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. 2022 Sep 24;13:5603. doi: 10.1038/s41467-022-33379-6

Fig. 1. Comparison of the epitopes of transmission-blocking antibodies 85RF45.1 and 32F3.

Fig. 1

A The structure of the C-terminal domain of Pfs48/45 (Pfs48/45-D3; blue) bound to antibody 32F3 (orange). The upper right inset shows a close-up of a Pfs48/45 loop which becomes ordered on 32F3 binding. The lower inset shows the equivalent view of the complex of Pfs48/45-D3 (blue) bound to 85RF45.1 (red). B An alignment of the structures of 32F3 (orange) and 85RF45.1 (red) bound to Pfs48/45-D3 (blue). C Surface plasmon resonance analysis of the binding of Pfs48/45-D3 to immobilised 32F3 and 85RF45.1. In both cases, the black lines show the responses due to a two-fold dilution series with a top concentration of 7.8 nM for 85RF45.1 and 125 nM for 32F3. The red dashed lines show fitting to a 1-to-1 binding model.