Targeting of the Ring Exported Protein 1 to the Maurer's Clefts is Mediated by a Two-Phase Process

Early development of Plasmodium falciparum within the erythrocyte is characterized by the large-scale export of proteins to the host cell. In many cases, export is mediated by a short sequence called the Plasmodium export element (PEXEL) or vacuolar transport signal; however, a number of previously...

Full description

Saved in:
Bibliographic Details
Published in:Traffic (Copenhagen, Denmark) Denmark), 2008-08, Vol.9 (8), p.1316-1326
Main Authors: Dixon, Matthew W.A, Hawthorne, Paula L, Spielmann, Tobias, Anderson, Karen L, Trenholme, Katharine R, Gardiner, Donald L
Format: Article
Language:English
Subjects:
Animals
Animals, Genetically Modified
Cytosol - metabolism
DNA Primers - chemistry
Erythrocytes - parasitology
Green Fluorescent Proteins - metabolism
host-cell remodelling
malaria
Maurer's clefts
Microscopy, Fluorescence
Models, Biological
PEXEL
Plasmodium falciparum - metabolism
Plasmodium falciparum - physiology
Protein Transport
Protozoan Proteins - chemistry
Protozoan Proteins - metabolism
ring stage
Transfection
Vacuoles - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Early development of Plasmodium falciparum within the erythrocyte is characterized by the large-scale export of proteins to the host cell. In many cases, export is mediated by a short sequence called the Plasmodium export element (PEXEL) or vacuolar transport signal; however, a number of previously characterized exported proteins do not contain such an element. In this study, we investigated the mechanisms of export of the PEXEL-negative ring exported protein 1 (REX1). This protein localizes to the Maurer's clefts, parasite-induced structures in the host-cell cytosol. Transgenic parasites expressing green fluorescent protein-REX1 chimeras revealed that the single hydrophobic stretch plus an additional 10 amino acids mediate the export of REX1. Biochemical characterization of these chimeras indicated that REX1 was exported as a soluble protein. Inclusion of a sequence containing a predicted coiled-coil motif led to the correct localization of REX1 at the Maurer's clefts, suggesting that association with the clefts occurs at the final stage of protein export only. These results indicate that PEXEL-negative exported proteins can be exported in a soluble state and that sequences without any apparent resemblance to a PEXEL motif can mediate export across the parasitophorous vacuole membrane.
ISSN:1398-9219
1600-0854
DOI:10.1111/j.1600-0854.2008.00768.x