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Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmic reticulum translocation interactome for

Danushka S Marapana1,2, Laura F Dagley1,2, Jarrod J Sandow1,2

  • 1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.

Nature Microbiology
|August 22, 2018
PubMed

Insights

This study identifies a unique protein complex essential for Plasmodium falciparum to export virulence factors into red blood cells. This pathway is crucial for parasite survival and disease pathogenesis.

Area of Science:

  • Molecular Biology
  • Parasitology
  • Cell Biology

Background:

  • Plasmodium falciparum exports numerous virulence proteins into infected erythrocytes.
  • Cleavage of the Plasmodium export element (PEE) by plasmepsin V is essential for this export.
  • The translocation mechanism for these effector proteins remains incompletely understood.

Purpose of the Study:

  • To identify proteins interacting with plasmepsin V.
  • To elucidate the mechanism of effector protein translocation into the parasite ER.
  • To characterize a novel pathway distinct from the classical secretory pathway.

Main Methods:

  • Proteomic analysis to identify plasmepsin V-binding proteins.
  • Investigating protein-protein interactions within the parasite ER.
  • Functional assays to determine the role of identified proteins in protein translocation.

Main Results:

  • A unique interactome involving PfSec61, PfSPC25, plasmepsin V, and PfSec62 was identified.
  • This interactome forms a distinct portal for PEE-containing effector protein translocation.
  • The identified pathway is functionally distinct from the Sec61-signal peptidase complex.

Conclusions:

  • A novel ER translocation machinery is essential for Plasmodium falciparum virulence.
  • This pathway facilitates the export of effector proteins, contributing to infected erythrocyte remodeling.
  • Targeting this pathway could offer new strategies against malaria.

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