Fig. 4: Antibodies which block the RH5:CyRPA interface are not growth inhibitory.
From: Heterotypic interactions drive antibody synergy against a malaria vaccine candidate
A Relative binding of 100 nM of each mAb to the reconstituted recombinant RCR complex divided by their binding to CyRPA at the same concentration, as determined by SPR analysis. Dotted line indicates relative binding of 1.0. B Crystal structure of RH5 (yellow) bound to Fab fragments of growth inhibitory mAb R5.016 (red) and CyRPA-blocking non-growth inhibitory mAb R5.015 (light blue). C Comparison of a model of the CyRPA:RH5 complex, derived from cryo-electron microscopy (PDB: 6MPV), with the structures of CyRPA bound to Cy.002 and RH5 bound to R5.015 shows that both Cy.002 and R5.015 will prevent the formation of the CyRPA:RH5 complex through a steric mechanism.
