5EZO
Crystal Structure of PfCyRPA in complex with an invasion-inhibitory antibody Fab.
Summary for 5EZO
| Entry DOI | 10.2210/pdb5ezo/pdb |
| Descriptor | PfCyRPA, c12 FAB, c12 Fab, ... (4 entities in total) |
| Functional Keywords | malaria inhibitory antibody, fab, immune system, cyrpa |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 87144.38 |
| Authors | Favuzza, P.,Pluschke, G.,Rudolph, M.G. (deposition date: 2015-11-26, release date: 2017-01-11, Last modification date: 2024-11-20) |
| Primary citation | Favuzza, P.,Guffart, E.,Tamborrini, M.,Scherer, B.,Dreyer, A.M.,Rufer, A.C.,Erny, J.,Hoernschemeyer, J.,Thoma, R.,Schmid, G.,Gsell, B.,Lamelas, A.,Benz, J.,Joseph, C.,Matile, H.,Pluschke, G.,Rudolph, M.G. Structure of the malaria vaccine candidate antigen CyRPA and its complex with a parasite invasion inhibitory antibody. Elife, 6:-, 2017 Cited by PubMed Abstract: Invasion of erythrocytes by merozoites is a composite process involving the interplay of several proteins. Among them, the 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. PubMed: 28195038DOI: 10.7554/eLife.20383 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.63 Å) |
Structure validation
Download full validation report
