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Members of the Low‐Molecular‐Mass Rhoptry Protein Complex of Plasmodium falciparum Bind to the Surface of Normal Erythrocytes

Y. Sterkers 1 C. Scheidig 1 M. da Rocha 1 C. Lepolard 2 J. Gysin 2 Artur Scherf 1, *
* Auteur correspondant
2 EA3282 - parasitologie expérimentale
Université de la Méditerranée - Aix-Marseille 2, Institut Pasteur [Paris]
Abstract : The destruction of erythrocytes is one of the most frequently observed causes of severe malarial anemia. Recently, we showed that tagging normal erythrocytes and cells of erythroid precursors with rhoptry-derived proteins can trigger their destruction. In the present study, we used rhoptry-associated protein (RAP)-1 and RAP-3 gene-disruption mutant Plasmodium falciparum parasites and showed that 2 members of a rhoptry protein complex, RAP-1 and RAP-2, bind to the surface of normal erythrocytes. Surface iodination experiments showed that RAP-1 but not RAP-3 mutant parasites lose their capacity to tag erythrocytes. This work opens new doors into the investigation of the molecular mechanism of anemia in patients with malaria.
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https://hal.umontpellier.fr/hal-02507476
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Soumis le : vendredi 13 mars 2020 - 11:17:40
Dernière modification le : mercredi 18 mars 2020 - 01:32:26

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Y. Sterkers, C. Scheidig, M. da Rocha, C. Lepolard, J. Gysin, et al.. Members of the Low‐Molecular‐Mass Rhoptry Protein Complex of Plasmodium falciparum Bind to the Surface of Normal Erythrocytes. Journal of Infectious Diseases, Oxford University Press (OUP), 2007, 196 (4), pp.617-621. ⟨10.1086/519685⟩. ⟨hal-02507476⟩

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