| Autor: |
Paola Favuzza, Elena Guffart, Marco Tamborrini, Bianca Scherer, Anita M Dreyer, Arne C Rufer, Johannes Erny, Joerg Hoernschemeyer, Ralf Thoma, Georg Schmid, Bernard Gsell, Araceli Lamelas, Joerg Benz, Catherine Joseph, Hugues Matile, Gerd Pluschke, Markus G Rudolph |
| Jazyk: |
angličtina |
| Rok vydání: |
2017 |
| Předmět: |
|
| Zdroj: |
eLife, Vol 6 (2017) |
| Druh dokumentu: |
article |
| ISSN: |
2050-084X |
| DOI: |
10.7554/eLife.20383 |
| Popis: |
Invasion of erythrocytes by Plasmodial merozoites is a composite process involving the interplay of several proteins. Among them, the Plasmodium falciparum Cysteine-Rich Protective Antigen (PfCyRPA) is a crucial component of a ternary complex, including Reticulocyte binding-like Homologous protein 5 (PfRH5) and the RH5-interacting protein (PfRipr), essential for erythrocyte invasion. Here, we present the crystal structures of PfCyRPA and its complex with the antigen-binding fragment of a parasite growth inhibitory antibody. PfCyRPA adopts a 6-bladed β-propeller structure with similarity to the classic sialidase fold, but it has no sialidase activity and fulfills a purely non-enzymatic function. Characterization of the epitope recognized by protective antibodies may facilitate design of peptidomimetics to focus vaccine responses on protective epitopes. Both in vitro and in vivo anti-PfCyRPA and anti-PfRH5 antibodies showed more potent parasite growth inhibitory activity in combination than on their own, supporting a combined delivery of PfCyRPA and PfRH5 in vaccines. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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