dc.contributor.author
Matz, Joachim M.
dc.contributor.author
Goosmann, Christian
dc.contributor.author
Brinkmann, Volker
dc.contributor.author
Grützke, Josephine
dc.contributor.author
Ingmundson, Alyssa
dc.contributor.author
Matuschewski, Kai
dc.contributor.author
Kooij, Taco W. A.
dc.date.accessioned
2018-06-08T07:16:07Z
dc.date.available
2015-08-31T10:26:10.437Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/17536
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-21420
dc.description.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.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit
dc.title
The Plasmodium berghei translocon of exported proteins reveals spatiotemporal
dynamics of tubular extensions
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Scientific Reports. - 5 (2015), Artikel Nr. 12532
dcterms.bibliographicCitation.doi
10.1038/srep12532
dcterms.bibliographicCitation.url
http://www.nature.com/articles/srep12532
refubium.affiliation
Charité - Universitätsmedizin Berlin
de
refubium.mycore.fudocsId
FUDOCS_document_000000023007
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000005334
dcterms.accessRights.openaire
open access