Hemoglobins S and C Interfere with actin remodeling in Plasmodium falciparum-infected erythrocytes

The hemoglobins S and C protect carriers from severe Plasmodium falciparum malaria. Here, we found that these hemoglobinopathies affected the trafficking system that directs parasite-encoded proteins to the surface of infected erythrocytes. Cryoelectron tomography revealed that the parasite generate...

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Hauptverfasser: Cyrklaff, Marek (VerfasserIn) , Sanchez, Cecilia P. (VerfasserIn) , Kilian, Nicole (VerfasserIn) , Frischknecht, Friedrich (VerfasserIn) , Lanzer, Michael (VerfasserIn)
Dokumenttyp: Article (Journal) Kapitel/Artikel
Sprache:Englisch
Veröffentlicht: 02 Dec 2011
In: Science
Year: 2011, Jahrgang: 334, Heft: 6060, Pages: 1283-1286
DOI:10.1126/science.1213775
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1126/science.1213775
Verlag, Volltext: http://science.sciencemag.org/content/334/6060/1283
Volltext
Verfasserangaben:Marek Cyrklaff, Cecilia P. Sanchez, Nicole Kilian, Cyrille Bisseye, Jacques Simpore, Friedrich Frischknecht, Michael Lanzer

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520 |a The hemoglobins S and C protect carriers from severe Plasmodium falciparum malaria. Here, we found that these hemoglobinopathies affected the trafficking system that directs parasite-encoded proteins to the surface of infected erythrocytes. Cryoelectron tomography revealed that the parasite generated a host-derived actin cytoskeleton within the cytoplasm of wild-type red blood cells that connected the Maurer’s clefts with the host cell membrane and to which transport vesicles were attached. The actin cytoskeleton and the Maurer’s clefts were aberrant in erythrocytes containing hemoglobin S or C. Hemoglobin oxidation products, enriched in hemoglobin S and C erythrocytes, inhibited actin polymerization in vitro and may account for the protective role in malaria. The malaria parasite mines actin from the membrane skeleton of its erythrocyte host to generate a cytoskeletal structure. 
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