Journal article
A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cell
M Gabriela, KM Matthews, C Boshoven, B Kouskousis, TK Jonsdottir, HE Bullen, J Modak, DL Steer, BE Sleebs, BS Crabb, TF de Koning-Ward, PR Gilson
Plos Pathogens | PUBLIC LIBRARY SCIENCE | Published : 2022
Abstract
Plasmodium falciparum exports ∼10% of its proteome into its host erythrocyte to modify the host cell's physiology. The Plasmodium export element (PEXEL) motif contained within the N-terminus of most exported proteins directs the trafficking of those proteins into the erythrocyte. To reach the host cell, the PEXEL motif of exported proteins is processed by the endoplasmic reticulum (ER) resident aspartyl protease plasmepsin V. Then, following secretion into the parasite-encasing parasitophorous vacuole, the mature exported protein must be unfolded and translocated across the parasitophorous vacuole membrane by the Plasmodium translocon of exported proteins (PTEX). PTEX is a protein-conducting..
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Grants
Awarded by National Health and Research Council
Funding Acknowledgements
T.K.J.is a recipient of the Melbourne Research Scholarshipand M.G.a recipientof a Deakin University Postgraduate Research Scholarship.T.F.dK-Wis an NHMRC Senior Research Fellow.B.E.S.is an Ellen Corin Fellow.We thank the NoraBaart Foundation for travel support for CB. This workwas supported by the Victorian Operational Infrastructure Support Program received by the Burnet Institute and National Health and Research Council grants1092789,1128198and 1197805(https://www.nhmrc.gov.au). The fundershad no role in studydesign,data collectionand analysis,decisiontopublish,or preparationof the manuscrip