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Summary: ARTICLES
An aspartyl protease directs malaria
effector proteins to the host cell
Justin A. Boddey1
, Anthony N. Hodder1
, Svenja Gušnther1
, Paul R. Gilson2
, Heather Patsiouras3
, Eugene A. Kapp3
,
J. Andrew Pearce1
, Tania F. de Koning-Ward4
, Richard J. Simpson1,3
, Brendan S. Crabb2
& Alan F. Cowman1
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
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