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

Department of Medicine and Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110

Address correspondence to Daniel E. Goldberg, Dept. of Molecular Microbiology, Washington University School of Medicine, 660 S. Euclid Ave., Box 8230, St. Louis, MO 63110. Tel.: (314) 362-1514. Fax: (314) 367-3214. email: goldberg{at}borcim.wustl.edu

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.

Key Words: protease; protein trafficking; brefeldin A; endoplasmic reticulum; hemoglobin

Abbreviations used in this paper: ALLN, N-acetyl-L-leucyl-L-leucyl-L-norleucinal; BFA, brefeldin A; HAP, histo-aspartic protease; mPM, mature plasmepsin; PM, plasmepsin.

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