Figure 4From: Quantification of Plasmodium-host protein interactions on intact, unmodified erythrocytes by back-scattering interferometry Backscattering interferometry detects the PfRH5-BSG interaction on intact unmodified erythrocytes. (A) Full-length PfRH5 was expressed and purified as a Cd4-tagged monomer and resolved under reducing conditions by SDS-PAGE. Coomassie staining revealed that the PfRH5-Cd4 preparation primarily consisted of the unprocessed full-length form. (B) Quantitation of PfRH5 binding to intact unmodified erythrocytes at equilibrium using BSI. Erythrocytes that were pre-coated with anti-BSG monoclonal antibody MEM-M6/6 (red circles) were used as control samples. Data points are means ± SD from seven independent experiments.Back to article page