An aspartyl protease directs malaria effector proteins to the host cell
Details
Publication Year 2010-02-04, Volume 463, Issue #7281, Page 627-U52
Journal Title
NATURE
Publication Type
Journal Article
Abstract
Plasmodium falciparum causes the virulent form of malaria and disease manifestations are linked to growth inside infected erythrocytes. To survive and evade host responses the parasite remodels the erythrocyte by exporting several hundred effector proteins beyond the surrounding parasitophorous vacuole membrane. A feature of exported proteins is a pentameric motif (RxLxE/Q/D) that is a substrate for an unknown protease. Here we show that the protein responsible for cleavage of this motif is plasmepsin V (PMV), an aspartic acid protease located in the endoplasmic reticulum. PMV cleavage reveals the export signal (xE/Q/D) at the amino terminus of cargo proteins. Expression of an identical mature protein with xQ at the N terminus generated by signal peptidase was not exported, demonstrating that PMV activity is essential and linked with other key export events. Identification of the protease responsible for export into erythrocytes provides a novel target for therapeutic intervention against this devastating disease.
Publisher
NATURE PUBLISHING GROUP
Keywords
FALCIPARUM-INFECTED ERYTHROCYTES; PLASMODIUM EXPORT ELEMENT; ENDOPLASMIC-RETICULUM; PARASITE PROTEINS; HIV-1 PROTEASE; TRAFFICKING; EXPRESSION; VIRULENCE; CYTOADHERENCE; INVASION
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Creation Date: 2010-02-04 12:00:00
Last Modified: 0001-01-01 12:00:00
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