• Medientyp: E-Artikel
  • Titel: Plasmodium falciparum CTP:phosphocholine cytidylyltransferase possesses two functional catalytic domains and is inhibited by a CDP‐choline analog selected from a virtual screening
  • Beteiligte: Contet, Alicia; Pihan, Emilie; Lavigne, Marina; Wengelnik, Kai; Maheshwari, Sweta; Vial, Henri; Douguet, Dominique; Cerdan, Rachel
  • Erschienen: Wiley, 2015
  • Erschienen in: FEBS Letters
  • Sprache: Englisch
  • DOI: 10.1016/j.febslet.2015.03.003
  • ISSN: 0014-5793; 1873-3468
  • Schlagwörter: Cell Biology ; Genetics ; Molecular Biology ; Biochemistry ; Structural Biology ; Biophysics
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  • Beschreibung: <jats:p>Phosphatidylcholine is the major lipid component of the malaria parasite membranes and is required for parasite multiplication in human erythrocytes. <jats:italic>Plasmodium falciparum</jats:italic> CTP:phosphocholine cytidylyltransferase (<jats:italic>Pf</jats:italic>CCT) is the rate‐limiting enzyme of the phosphatidylcholine biosynthesis pathway and thus considered as a potential antimalarial target. In contrast to its mammalian orthologs, <jats:italic>Pf</jats:italic>CCT contains a duplicated catalytic domain. Here, we show that both domains are catalytically active with similar kinetic parameters. A virtual screening strategy allowed the identification of a drug‐size molecule competitively inhibiting the enzyme. This compound also prevented phosphatidylcholine biosynthesis in parasites and exerted an antimalarial effect. This study constitutes the first step towards a rationalized design of future new antimalarial agents targeting <jats:italic>Pf</jats:italic>CCT.</jats:p>
  • Zugangsstatus: Freier Zugang