Trafficking of the exported P. falciparum chaperone PfHsp70x

• Verfasst von: Rhiel, Manuel [VerfasserIn]
• Verfasst von: Lanzer, Michael [VerfasserIn]
• Verfasst von: 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
• Teil: year:2016
• Teil: 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
• DOI: doi:10.1038/srep36174
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1745201432

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.