Journal article
Role of Plasmepsin V in Export of Diverse Protein Families from the Plasmodium falciparum Exportome
JA Boddey, TG Carvalho, AN Hodder, TJ Sargeant, BE Sleebs, D Marapana, S Lopaticki, T Nebl, AF Cowman
Traffic | Published : 2013
DOI: 10.1111/tra.12053
Abstract
Plasmodium falciparum exports several hundred effector proteins that remodel the host erythrocyte and enable parasites to acquire nutrients, sequester in the circulation and evade immune responses. The majority of exported proteins contain the Plasmodium export element (PEXEL; RxLxE/Q/D) in their N-terminus, which is proteolytically cleaved in the parasite endoplasmic reticulum by Plasmepsin V, and is necessary for export. Several exported proteins lack a PEXEL or contain noncanonical motifs. Here, we assessed whether Plasmepsin V could process the N-termini of diverse protein families in P. falciparum. We show that Plasmepsin V cleaves N-terminal sequences from RIFIN, STEVOR and RESA multig..
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Awarded by Ramaciotti Foundation
Funding Acknowledgements
This work was funded by the National Health and Medical Research Council of Australia and the Ramaciotti Foundation (Establishment Grant 3197/2010 to J. A. B.). We thank Cameron Nowell (Centre for Dynamic Imaging, Walter and Eliza Hall Institute) for valuable assistance with quantification of export. We are especially grateful to the Red Cross blood bank in Melbourne for providing human erythrocytes. This work was supported through Victorian State Government Operational Infrastructure Support and Australian Government NHMRC IRIISS. JAB is an Australian Research Council QEII Fellow and AFC is a Howard Hughes International Scholar and an Australia Fellow of the NHMRC. The authors have no conflict of interests with this manuscript.