5EZO

Crystal Structure of PfCyRPA in complex with an invasion-inhibitory antibody Fab.

5EZO の概要

• エントリーDOI: 10.2210/pdb5ezo/pdb
• 分子名称: PfCyRPA, c12 FAB, c12 Fab, ... (4 entities in total)
• 機能のキーワード: malaria inhibitory antibody, fab, immune system, cyrpa
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87144.38

構造登録者

Favuzza, P.,Pluschke, G.,Rudolph, M.G. (登録日: 2015-11-26, 公開日: 2017-01-11, 最終更新日: 2024-11-20)

主引用文献

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

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: 28195038
DOI: 10.7554/eLife.20383

実験手法

X-RAY DIFFRACTION (3.63 Å)