Trafficking of the exported P. falciparum chaperone PfHsp70x

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dc.contributor.authorRhiel, Manuel
dc.contributor.authorBittl, Verena
dc.contributor.authorTribensky, Anke
dc.contributor.authorCharnaud, Sarah C
dc.contributor.authorStrecker, Maja
dc.contributor.authorMüller, Sebastian
dc.contributor.authorLanzer, Michael
dc.contributor.authorSanchez, Cecilia
dc.contributor.authorSchaeffer-Reiss, Christine
dc.contributor.authorWestermann, Benoit
dc.contributor.authorCrabb, Brendan S
dc.contributor.authorGilson, Paul R
dc.contributor.authorKülzer, Simone
dc.contributor.authorPrzyborski, Jude M
dc.date.accessioned2018-08-13T23:24:17Z
dc.date.available2018-08-13T23:24:17Z
dc.date.issued2016-11-08
dc.description.abstractPlasmodium 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.en_AU
dc.description.sponsorshipWork in the Przyborski lab is supported by the SPP1580, German Research Council (PR1099/3-2). SK was supported by a post-doctoral fellowship from the German Research Council.en_AU
dc.format13 pagesen_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn2045-2322en_AU
dc.identifier.urihttp://hdl.handle.net/1885/146279
dc.publisherNature Publishing Groupen_AU
dc.rights© The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/en_AU
dc.sourceScientific reportsen_AU
dc.subjectamino acid motifsen_AU
dc.subjecterythrocytesen_AU
dc.subjecthsp70 heat-shock proteinsen_AU
dc.subjecthumansen_AU
dc.subjectPlasmodium falciparumen_AU
dc.subjectprotein transporten_AU
dc.subjectprotozoan proteinsen_AU
dc.titleTrafficking of the exported P. falciparum chaperone PfHsp70xen_AU
dc.typeJournal articleen_AU
dcterms.accessRightsOpen Accessen_AU
dcterms.dateAccepted2016-10-07
local.bibliographicCitation.issue1en_AU
local.bibliographicCitation.startpage36174en_AU
local.contributor.affiliationKulzer, Simone, Research School of Biology, The Australian National Universityen_AU
local.contributor.authoremailprzybors@staff.uni-marburg.deen_AU
local.identifier.citationvolume6en_AU
local.identifier.doi10.1038/srep36174en_AU
local.identifier.essn2045-2322en_AU
local.identifier.uidSubmittedByu4579722en_AU
local.publisher.urlhttps://www.nature.com/en_AU
local.type.statusPublished Versionen_AU

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