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Published 21 July 2003. doi:10.1083/jcb.200301046
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© The Rockefeller University Press, 0021-9525/2003/7/317 $5.00
The Journal of Cell Biology, Volume 162, Number 2, 317-327

Article

 The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking

Tim-Wolf Gilberger, Jennifer K. Thompson, Michael B. Reed, Robert T. Good and Alan F. Cowman

The Walter and Eliza Hall Institute of Medical Research, Melbourne 3050, Australia

Address correspondence to Alan F. Cowman, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Melbourne 3050, Australia. Tel.: 61-3-9345 2555. Fax: 61-3-9347 0852. E-mail: cowman{at}wehi.edu.au

The invasion of host cells by the malaria parasite Plasmodium falciparum requires specific protein–protein interactions between parasite and host receptors and an intracellular translocation machinery to power the process. The transmembrane erythrocyte binding protein-175 (EBA-175) and thrombospondin-related anonymous protein (TRAP) play central roles in this process. EBA-175 binds to glycophorin A on human erythrocytes during the invasion process, linking the parasite to the surface of the host cell. In this report, we show that the cytoplasmic domain of EBA-175 encodes crucial information for its role in merozoite invasion, and that trafficking of this protein is independent of this domain. Further, we show that the cytoplasmic domain of TRAP, a protein that is not expressed in merozoites but is essential for invasion of liver cells by the sporozoite stage, can substitute for the cytoplasmic domain of EBA-175. These results show that the parasite uses the same components of its cellular machinery for invasion regardless of the host cell type and invasive form.

Key Words: malaria; micronemes; erythrocyte; function; substitution

* Abbreviation used in this paper: TRAP, thrombospondin-related anonymous protein.


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