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

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  • Justin A. Boddey

    (The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
    University of Melbourne)

  • 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
    University of Melbourne
    Present address: Monash University, Wellington Road, Clayton, Victoria 3800, Australia)

  • Anthony N. Hodder

    (The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
    University of Melbourne)

  • 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
    Present address: University of Cologne, Joseph-Stelzmann-Strasse 20, 50931 Cologne, Germany)

  • 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
    University of Melbourne)

  • Alan F. Cowman

    (The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade
    University of Melbourne)

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.

Suggested Citation

  • 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 & T, 2016. "Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding," Nature Communications, Nature, vol. 7(1), pages 1-14, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10470
    DOI: 10.1038/ncomms10470
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