title: Trafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX translocon.
abstract: Having entered the mature human erythrocyte, the malaria parasite survives and propagates within a parasitophorous vacuole, a membrane-bound compartment separating the parasite from the host cell cytosol. The bounding membrane of this vacuole, referred to as the parasitophorous vacuolar membrane (PVM), contains parasite-encoded proteins, but how these membrane proteins are trafficked to the PVM remains unknown. Here, we have studied the trafficking of PfExp1 to the PVM. We find that trafficking of PfExp1 to the PVM is independent of the folding state of the protein and also continues unabated upon inactivation of the PVM translocon Plasmodium Translocon of Exported proteins (PTEX). Our data strongly suggest that the trafficking of membrane proteins to the PVM occurs by as yet unknown mechanism, potentially unique to Plasmodium.
authors.affiliation: Department of Parasitology, University of Marburg, Marburg, Germany.
authors.forename: Anke
authors.initials: A
authors.lastname: Tribensky
authors.affiliation: Department of Parasitology, University of Marburg, Marburg, Germany.
authors.forename: Andreas W
authors.initials: AW
authors.lastname: Graf
authors.affiliation: Department of Parasitology, University of Marburg, Marburg, Germany.
authors.forename: Mathias
authors.initials: M
authors.lastname: Diehl
authors.affiliation: Department of Parasitology, University of Marburg, Marburg, Germany.
authors.forename: Wiebke
authors.initials: W
authors.lastname: Fleck
authors.affiliation: Department of Parasitology, University of Marburg, Marburg, Germany.
authors.forename: Jude M
authors.initials: JM
authors.lastname: Przyborski
mesh_terms: D000953:Antigens, Protozoan / Q000378:metabolism*; D002478:Cells, Cultured; D004912:Erythrocytes / Q000469:parasitology; D006801:Humans; D010963:Plasmodium falciparum / Q000502:physiology*; D017510:Protein Folding; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism*; D000069816:SEC Translocation Channels / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism* / Q000469:parasitology
chemical_list: D000953:Antigens, Protozoan; D015800:Protozoan Proteins; C063362:QF116 antigen, Plasmodium falciparum; D000069816:SEC Translocation Channels
keywords: Exp1; PTEX; malaria; parasitophorous vacuole; protein folding