Extended Data Fig. 1: Stoichiometry of the Rh5–CyRPA–Ripr complex, interaction with soluble or full-length basigin and JK-1 cells.

a, Chemical cross-linking of Rh5–CyRPA–Ripr complex by disuccinimidyl suberate (DSS), analysed on an SDS–PAGE. b, Negative-stain electron microscopy of purified Rh5–CyRPA–Ripr ternary complex, showing the elongated shape of the complex. c, Size-exclusion chromotography analysis of a mixture containing recombinant Rh5–CyRPA–Ripr complex and soluble basigin. Soluble basigin was eluted separately from the ternary complex, indicating no binding to basigin. d, Immuno-precipitation of Rh5–CyRPA (tagged with haemagglutinin (HA))–Ripr from parasite schizont-stage extract using anti-HA resins could not pull down soluble basigin. e, Native PAGE analysis of the size-exclusion chromotography (left) and anion-exchange chromatography (right) eluted fractions, showing the migration of the quaternary complex comprised Rh5–CyRPA–Ripr–full-length basigin, close to ~ 600 kDa. f, Western blot analysis of the ion-exchange chromatography elutions indicated the presence of full-length basigin in the complex. g, Size-exclusion chromotography analysis showed that Rh5 and Ripr are eluted separately from each other, which indicates that no complex is formed in the absence of CyRPA. h, Labelling of JK-1 and JK-1ΔBSG cells with anti-CD147 (basigin) and analysis using flow cytometry. i, Analysis of Rh5 (blue line), Rh5–CyRPA (red line) and Rh5–CyRPA–Ripr (green line) binding to JK-1 and JK-1ΔBSG (ΔBSG) cells. j, Differential solubilization showing that peripheral membrane protein (spectrin), integral membrane protein (glycophorin) and detergent-resistant membrane protein flotillin were localized in the sodium-bicarbonate-soluble, TX100-soluble and TX100-insoluble fractions, respectively. Experiments in a–j were repeated three times with biologically independent samples, and were reproducible.