| Online-Ressource |
Verfasst von: | Rhiel, Manuel [VerfasserIn]  |
| Lanzer, Michael [VerfasserIn]  |
| Sanchez, Cecilia P. [VerfasserIn]  |
Titel: | Trafficking of the exported P. falciparum chaperone PfHsp70x |
Verf.angabe: | 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 |
E-Jahr: | 2016 |
Jahr: | 08 November 2016 |
Umfang: | 13 S. |
Teil: | volume:6 |
| year:2016 |
| extent:13 |
Fussnoten: | Gesehen am 21.10.2021 |
Titel Quelle: | Enthalten in: Scientific reports |
Ort Quelle: | [London] : Macmillan Publishers Limited, part of Springer Nature, 2011 |
Jahr Quelle: | 2016 |
Band/Heft Quelle: | 6(2016) Artikel-Nummer 36174, 13 Seiten |
ISSN Quelle: | 2045-2322 |
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. |
DOI: | doi:10.1038/srep36174 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1038/srep36174 |
| Volltext: https://www.nature.com/articles/srep36174 |
| DOI: https://doi.org/10.1038/srep36174 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1745201432 |
Verknüpfungen: | → Zeitschrift |
Trafficking of the exported P. falciparum chaperone PfHsp70x / Rhiel, Manuel [VerfasserIn]; 08 November 2016 (Online-Ressource)