Localization of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum to the Golgi apparatus

William H. Witola, Gabriella Pessi, Kamal El Bissati, Jennifer M. Reynolds, Choukri Ben Mamoun

Research output: Research - peer-reviewArticle

Abstract

Phosphatidylcholine is the most abundant phospholipid in the membranes of Plasmodium falciparum, the agent of severe human malaria. The synthesis of this phospholipid occurs via two routes, the CDP-choline pathway, which uses host choline as a precursor, and the plant-like serine decarboxylase- phosphoethanolamine methyltransferase (SDPM) pathway, which uses host serine as a precursor. Although various components of these pathways have been identified, their cellular locations remain unknown. We have previously reported the identification and characterization of the phosphoethanolamine methyltransferase, Pfpmt, of P. falciparum and shown that it plays a critical role in the synthesis of phosphatidylcholine via the SDPM pathway. Here we provide the first evidence that the transmethylation step of the SDPM pathway occurs in the parasite Golgi apparatus. We show that the level of Pfpmt protein in the infected erythrocyte is regulated in a stage-specific fashion, with high levels detected during the trophozoite stage at the peak of parasite membrane biogenesis. Confocal microscopy revealed that Pfpmt is not cytoplasmic. Immunoelectron microscopy revealed that Pfpmt localizes to membrane structures that extend from the nuclear membrane but that it only partially co-localizes with the endoplasmic reticulum marker BiP. Using transgenic parasites expressing green fluorescent protein targeted to different cellular compartments, a complete co-localization was detected with Rab6, a marker of the Golgi apparatus. Together these studies provide the first evidence that the transmethylation step of the SDPM pathway of P. falciparum occurs in the Golgi apparatus and indicate an important role for this organelle in parasite membrane biogenesis.

LanguageEnglish (US)
Pages21305-21311
Number of pages7
JournalJournal of Biological Chemistry
Volume281
Issue number30
DOIs
StatePublished - Jul 28 2006
Externally publishedYes

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Falciparum Malaria
Golgi Apparatus
Serine
Parasites
phosphoethanolamine methyltransferase
Carboxy-Lyases
Membranes
Plasmodium falciparum
Phosphatidylcholines
Phospholipids
Cytidine Diphosphate Choline
Trophozoites
Immunoelectron Microscopy
Nuclear Envelope
Choline
Green Fluorescent Proteins
Confocal Microscopy
Endoplasmic Reticulum
Organelles
Malaria

ASJC Scopus subject areas

  • Biochemistry

Cite this

Localization of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum to the Golgi apparatus. / Witola, William H.; Pessi, Gabriella; El Bissati, Kamal; Reynolds, Jennifer M.; Mamoun, Choukri Ben.

In: Journal of Biological Chemistry, Vol. 281, No. 30, 28.07.2006, p. 21305-21311.

Research output: Research - peer-reviewArticle

Witola, William H. ; Pessi, Gabriella ; El Bissati, Kamal ; Reynolds, Jennifer M. ; Mamoun, Choukri Ben. / Localization of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum to the Golgi apparatus. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 30. pp. 21305-21311
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