Trafficking of the exported P. falciparum chaperone PfHsp70x
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 membr...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
08 November 2016
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| In: |
Scientific reports
Year: 2016, Volume: 6 |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep36174 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/srep36174 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/srep36174 
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| Author Notes: | Manuel Rhiel, Verena Bittl, Anke Tribensky, Sarah C. Charnaud, Maja Strecker, Sebastian Müller, Michael Lanzer, Cecilia Sanchez, Christine Schaeffer-Reiss, Benoit Westermann, Brendan S. Crabb, Paul R. Gilson, Simone Külzer & Jude M. Przyborski |
| Summary: | 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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| Item Description: | Gesehen am 21.10.2021 |
| Physical Description: | Online Resource |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep36174 |