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J. Biol. Chem., Vol. 269, Issue 4, 2597-2606, 01, 1994
P Gerold, A Dieckmann-Schuppert and RT Schwarz
Plasmodium falciparum is the causative agent of malaria tropica in man.
Biochemical studies were focused on the asexual, intraerythrocytic stages
of P. falciparum, because of their role in the clinical phase of the
disease and the possibility of propagation in a cell culture system. In
this report, we describe the in-culture labeling of malarial glycolipids
and the analysis of their hydrophilic moieties. They were identified as
glycosylphosphatidylinositols (GPIs) by: 1) labeling with [3H]mannose,
[3H]glucosamine, and [3H]ethanolamine and 2) sensitivity toward
glycosylphosphatidylinositol-specific phospholipase D, phospholipase A2,
and nitrous acid. Malarial GPIs are shown to be unaffected by treatment
with phosphatidylinositol-specific phospholipase C, regardless of prior
treatment with mild base commonly used for inositol deacylation. Two
candidates for putative GPI-anchor precursors to malarial membrane proteins
with the structures ethanolamine-phosphate-6(Man alpha 1-2)Man alpha 1-2Man
alpha 1-6Man alpha 1-4 GlcN-PI (Pfg1 alpha) and ethanolamine-phosphate-6Man
alpha 1- 2Man alpha 1-6Man-alpha 1-4-GlcN-PI (Pfg1 beta) were identified.
Glycosylphosphatidylinositols synthesized by asexual erythrocytic stages of the malarial parasite, Plasmodium falciparum. Candidates for plasmodial glycosylphosphatidylinositol membrane anchor precursors and pathogenicity factors
Zentrum fur Hygiene und Medizinische Mikrobiologie, Philipps- Universitat Marburg, Germany.
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