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KAHRP dynamically relocalizes to remodeled actin junctions and associates with knob spirals in Plasmodium falciparum-infected erythrocytes

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 erythr...

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Main Authors: Sanchez, Cecilia P. (Author) , Patra, Pintu (Author) , Chang, Shih-Ying Scott (Author) , Karathanasis, Christos (Author) , Hanebutte, Lukas (Author) , Kilian, Nicole (Author) , Cyrklaff, Marek (Author) , Heilemann, Mike (Author) , Schwarz, Ulrich S. (Author) , Kudryashev, Mikhail (Author) , Lanzer, Michael (Author)
Format: Article (Journal)
Language:English
Published: 2022
In: Molecular microbiology
Year: 2022, Volume: 117, Issue: 2, Pages: 274-292
ISSN:1365-2958
DOI:10.1111/mmi.14811
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1111/mmi.14811
Verlag, kostenfrei, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.14811
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Author Notes: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
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Summary: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.
Item Description:First published: 13 September 2021
Gesehen am 23.05.2022
Physical Description:Online Resource
ISSN:1365-2958
DOI:10.1111/mmi.14811

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