Journal article

Targeted mutagenesis of the ring-exported protein-1 of Plasmodium falciparum disrupts the architecture of Maurer's cleft organelles

Eric Hanssen, Paula Hawthorne, Matthew WA Dixon, Katharine R Trenholme, Paul J McMillan, Tobias Spielmann, Donald L Gardiner, Leann Tilley

MOLECULAR MICROBIOLOGY | WILEY | Published : 2008

Abstract

Mature red blood cells have no internal trafficking machinery, so the intraerythrocytic malaria parasite, Plasmodium falciparum, establishes its own transport system to export virulence factors to the red blood cell surface. Maurer's clefts are parasite-derived membranous structures that form an important component of this exported secretory system. A protein with sequence similarity to a Golgi tethering protein, referred to as ring-exported protein-1 (REX1), is associated with Maurer's clefts. A REX1-GFP chimera is trafficked to the Maurer's clefts and preferentially associates with the edges of these structures, as well as with vesicle-like structures and with stalk-like extensions that ar..

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Funding Acknowledgements

We would like to thank the following colleagues for providing for antibodies: Cornelia Spycher and Peter Beck (anti-MAHRP1), Claudia Daubenberger (anti-GAPDH), Swiss Tropical Institute, Brian Cooke, Monash University (anti-SBP1) and Mike Ryan, La Trobe University (rabbit anti-GFP). We thank Dr Kenneth Goldie, Microscopy and Nanobiotechnology Centre, Bio21 Institute, for help with the electron tomography, Sam Deed, La Trobe University, for technical support and Dr Gregor Anderluh, University of Ljubljana, Slovenia, for supplying the Eqtll expression construct. This work was supported by funds from the Australian Research Council and the National Health and Medical Research Council of Australia. M.W.A.D. is supported by an ANZ Trustees PhD scholarship. T.S. gratefully acknowledges the Swiss National Science Foundation and the Alexander von Humboldt Foundation. D.G. and K.T. gratefully acknowledge support from Australian NHMRC and Mark Nicholson, Alice Hill and The Tudor Foundation. P.L.H. was funded by an NHMRC postgraduate scholarship.