Food vacuole targeting and trafficking of falcipain-2, an important cysteine protease of human malaria parasite Plasmodium falciparum
Details
Publication Year 2007-11, Volume 156, Issue #1, Page 12-23
Journal Title
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Publication Type
Journal Article
Abstract
Malaria proteases are attractive anti-malarial targets because of their roles in parasite development and infection. Falcipain-2 (FP-2), a food vacuole eysteine protease in Plasmodium falciparum, is involved in hemoglobin degradation and cleavage of cytoskeletal elements. To understand the route of trafficking and identify the signals involved in trafficking to food vacuole, we have generated transgenic parasites expressing green fluorescent protein (GFP) fusion proteins comprising of N-terminal regions of falcipain-2 fused to GFP. Using falcipain2-GFP chimeras and antifalcipain-2 antibody, we show that falcipain-2 is trafficked through a classical vesicle mediated secretory pathway involving encloplasmic reticulurn and Golgi-like apparatus. Photobleaching and confocal microscopy techniques reveal that falcipain-2 is carried to the food vacuole in the form of cytostomal vesicles. We identify an N-terminal sequence (1-120aa) of falcipain-2, sufficient for its transport to the food vacuole. Analysis of sequences of few other food vacuole targeted proteins suggests a common mechanism for protein trafficking to food vacuole of malaria parasite. (C) 2007 Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Keywords
RECOMBINANT FALCIPAIN-2; PARASITOPHOROUS VACUOLE; HOST ERYTHROCYTE; PROTEINS; ANTIMALARIALS; HEMOGLOBINASE; LOCALIZATION; TOXOPLASMA; VIRULENCE; SECRETOME
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Creation Date: 2007-11-01 12:00:00
Last Modified: 0001-01-01 12:00:00
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