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Originally published In Press as doi:10.1074/jbc.M207039200 on November 26, 2002

J. Biol. Chem., Vol. 278, Issue 8, 6532-6542, February 21, 2003
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The Signal Sequence of Exported Protein-1 Directs the Green Fluorescent Protein to the Parasitophorous Vacuole of Transfected Malaria Parasites*

Akinola AdisaDagger , Melanie RugDagger , Nectarios KlonisDagger §, Michael FoleyDagger §, Alan F. Cowman, and Leann TilleyDagger §||

From the Dagger  Department of Biochemistry and § Co-operative Research Center for Diagnostics, La Trobe University, Bundoora, 3086, Victoria, Australia and  Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, PO RMH, 3052, Victoria, Australia

The malaria parasite, Plasmodium falciparum, spends part of its life cycle inside the erythrocytes of its human host. In the mature stages of intraerythrocytic growth, the parasite undertakes extensive remodeling of its adopted cellular home by exporting proteins beyond the confines of its own plasma membrane. To examine the signals involved in export of parasite proteins, we have prepared transfected parasites expressing a chimeric protein comprising the N-terminal region of the Plasmodium falciparum exported protein-1 appended to green fluorescent protein. The majority of the population of the chimeric protein appears to be correctly processed and trafficked to the parasitophorous vacuole, indicating that this is the default destination for protein secretion. Some of the protein is redirected to the parasite food vacuole and further degraded. Photobleaching studies reveal that the parasitophorous vacuole contains subcompartments that are only partially interconnected. Dual labeling with the lipid probe, BODIPY-TR-ceramide, reveals the presence of membrane-bound extensions that can bleb from the parasitophorous vacuole to produce double membrane-bound compartments. We also observed regions and extensions of the parasitophorous vacuole, where there is segregation of the lumenal chimera from the lipid components. These regions may represent sites for the sorting of proteins destined for the trafficking to sites beyond the parasitophorous vacuole membrane.


* This work was supported by the National Health and Medical Research Council, Australia.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed. Tel.: 61-3-94791375; Fax: 61-3-94792467; E-mail: L.Tilley@LaTrobe.edu.au.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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