Uncovering common principles in protein export of malaria parasites

Christof Grüring, Arlett Heiber, Florian Kruse, Sven Flemming, Gianluigi Franci, Sara F. Colombo, Elisa Fasana, Hanno Schoeler, Nica Borgese, Hendrik G. Stunnenberg, Jude M. Przyborski, Tim Wolf Gilberger, Tobias Spielmann

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

99 Citaten (Scopus)


For proliferation, the malaria parasite Plasmodium falciparum needs to modify the infected host cell extensively. To achieve this, the parasite exports proteins containing a Plasmodium export element (PEXEL) into the host cell. Phosphatidylinositol-3-phosphate binding and cleavage of the PEXEL are thought to mediate protein export. We show that these requirements can be bypassed, exposing a second level of export control in the N terminus generated after PEXEL cleavage that is sufficient to distinguish exported from nonexported proteins. Furthermore, this region also corresponds to the export domain of a second group of exported proteins lacking PEXELs (PNEPs), indicating shared export properties among different exported parasite proteins. Concordantly, export of both PNEPs and PEXEL proteins depends on unfolding, revealing translocation as a common step in export. However, translocation of transmembrane proteins occurs at the parasite plasma membrane, one step before translocation of soluble proteins, indicating unexpectedly complex translocation events at the parasite periphery.

Originele taal-2Engels
Pagina's (van-tot)717-729
Aantal pagina's13
TijdschriftCell Host and Microbe
Nummer van het tijdschrift5
StatusGepubliceerd - 15 nov. 2012
Extern gepubliceerdJa


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