An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes

Steven Batinovic, Emma McHugh, Scott A. Chisholm, Kathryn Matthews, Boiyin Liu, Laure Dumont, Sarah C. Charnaud, Molly Parkyn Schneider, Paul R. Gilson, Tania F. de Koning-Ward, Matthew W. A. Dixon and Leann Tilley ()
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Steven Batinovic: Bio21 Institute, The University of Melbourne
Emma McHugh: Bio21 Institute, The University of Melbourne
Scott A. Chisholm: School of Medicine, Deakin University
Kathryn Matthews: School of Medicine, Deakin University
Boiyin Liu: Bio21 Institute, The University of Melbourne
Laure Dumont: Bio21 Institute, The University of Melbourne
Sarah C. Charnaud: Macfarlane Burnet Institute for Medical Research and Public Health
Molly Parkyn Schneider: Bio21 Institute, The University of Melbourne
Paul R. Gilson: Macfarlane Burnet Institute for Medical Research and Public Health
Tania F. de Koning-Ward: School of Medicine, Deakin University
Matthew W. A. Dixon: Bio21 Institute, The University of Melbourne
Leann Tilley: Bio21 Institute, The University of Melbourne

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract The malaria parasite, Plasmodium falciparum, displays the P. falciparum erythrocyte membrane protein 1 (PfEMP1) on the surface of infected red blood cells (RBCs). We here examine the physical organization of PfEMP1 trafficking intermediates in infected RBCs and determine interacting partners using an epitope-tagged minimal construct (PfEMP1B). We show that parasitophorous vacuole (PV)-located PfEMP1B interacts with components of the PTEX (Plasmodium Translocon of EXported proteins) as well as a novel protein complex, EPIC (Exported Protein-Interacting Complex). Within the RBC cytoplasm PfEMP1B interacts with components of the Maurer’s clefts and the RBC chaperonin complex. We define the EPIC interactome and, using an inducible knockdown approach, show that depletion of one of its components, the parasitophorous vacuolar protein-1 (PV1), results in altered knob morphology, reduced cell rigidity and decreased binding to CD36. Accordingly, we show that deletion of the Plasmodium berghei homologue of PV1 is associated with attenuation of parasite virulence in vivo.

Date: 2017
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DOI: 10.1038/ncomms16044

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