Journal article

Role of the Plasmodium Export Element in Trafficking Parasite Proteins to the Infected Erythrocyte

Justin A Boddey, Robert L Moritz, Richard J Simpson, Alan F Cowman

TRAFFIC | WILEY | Published : 2009

Abstract

The intracellular survival of Plasmodium falciparum within human erythrocytes is dependent on export of parasite proteins that remodel the host cell. Most exported proteins require a conserved motif (RxLxE/Q/D), termed the Plasmodium export element (PEXEL) or vacuolar targeting sequence (VTS), for targeting beyond the parasitophorous vacuole membrane and into the host cell; however, the precise role of this motif in export is poorly defined. We used transgenic P. falciparum expressing chimeric proteins to investigate the function of the PEXEL motif for export. The PEXEL constitutes a bifunctional export motif comprising a protease recognition sequence that is cleaved, in the endoplasmic reti..

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Grants

Awarded by National Institutes of Health


Awarded by Australian NHMRC


Awarded by NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES


Funding Acknowledgements

We thank Alex Maier and Matt O'Neill for pGlux.1, Andrew Pearce, for insightful discussions and critically reading the manuscript and the Red Cross Blood Service (Melbourne, Australia) for supplying erythrocytes. This work was supported by the National Health and Medical Research Council of Australia (NHMRC) and the National Institutes of Health (RO1 AI44008). Proteomic data analysis was supported by the Australian Proteomics Computational Facility funded by the Australian NHMRC under enabling grant no. 381413. J. A. B. is an NHMRC Peter Doherty Fellow and A. F. C. is a Howard Hughes International Research Scholar and NHMRC Australia Fellow.