Journal article

Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150

Brendan Elsworth, Paul R Sanders, Thomas Nebl, Steven Batinovic, Ming Kalanon, Catherine Q Nie, Sarah C Charnaud, Hayley E Bullen, Tania F de Koning Ward, Leann Tilley, Brendan S Crabb, Paul R Gilson



The Plasmodium translocon for exported proteins (PTEX) has been established as the machinery responsible for the translocation of all classes of exported proteins beyond the parasitophorous vacuolar membrane of the intraerythrocytic malaria parasite. Protein export, particularly in the asexual blood stage, is crucial for parasite survival as exported proteins are involved in remodelling the host cell, an essential process for nutrient uptake, waste removal and immune evasion. Here, we have truncated the conserved C-terminus of one of the essential PTEX components, PTEX150, in Plasmodium falciparum in an attempt to create mutants of reduced functionality. Parasites tolerated C-terminal trunca..

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Awarded by National Health and Medical Research Council of Australia

Funding Acknowledgements

B. E. is recipient of an Australian Post Graduate Awards and S. C. C. is recipient of a Monash Graduate Scholarship. We thank the Australian Red Cross Blood Bank for the provision of human blood, Jacobus Pharmaceuticals for providing WR99210 and Monash Micro Imaging. We are grateful to Brian Cooke and Alan Cowman for the SBP and KAHRP antibodies to Eugene Kapp for providing the non-redundant LudwigNR protein database, respectively, and to Hnin (Honey) Pwint Oo for technical support. The authors gratefully acknowledge funding from the Victorian Operational Infrastructure Support Program received by the Burnet Institute and for grants from the National Health and Medical Research Council of Australia (1068287, 1021560 and 637406).