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

Author

Sanchez, Cecilia P., primary, Patra, Pintu, additional, Chang, Shih‐Ying Scott, additional, Karathanasis, Christos, additional, Hanebutte, Lukas, additional, Kilian, Nicole, additional, Cyrklaff, Marek, additional, Heilemann, Mike, additional, Schwarz, Ulrich S., additional, Kudryashev, Mikhail, additional, and Lanzer, Michael, additional

Published
2021
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5. Structure of the merozoite surface protein 1 from Plasmodium falciparum

Author

Dijkman, Patricia M., Marzluf, Tanja, Zhang, Yingying, Chang, Shih-Ying Scott, Helm, Dominic, Lanzer, Michael, Bujard, Hermann, Kudryashev, Mikhail, Dijkman, Patricia M., Marzluf, Tanja, Zhang, Yingying, Chang, Shih-Ying Scott, Helm, Dominic, Lanzer, Michael, Bujard, Hermann, and Kudryashev, Mikhail

Abstract

The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity.

Published
2021

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

Author

Sanchez CP, Patra P, Chang SS, Karathanasis C, Hanebutte L, Kilian N, Cyrklaff M, Heilemann M, Schwarz US, Kudryashev M, and Lanzer M

Subjects
Erythrocytes metabolism, Histidine metabolism, Peptides metabolism, Protozoan Proteins metabolism, Actins metabolism, Plasmodium falciparum metabolism
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., (© 2021 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.)

Published
2022
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