Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex
Wilson Wong, Rick Huang, Sebastien Menant, Chuan Hong, Jarrod J Sandow, Richard W Birkinshaw, Julie Healer, Anthony N Hodder, Usheer Kanjee, Christopher J Tonkin, Denise Heckmann, Vladislav Soroka, Teit Max Moscote Sogaard, Thomas Jorgensen, Manoj T Duraisingh, Peter E Czabotar, Willem A de Jongh, Wai-Hong Tham, Andrew I Webb, Zhiheng Yu Show all
NATURE | NATURE PUBLISHING GROUP | Published : 2019
Plasmodium falciparum causes the severe form of malaria that has high levels of mortality in humans. Blood-stage merozoites of P. falciparum invade erythrocytes, and this requires interactions between multiple ligands from the parasite and receptors in hosts. These interactions include the binding of the Rh5-CyRPA-Ripr complex with the erythrocyte receptor basigin1,2, which is an essential step for entry into human erythrocytes. Here we show that the Rh5-CyRPA-Ripr complex binds the erythrocyte cell line JK-1 significantly better than does Rh5 alone, and that this binding occurs through the insertion of Rh5 and Ripr into host membranes as a complex with high molecular weight. We report a cry..View full abstract
We thank L. Chen, J. Thompson, E. Hanssen, A. Leis and P. de Fonseca for experimental assistance, and the Victorian Red Cross Blood Bank for blood. The data presented here were made possible through Victorian State Government Operational Infrastructure Support and Australian Government NHMRC IRIISS. The research was directly supported by a National Health and Medical Research Council of Australia (NHMRC).