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Malaria parasite translocon structure and mechanism of effector export
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Malaria parasite translocon structure and mechanism of effector export
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Journal Article
Malaria parasite translocon structure and mechanism of effector export
2018
Overview
The putative
Plasmodium
translocon of exported proteins (PTEX) is essential for transport of malarial effector proteins across a parasite-encasing vacuolar membrane into host erythrocytes, but the mechanism of this process remains unknown. Here we show that PTEX is a bona fide translocon by determining structures of the PTEX core complex at near-atomic resolution using cryo-electron microscopy. We isolated the endogenous PTEX core complex containing EXP2, PTEX150 and HSP101 from
Plasmodium falciparum
in the ‘engaged’ and ‘resetting’ states of endogenous cargo translocation using epitope tags inserted using the CRISPR–Cas9 system. In the structures, EXP2 and PTEX150 interdigitate to form a static, funnel-shaped pseudo-seven-fold-symmetric protein-conducting channel spanning the vacuolar membrane. The spiral-shaped AAA+ HSP101 hexamer is tethered above this funnel, and undergoes pronounced compaction that allows three of six tyrosine-bearing pore loops lining the HSP101 channel to dissociate from the cargo, resetting the translocon for the next threading cycle. Our work reveals the mechanism of
P. falciparum
effector export, and will inform structure-based design of drugs targeting this unique translocon.
Cryo-electron microscopy analysis of the purified
Plasmodium
translocon of exported proteins (PTEX) reveals two distinct resolved states, suggesting a mechanism by which
Plasmodium falciparum
exports malarial effector proteins into erythrocytes.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 101/28
/ 101/58
/ 82/83
/ 96/31
/ 96/35
/ Animals
/ CRISPR
/ Drugs
/ Epitopes
/ Exports
/ Humanities and Social Sciences
/ Malaria
/ Malaria, Falciparum - drug therapy
/ Malaria, Falciparum - parasitology
/ Molecular Targeted Therapy - trends
/ Movement
/ Phenols (Class of compounds)
/ Plasmodium falciparum - chemistry
/ Plasmodium falciparum - metabolism
/ Plasmodium falciparum - ultrastructure
/ Protein Structure, Quaternary
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - metabolism
/ Protozoan Proteins - ultrastructure
/ Science
/ Tyrosine
