title: The Plasmodium berghei translocon of exported proteins reveals spatiotemporal dynamics of tubular extensions.
abstract: The erythrocyte is an extraordinary host cell for intracellular pathogens and requires extensive remodelling to become permissive for infection. Malaria parasites modify their host red blood cells through protein export to acquire nutrients and evade immune responses. Endogenous fluorescent tagging of three signature proteins of the Plasmodium berghei translocon of exported proteins (PTEX), heat shock protein 101, exported protein 2 (EXP2), and PTEX88, revealed motile, tubular extensions of the parasitophorous vacuole that protrude from the parasite far into the red blood cell. EXP2 displays a more prominent presence at the periphery of the parasite, consistent with its proposed role in pore formation. The tubular compartment is most prominent during trophozoite growth. Distinct spatiotemporal expression of individual PTEX components during sporogony and liver-stage development indicates additional functions and tight regulation of the PTEX translocon during parasite life cycle progression. Together, live cell imaging and correlative light and electron microscopy permitted previously unrecognized spatiotemporal and subcellular resolution of PTEX-containing tubules in murine malaria parasites. These findings further refine current models for Plasmodium-induced erythrocyte makeover.
authors.affiliation: 1] Parasitology Unit, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany [2] Institute of Biology, Humboldt University, 10117 Berlin, Germany [3] Department of Medical Microbiology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands.
authors.forename: Joachim M
authors.initials: JM
authors.lastname: Matz
authors.affiliation: Microscopy Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Goosmann
authors.affiliation: Microscopy Core Facility, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.
authors.forename: Volker
authors.initials: V
authors.lastname: Brinkmann
authors.affiliation: Parasitology Unit, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.
authors.forename: Josephine
authors.initials: J
authors.lastname: Grützke
authors.affiliation: Parasitology Unit, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.
authors.forename: Alyssa
authors.initials: A
authors.lastname: Ingmundson
authors.affiliation: 1] Parasitology Unit, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany [2] Institute of Biology, Humboldt University, 10117 Berlin, Germany.
authors.forename: Kai
authors.initials: K
authors.lastname: Matuschewski
authors.affiliation: 1] Parasitology Unit, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany [2] Department of Medical Microbiology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands [3] Centre for Molecular and Biomolecular Informatics, Radboud Institute for Molecular Life Sciences, Radboud University Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands.
authors.forename: Taco W A
authors.initials: TW
authors.lastname: Kooij
mesh_terms: D004912:Erythrocytes / Q000378:metabolism / Q000469:parasitology; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D008018:Life Cycle Stages; D010962:Plasmodium berghei / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D006360:Heat-Shock Proteins; D015800:Protozoan Proteins