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MBC in Press, published online ahead of print January 26, 2003
Mol. Biol. Cell 10.1091/mbc.E02-04-0240

A more recent version of this article appeared on April 1, 2003 Originally published as MBC in Press, 10.1091/mbc.E02-04-0240 on February 6, 2003
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Submitted on April 30, 2002
Revised on December 3, 2002
Accepted on December 23, 2002

etramps, a new Plasmodium falciparum gene family coding for developmentally regulated and highly charged membrane proteins located at the parasite-host cell interface

Tobias Spielmann1, David J. P. Fergusen2, and Hans-Peter Beck3*

1 Department of Medical Parasitology and Infection Biology, Swiss Tropical Institute, Basel, Switzerland (present address: Queensland Institute of Medical Research, Brisbane Australia)
2 Nuffield Department of Pathology, University of Oxford, John Radcliffe Hospital, Oxford, UK
3 Department of Medical Parasitology and Infection Biology, Swiss Tropical Institute, Basel, Switzerland

* Corresponding author. E-mail address: Hans-Peter.Beck{at}unibas.ch.

After invasion of erythrocytes the human malaria parasite Plasmodium falciparum resides within a parasitophorous vacuole (PV) and develops from morphologically and metabolically distinct ring to trophozoite stages. During these developmental phases major structural changes occur within the erythrocyte, but neither the molecular events governing this development nor the molecular composition of the parasitophorous vacuole membrane (PVM) are well known. Here we describe a new family of highly cationic proteins from P. falciparum termed early transcribed membrane proteins (ETRAMPs). 13 members were identified sharing a conserved structure, of which 6 were found only during ring stages as judged from Northern and Western analysis. Other members showed different stage-specific expression patterns. Furthermore, ETRAMPs were associated with the membrane fractions in Western blots, and co-localization and selective permeabilization studies demonstrated that ETRAMPs were located in the PVM. This was confirmed by immuno-electron microscopy where the PVM and tubovesicular extensions of the PVM were labelled. Early expressed ETRAMPs clearly defined separate PVM domains when compared to the negatively charged integral PVM protein EXP-1, suggesting functionally different domains in the PVM with an oppositely charged surface coat. We also show that the dynamic change of ETRAMP composition in the PVM coincides with the morphological changes during development. The P. falciparum PVM is an important structure for parasite survival and its analysis might provide better understanding of the requirements of intracellular parasites.




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