Fig. 1: Characterization of growth inhibitory activity and binding properties of a panel of anti-CyRPA mAbs.
From: Heterotypic interactions drive antibody synergy against a malaria vaccine candidate

A In vitro growth inhibitory activity (GIA) of monoclonal antibodies against the 3D7 clone of P. falciparum at 0.5 mg/ml, individual points indicate the value of each independent replicate, the bar indicates the mean, and errors bars indicate standard deviation across independent replicates (n = 2, Cy.002, Cy.005 and Cy.010, n = 3 Cy.003, Cy.004, Cy.007, Cy.009). B GIA dilution curve starting at 2 mg/ml of each inhibitory antibody, including chimeric human c12 and 8A7. Points show mean of triplicates and error bars indicate standard deviation. Curve fit used a four-parameter dose-response curve with the upper bound constrained to 100% GIA. All GIA curves were repeated at least twice with a single representative dilution curve shown here. C Competing interactions between mAbs based on the data in panel (D). Red box contains inhibitory mAbs and black lines indicate mAbs that compete with one another. D Competition matrix of all nine anti-CyRPA mAbs. The value contained in each box is the mean OD405 of a given mAb pair across triplicate; a value <0.25 was taken to be negative binding of the detection mAb. Competing combinations are highlighted in pink. Non-competing pairs are shown in blue. E Kinetic parameters for the binding of each antibody to CyRPA, as determined by surface plasmon resonance analysis.