scholarly journals Correction: Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum

2004 ◽  
Vol 164 (4) ◽  
pp. 625-625
Author(s):  
Michael Klemba ◽  
Wandy Beatty ◽  
Ilya Gluzman ◽  
Daniel E. Goldberg
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Food Vacuole ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Plasmepsin Ii

Food vacuole-associated lipid bodies and heterogeneous lipid environments in the malaria parasite, Plasmodium falciparum

2004 ◽  
Vol 54 (1) ◽  
pp. 109-122 ◽  
Author(s):  
Katherine E. Jackson ◽  
Nectarios Klonis ◽  
David J. P. Ferguson ◽  
Akinola Adisa ◽  
Con Dogovski ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Food Vacuole ◽  
Lipid Bodies ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

scholarly journals Fate of haem iron in the malaria parasite Plasmodium falciparum

2002 ◽  
Vol 365 (2) ◽  
pp. 343-347 ◽  
Author(s):  
Timothy J. EGAN ◽  
Jill M. COMBRINCK ◽  
Joanne EGAN ◽  
Giovanni R. HEARNE ◽  
Helder M. MARQUES ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Chemical Analysis ◽  
Malaria Parasite ◽  
Spectroscopic Imaging ◽  
Food Vacuole ◽  
Electron Spectroscopic Imaging ◽  
Iron Species ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Haem Iron

Chemical analysis has shown that Plasmodium falciparum trophozoites contain 61±2% of the iron within parasitized erythrocytes, of which 92±6% is located within the food vacuole. Of this, 88±9% is in the form of haemozoin. 57Fe-Mössbauer spectroscopy shows that haemozoin is the only detectable iron species in trophozoites. Electron spectroscopic imaging confirms this conclusion.

scholarly journals Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum

2004 ◽  
Vol 164 (1) ◽  
pp. 47-56 ◽  
Author(s):  
Michael Klemba ◽  
Wandy Beatty ◽  
Ilya Gluzman ◽  
Daniel E. Goldberg
Keyword(s):  
Plasmodium Falciparum ◽  
Fluorescent Protein ◽  
Green Fluorescent Protein Fluorescence ◽  
Food Vacuole ◽  
Protein Fluorescence ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Plasmepsin Ii ◽  
Green Fluorescent ◽  
Secretory System

fA amily of aspartic proteases, the plasmepsins (PMs), plays a key role in the degradation of hemoglobin in the Plasmodium falciparum food vacuole. To study the trafficking of proPM II, we have modified the chromosomal PM II gene in P. falciparum to encode a proPM II–GFP chimera. By taking advantage of green fluorescent protein fluorescence in live parasites, the ultrastructural resolution of immunoelectron microscopy, and inhibitors of trafficking and PM maturation, we have investigated the biosynthetic path leading to mature PM II in the food vacuole. Our data support a model whereby proPM II is transported through the secretory system to cytostomal vacuoles and then is carried along with its substrate hemoglobin to the food vacuole where it is proteolytically processed to mature PM II.

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