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Figure 2 | Malaria Journal

Figure 2

From: Quantification of Plasmodium-host protein interactions on intact, unmodified erythrocytes by back-scattering interferometry

Figure 2

Using backscattering interferometry to quantify Plasmodium -host protein interactions on intact, unmodified erythrocytes. A schematic illustrating how the BSI method was used to detect and quantify Plasmodium-host protein interactions at the surface of intact erythrocytes. Erythrocytes are used either unmodified (test samples), or modified to produce a non-binding reference (control samples) either by blocking specific receptors by pre-incubation with monoclonal antibodies (blue ovals), or, in the case of the PfEBA175-GYPA interaction, treated with neuraminidase. Both the control and test samples are independently incubated with varying concentrations of recombinant soluble Plasmodium ligands (green crescents) until binding equilibrium is reached and the binding signal is then quantified by backscattering interferometry. For each ligand concentration, the phase shift response in the control sample is subtracted from that in the test sample and plotted as a function of the ligand concentration. The equilibrium binding constant is calculated by curve fitting using a square hyperbolic function to the binding isotherm.

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