Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding

Justin A. Boddey (), Matthew T. O’Neill, Sash Lopaticki, Teresa G. Carvalho, Anthony N. Hodder, Thomas Nebl, Stephan Wawra, Pieter van West, Zeinab Ebrahimzadeh, Dave Richard, Sven Flemming, Tobias Spielmann, Jude Przyborski, Jeff J. Babon and Alan F. Cowman ()
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Justin A. Boddey: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Matthew T. O’Neill: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Sash Lopaticki: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Teresa G. Carvalho: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Anthony N. Hodder: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Thomas Nebl: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Stephan Wawra: Aberdeen Oomycete Laboratory, College of Life Sciences and Medicine, University of Aberdeen–Foresterhill
Pieter van West: Aberdeen Oomycete Laboratory, College of Life Sciences and Medicine, University of Aberdeen–Foresterhill
Zeinab Ebrahimzadeh: Faculté de Médecine, Université Laval
Dave Richard: Faculté de Médecine, Université Laval
Sven Flemming: Parasitology Section, Bernhard Nocht Institute for Tropical Medicine
Tobias Spielmann: Parasitology Section, Bernhard Nocht Institute for Tropical Medicine
Jude Przyborski: Philipps University Marburg
Jeff J. Babon: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
Alan F. Cowman: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade

Nature Communications, 2016, vol. 7, issue 1, 1-14

Abstract: Abstract Plasmodium falciparum exports proteins into erythrocytes using the Plasmodium export element (PEXEL) motif, which is cleaved in the endoplasmic reticulum (ER) by plasmepsin V (PMV). A recent study reported that phosphatidylinositol-3-phosphate (PI(3)P) concentrated in the ER binds to PEXEL motifs and is required for export independent of PMV, and that PEXEL motifs are functionally interchangeable with RxLR motifs of oomycete effectors. Here we show that the PEXEL does not bind PI(3)P, and that this lipid is not concentrated in the ER. We find that RxLR motifs cannot mediate export in P. falciparum. Parasites expressing a mutated version of KAHRP, with the PEXEL motif repositioned near the signal sequence, prevented PMV cleavage. This mutant possessed the putative PI(3)P-binding residues but is not exported. Reinstatement of PEXEL to its original location restores processing by PMV and export. These results challenge the PI(3)P hypothesis and provide evidence that PEXEL position is conserved for co-translational processing and export.

Date: 2016
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DOI: 10.1038/ncomms10470

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