Fig. 4: A small region of Ripr is sufficient for PTRAMP-CSS binding in P. falciparum, P. vivax, and P. knowlesi. | Nature Communications

Fig. 4: A small region of Ripr is sufficient for PTRAMP-CSS binding in P. falciparum, P. vivax, and P. knowlesi.

From: PTRAMP, CSS and Ripr form a conserved complex required for merozoite invasion of Plasmodium species into erythrocytes

Fig. 4: A small region of Ripr is sufficient for PTRAMP-CSS binding in P. falciparum, P. vivax, and P. knowlesi.

a SDS-PAGE of recombinantly expressed PkPTRAMP, PkCSS and PkPC heterodimer. Purification was repeated at least three times with similar results. bd Representative biolayer interferometry sensorgrams of PkPC, PkPTRAMP, PkCSS and PkRipr binding assays. Dilution series data are shown in color and 1:1 model best fit is shown in black. e Mass distribution of PkPC and PkRipr after pre-incubation as measured by mass photometry. Histogram data are shown in gray and Gaussian curve fit in black. f The ability of Ripr and Ripr truncations to bind to PTRAMP-CSS in P. falciparum, P. vivax and P. knowlesi. The table shows the truncations used and their dissociation constant (KD, in nM, with standard error of the mean (SEM)) for binding their cognate heterodimer. N.B indicates no binding. Source data for all graphs are provided as a Source Data file.

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