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