: vial{at}univ-montp2.fr

Malaria, a disease affecting humans and other animals, is caused by a protist of the genus Plasmodium. At the intraerythrocytic stage, the parasite synthesizes a high amount of phospholipids through a bewildering number of pathways. In the human Plasmodium falciparum species, a plant-like pathway that relies on serine decarboxylase and phosphoethanolamine N-methyltransferase activities diverts host serine to provide additional phosphatidylcholine and phosphatidylethanolamine to the parasite. This feature of parasitic dependence toward its host was investigated in other Plasmodium species. In silico analyses led to the identification of phosphoethanolamine N-methyltransferase gene orthologs in primate and bird parasite genomes. However, the gene was not detected in the rodent P. berghei, P. yoelii, and P. chabaudi species. Biochemical experiments with labeled choline, ethanolamine, and serine showed marked differences in biosynthetic pathways when comparing rodent P. berghei and P. vinckei, and human P. falciparum species. Notably, in both rodent parasites, ethanolamine and serine were not significantly incorporated into phosphatidylcholine, indicating the absence of phosphoethanolamine N-methyltransferase activity. To our knowledge, this is the first study to highlight a crucial difference in phospholipid metabolism between Plasmodium species. The findings should facilitate efforts to develop more rational approaches to identify and evaluate new targets for antimalarial therapy.

Supplementary key words Plasmodium falciparum • Plasmodium berghei • Plasmodium vinckei • lipid • phospholipid biosynthesis • phosphatidylcholine • phosphatidylethanolamine • phosphatidylserine • phosphoethanolamine N-methyltransferase • serine decarboxylase

Abbreviations: CCT, CTP:phosphocholine cytidylyltransferase; CDP-Cho, cytidine-diphospho-choline; CDP-DAG, cytidine-diphospho-diacylglycerol; CDP-Etn, cytidine-diphospho-ethanolamine; CEPT, choline/ethanolamine-phosphotransferase; Cho, choline; EST, expressed sequence tag; Etn, ethanolamine; LysoPC, lysophosphatidylcholine; PC, phosphatidylcholine; P-Cho, phosphocholine; PE, phosphatidylethanolamine; PEMT, phosphatidylethanolamine N-methyltransferase; P-Etn, phosphoethanolamine; PL, phospholipid; PMT, phosphoethanolamine N-methyltransferase; PS, phosphatidylserine; SD, serine decarboxylase; SDPM pathway, serine decarboxylase - phosphoethanolamine methyltransferase pathway; Ser, serine

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