Fig. 7: PTRAMP, CSS, and Ripr form a core invasion scaffold in Plasmodium spp.

a Cryo-EM 2D class averages of the PkPCR^tail complex. Addition of the 5B3 Fab fragment shows distinct density at the end of the Ripr tail (white triangle). Inset shows the PkPCR^tail complex colored according to the predicted structure. b AlphaFold 3 predicted structure (left) and cartoon schematic (right) of PkPCR^tail. Transmembrane domains, signal sequence and large disordered regions have been omitted for clarity. Inset shows the alignment of the PvPC (purple and dark green) structure and the PkPC predicted structure (pink and light green). c Erythrocyte binding assays of PkPC, PkRipr and PkPCR. Each color corresponds to one erythrocyte donor. PfRh5 was used as a positive control. Data from three independent experiments with three individual donors are shown with mean and SEM. d Erythrocyte binding assays of PkPC and PvPC using reticulocyte enriched cord blood. PvRBP2b was used as a positive control. Data from three independent experiments with three individual donors are shown with mean and SEM. e Schematic of the PCRCR complex of P. falciparum and PCR complexes of P. vivax, and P. knowlesi. PTRAMP, CSS and Ripr form a conserved three-membered complex that serves as a scaffold for an invasion complex. In P. falciparum this complex involves CyRPA and Rh5. In P. vivax and P. knowlesi this complex likely contains other components (dashed gray) that have yet to be identified, which engage with the erythrocyte membrane via host-cell specific receptors. Source data are provided as a Source Data file.