Fig. 1

Recognition of Pfs48/45 6C by potent transmission-blocking mAb 85RF45.1. a Domain organization of Pfs48/45. In the zoom in view of the Pfs48/45 6C domain, the dark orange regions represent areas contacted by mAb 85RF45.1. Red lines indicate the disulfide bonding pattern. SP signal peptide, ep epitope, GPI glycosylphosphatidylinositol anchor. b Overview of the 85RF45.1 Fab-Pfs48/45 6C co-crystal structure rendered as secondary structure cartoon and surface. The orange mesh represents the composite omit electron density map rendered at a 1.2σ contour level around Pfs48/45 6C. The six-cysteine residues in Pfs48/45 6C are shown as red sticks. The 85RF45.1 light and heavy chains are colored teal and magenta, respectively. Only the Fab variable region is shown for clarity. c Residues of the 85RF45.1 epitope on Pfs48/45 (dark orange surface) are recognized by all six CDRs (secondary structure cartoon). The insets show residues involved in H-bonds and salt bridges (black dashes). Colors are as in b