Journal article

The N-terminus of EXP2 forms the membrane-associated pore of the protein exporting translocon PTEX in Plasmodium falciparum

Paul R Sanders, Benjamin K Dickerman, Sarah C Charnaud, Paul A Ramsland, Brendan S Crabb, Paul R Gilson

JOURNAL OF BIOCHEMISTRY | OXFORD UNIV PRESS | Published : 2019

Abstract

In order to facilitate a number of processes including nutrient acquisition and immune evasion, malaria parasites extensively remodel their host erythrocyte. This remodelling is to a large extent accomplished through protein export, a crucial process mediated by the Plasmodium translocon for exported proteins (PTEX) translocon which is comprised of three core components, HSP101, PTEX150 and EXP2. EXP2 has been structurally and electrophysiologically shown to form the pore that spans the vacuole membrane enveloping the parasite. Here, we biochemically investigate the structure and function of EXP2. By differential alkylation we provide direct evidence that cysteines C113 and C140 form an intr..

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Grants

Awarded by National Health and Medical Research Council of Australia


Funding Acknowledgements

This work was supported by the National Health and Medical Research Council of Australia [1092789; 1128198]. The authors gratefully acknowledge support from the Victorian Operational Infrastructure Support Program received by the Burnet Institute.