Extended Data Fig. 10. Nanobody recognition of PfCSS and sequence conservation of PfCSS and PfPTRAMP.

a. D2 contacts an N-linked glycan on Asn88 of recombinant PfCSS. Interacting residues are shown as sticks. b. Representative sensorgram and 1:1 model best fit (black) for D2 binding to non-glycosylated PTRAMP-CSS determined by biolayer interferometry. A 2-fold dilution series was used, starting at 500 nM (light pink), 250 nM (lilac), 125 nM (purple), 62.5 nM (cyan). c. Superposition of the D1 domains from the D2-PfCSS and H2-PfCSS structures showing the β-strand is replaced by the H2 CDR3. d. Weblogo representation of PfCSS sequence diversity from 212 sequences from the PlasmoDB⁵⁵. D2 and H2 interacting residues are denoted with teal and pink circles, respectively. e. Weblogo representation of PfPTRAMP sequence diversity from 214 sequences from the PlasmoDB.