Journal article

Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmic reticulum translocation interactome for export to the erythrocyte

Danushka S Marapana, Laura F Dagley, Jarrod J Sandow, Thomas Nebl, Tony Triglia, Michal Pasternak, Benjamin K Dickerman, Brendan S Crabb, Paul R Gilson, Andrew Webb, Justin A Boddey, Alan F Cowman

NATURE MICROBIOLOGY | NATURE PUBLISHING GROUP | Published : 2018

Abstract

Plasmodium falciparum exports hundreds of virulence proteins within infected erythrocytes, a process that requires cleavage of a pentameric motif called Plasmodium export element or vacuolar transport signal by the endoplasmic reticulum (ER)-resident protease plasmepsin V. We identified plasmepsin V-binding proteins that form a unique interactome required for the translocation of effector cargo into the parasite ER. These interactions are functionally distinct from the Sec61-signal peptidase complex required for the translocation of proteins destined for the classical secretory pathway. This interactome does not involve the signal peptidase (SPC21) and consists of PfSec61, PfSPC25, plasmepsi..

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Grants

Awarded by EMBO


Funding Acknowledgements

We thank the Red Cross Blood Service (Melbourne, Victoria, Australia) for the supply of donor blood for our cell culture. This work was supported by the NHMRC of Australia and the Victorian State Government Operational Infrastructure Support and the Australian Government NHMRC IRIISS. A.F.C. is a Howard Hughes International Scholar. M.P. was supported by the EMBO Long-Term Fellowship ALTF 793-2016.