The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking
Details
Publication Year 2003-07-21, Volume 162, Issue #2, Page 317-327
Journal Title
JOURNAL OF CELL BIOLOGY
Publication Type
Journal Article
Abstract
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.
Publisher
ROCKEFELLER UNIV PRESS
Keywords
HOST-CELL INVASION; SPOROZOITE SURFACE PROTEIN-2; ERYTHROCYTE BINDING ANTIGEN; PARASITE TOXOPLASMA-GONDII; MALARIA PARASITES; CIRCUMSPOROZOITE PROTEIN; GLIDING MOTILITY; GLYCOPHORIN-A; RECEPTOR; ORGANELLES
Rights Notice
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Creation Date: 2003-07-21 12:00:00
Last Modified: 0001-01-01 12:00:00
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