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Verfasst von:Sanchez, Cecilia P. [VerfasserIn]   i
 Patra, Pintu [VerfasserIn]   i
 Chang, Shih-Ying Scott [VerfasserIn]   i
 Karathanasis, Christos [VerfasserIn]   i
 Hanebutte, Lukas [VerfasserIn]   i
 Kilian, Nicole [VerfasserIn]   i
 Cyrklaff, Marek [VerfasserIn]   i
 Heilemann, Mike [VerfasserIn]   i
 Schwarz, Ulrich S. [VerfasserIn]   i
 Kudryashev, Mikhail [VerfasserIn]   i
 Lanzer, Michael [VerfasserIn]   i
Titel:KAHRP dynamically relocalizes to remodeled actin junctions and associates with knob spirals in Plasmodium falciparum-infected erythrocytes
Verf.angabe:Cecilia P. Sanchez, Pintu Patra, Shih-Ying Scott Chang, Christos Karathanasis, Lukas Hanebutte, Nicole Kilian, Marek Cyrklaff, Mike Heilemann, Ulrich S. Schwarz, Mikhail Kudryashev, Michael Lanzer
Jahr:2022
Umfang:19 S.
Fussnoten:First published: 13 September 2021 ; Gesehen am 23.05.2022
Titel Quelle:Enthalten in: Molecular microbiology
Ort Quelle:Oxford [u.a.] : Wiley-Blackwell, 1987
Jahr Quelle:2022
Band/Heft Quelle:117(2022), 2, Seite 274-292
ISSN Quelle:1365-2958
Abstract:The knob-associated histidine-rich protein (KAHRP) plays a pivotal role in the pathophysiology of Plasmodium falciparum malaria by forming membrane protrusions in infected erythrocytes, which anchor parasite-encoded adhesins to the membrane skeleton. The resulting sequestration of parasitized erythrocytes in the microvasculature leads to severe disease. Despite KAHRP being an important virulence factor, its physical location within the membrane skeleton is still debated, as is its function in knob formation. Here, we show by super-resolution microscopy that KAHRP initially associates with various skeletal components, including ankyrin bridges, but eventually colocalizes with remnant actin junctions. We further present a 35 Å map of the spiral scaffold underlying knobs and show that a KAHRP-targeting nanoprobe binds close to the spiral scaffold. Single-molecule localization microscopy detected 60 KAHRP molecules/knob. We propose a dynamic model of KAHRP organization and a function of KAHRP in attaching other factors to the spiral scaffold.
DOI:doi:10.1111/mmi.14811
URL:kostenfrei: Volltext: https://doi.org/10.1111/mmi.14811
 kostenfrei: Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.14811
 DOI: https://doi.org/10.1111/mmi.14811
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:actin
 ankyrin
 erythrocyte
 malaria
 microscopy
 virulence factor
K10plus-PPN:1804098280
Verknüpfungen:→ Zeitschrift
 
 
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