2013
Plasmodium falciparum phosphoethanolamine methyltransferase is essential for malaria transmission
Bobenchik AM, Witola WH, Augagneur Y, Lochlainn L, Garg A, Pachikara N, Choi JY, Zhao YO, Usmani-Brown S, Lee A, Adjalley SH, Samanta S, Fidock DA, Voelker DR, Fikrig E, Mamoun C. Plasmodium falciparum phosphoethanolamine methyltransferase is essential for malaria transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 18262-18267. PMID: 24145416, PMCID: PMC3831454, DOI: 10.1073/pnas.1313965110.Peer-Reviewed Original ResearchConceptsAsexual replicationGametocyte developmentFunctional complementation assaysPhosphoethanolamine N-methyltransferaseHost serineComplementation assaysMalaria transmissionGenetic diversityPhosphoethanolamine methyltransferaseGametocyte differentiationFemale gametocytesSpecificity of inhibitionMetabolic analysisSynthesis of phosphatidylcholineGametocytogenesisChemical screeningPlasmodium speciesAnopheles mosquitoesN-methyltransferaseLow micromolar rangePathwayReplicationHuman erythrocytesParasitesGlobal burden
2011
Phosphoethanolamine methyltransferases in phosphocholine biosynthesis: functions and potential for antiparasite therapy
Bobenchik AM, Augagneur Y, Hao B, Hoch JC, Mamoun C. Phosphoethanolamine methyltransferases in phosphocholine biosynthesis: functions and potential for antiparasite therapy. FEMS Microbiology Reviews 2011, 35: 609-619. PMID: 21303393, PMCID: PMC4107886, DOI: 10.1111/j.1574-6976.2011.00267.x.Peer-Reviewed Original ResearchConceptsStress-resistant plantsImportant biochemical stepHuman malaria parasiteMethyl donor SAMPhosphocholine biosynthesisN-methyltransferasesFlorida lanceletDependent methyltransferasesNuclear divisionBiochemical stepsDependent methylationBiological functionsGene expressionGenetic characterizationDevelopment of therapiesMalaria parasitesMajor phospholipidsDiverse groupEnzymeSmall moleculesPlantsAntiparasite therapyEukaryotesPhosphoethanolamineMethyltransferases
2008
Disruption of the Plasmodium falciparum PfPMT Gene Results in a Complete Loss of Phosphatidylcholine Biosynthesis via the Serine-Decarboxylase-Phosphoethanolamine-Methyltransferase Pathway and Severe Growth and Survival Defects*
Witola WH, El Bissati K, Pessi G, Xie C, Roepe PD, Mamoun CB. Disruption of the Plasmodium falciparum PfPMT Gene Results in a Complete Loss of Phosphatidylcholine Biosynthesis via the Serine-Decarboxylase-Phosphoethanolamine-Methyltransferase Pathway and Severe Growth and Survival Defects*. Journal Of Biological Chemistry 2008, 283: 27636-27643. PMID: 18694927, PMCID: PMC2562060, DOI: 10.1074/jbc.m804360200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEthanolamineGene DeletionMethylationMethyltransferasesPhosphatidylcholinesPlasmodium falciparumProtozoan ProteinsSerineConceptsSDPM pathwayBiosynthesis of phosphatidylcholinePhosphatidylcholine biosynthesisParasite growthMajor membrane phospholipidsHuman malaria parasiteHost serineSerine decarboxylaseGenetic evidenceMethyltransferase enzymeSurvival defectGene resultsYeast cellsMethylation of phosphatidylethanolamineBiosynthesisSynthesis of phosphatidylcholineBiochemical studiesMembrane phospholipidsMalaria parasitesPlasmodium parasitesSevere growthPathwaySignificant defectsParasitesComplete loss
2004
A pathway for phosphatidylcholine biosynthesis in Plasmodium falciparum involving phosphoethanolamine methylation
Pessi G, Kociubinski G, Mamoun CB. A pathway for phosphatidylcholine biosynthesis in Plasmodium falciparum involving phosphoethanolamine methylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 6206-6211. PMID: 15073329, PMCID: PMC395947, DOI: 10.1073/pnas.0307742101.Peer-Reviewed Original Research