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


Marapana, DS; Dagley, LF; Sandow, JJ; Nebl, T; Triglia, T; Pasternak, M; Dickerman, BK; Crabb, BS; Gilson, PR; Webb, AI; Boddey, JA; Cowman, AF
2018-09
Nature Microbiology
Journal Article
3
9
1010-1022
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, plasmepsin V and PfSec62, which is an essential component of the post-translational ER translocon. Together, they form a distinct portal for the recognition and translocation of a large subset of Plasmodium export element effector proteins into the ER, thereby remodelling the infected erythrocyte that is required for parasite survival and pathogenesis.
Springer Nature
Infection and Immunity; Systems Biology and Personalised Medicine
10.1038/s41564-018-0219-2
30127496
Refer to copyright notice on published article.