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    Trafficking of the exported P. falciparum chaperone PfHsp70x

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    Author
    Rhiel, M; Bittl, V; Tribensky, A; Charnaud, SC; Strecker, M; Mueller, S; Lanzer, M; Sanchez, C; Schaeffer-Reiss, C; Westermann, B; ...
    Date
    2016-11-08
    Source Title
    Scientific Reports
    Publisher
    NATURE PUBLISHING GROUP
    University of Melbourne Author/s
    Crabb, Brendan; Charnaud, Sarah
    Affiliation
    Microbiology and Immunology
    Medical Biology (W.E.H.I.)
    Metadata
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    Document Type
    Journal Article
    Citations
    Rhiel, M., Bittl, V., Tribensky, A., Charnaud, S. C., Strecker, M., Mueller, S., Lanzer, M., Sanchez, C., Schaeffer-Reiss, C., Westermann, B., Crabb, B. S., Gilson, P. R., Kuelzer, S. & Przyborski, J. M. (2016). Trafficking of the exported P. falciparum chaperone PfHsp70x. SCIENTIFIC REPORTS, 6 (1), https://doi.org/10.1038/srep36174.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/258952
    DOI
    10.1038/srep36174
    Abstract
    Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.

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