Journal article

A repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein trafficking

Emma McHugh, Steven Batinovic, Eric Hanssen, Paul J McMillan, Shannon Kenny, Michael DW Griffin, Simon Crawford, Katharine R Trenholme, Donald L Gardiner, Matthew WA Dixon, Leann Tilley



The malaria parasite Plasmodium falciparum dramatically remodels its host red blood cell to enhance its own survival, using a secretory membrane system that it establishes outside its own cell. Cisternal organelles, called Maurer's clefts, act as a staging point for the forward trafficking of virulence proteins to the red blood cell (RBC) membrane. The Ring-EXported Protein-1 (REX1) is a Maurer's cleft resident protein. We show that inducible knockdown of REX1 causes stacking of Maurer's cleft cisternae without disrupting the organization of the knob-associated histidine-rich protein at the RBC membrane. Genetic dissection of the REX1 sequence shows that loss of a repeat sequence domain resu..

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Funding Acknowledgements

We thank Courtney Zlatic for technical support, and Dr Megan Dearnley and Dr Aaron Jex, for useful discussions. We thank Prof Brian Cooke (Monash University), Prof Mike Ryan (Monash University), Catherine Braun-Breton (Universite Montpellier), Dr Tania de Koning-Ward (Deaking University) and Prof Alan Cowman (Walter & Eliza Hall Institute) for generously providing antibodies. We thank Paul Gilson and Brendan Elsworth (Burnet Institute) for providing the glmS plasmid. Microscopy was performed at the Melbourne Advanced Microscopy Facility and the Biological Optical Microscopy Platform, University of Melbourne. This work was supported by grants from the Australian Research Council and the Australian National Health & Medical Research Council. LT is an ARC Australian Professorial Fellow. MDWG is an ARC Future Fellow.