Published 21 November 2005. doi:10.1083/jcb.200508051
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 4, 587-592
Signal-mediated export of proteins from the malaria parasite to the host erythrocyte
Matthias Marti1,
Jake Baum1,
Melanie Rug1,
Leann Tilley2, and
Alan F. Cowman1
1 The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3050, Australia
2 Department of Biochemistry, La Trobe University, Melbourne, Victoria 3000, Australia
Correspondence to Alan F. Cowman: cowman{at}wehi.edu.au
Abstract
Intracellular parasites from the genus Plasmodium reside and multiply in a variety of cells during their development. After invasion of human erythrocytes, asexual stages from the most virulent malaria parasite, P. falciparum, drastically change their host cell and export remodelling and virulence proteins. Recent data demonstrate that a specific NH2-terminal signal conserved across the genus Plasmodium plays a central role in this export process.
Abbreviations used in this paper: DBL, duffy binding-like; iRBC, infected RBC; KAHRP, knob-associated histidine-rich protein; PEXEL, Plasmodium export element; PfEMP, P. falciparum erythrocyte membrane protein; PHIST, Plasmodium helical interspersed subtelomeric family; PVM, parasitophorous vacuole membrane; RESA, ring-infected erythrocyte surface antigen.

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