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

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Version 3 2024-06-18, 02:47
Version 2 2024-06-04, 07:15
Version 1 2017-07-17, 11:19
journal contribution
posted on 2024-06-18, 02:47 authored by S Batinovic, E McHugh, SA Chisholm, Kat MatthewsKat Matthews, B Liu, L Dumont, SC Charnaud, MP Schneider, PR Gilson, Tania De Koning-WardTania De Koning-Ward, MWA Dixon, L Tilley
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.

History

Journal

Nature Communications

Volume

8

Article number

ARTN 16044

Pagination

1 - 14

Location

England

Open access

  • Yes

ISSN

2041-1723

eISSN

2041-1723

Language

English

Publication classification

C Journal article, C1 Refereed article in a scholarly journal

Copyright notice

2017, The Authors

Issue

1

Publisher

NATURE PUBLISHING GROUP