Extended Data Fig. 5: Comparison of the RUPA-154 and 10D8 binding sites on full-length Pfs48/45 from the cryoEM structure (a-c) and conservation of the RUPA-58 and RUPA-154 binding sites across Pf isolates (d-h). | Nature Structural & Molecular Biology

Extended Data Fig. 5: Comparison of the RUPA-154 and 10D8 binding sites on full-length Pfs48/45 from the cryoEM structure (a-c) and conservation of the RUPA-58 and RUPA-154 binding sites across Pf isolates (d-h).

From: Structural elucidation of full-length Pfs48/45 in complex with potent monoclonal antibodies isolated from a naturally exposed individual

Extended Data Fig. 5

(a) The variable domains of 10D8 and RUPA-154 bound to D1D2 with RUPA-154 (tan), 10D8 (dark gray), and shared (coral) D2 contact residues indicated with RUPA-154 (tan), 10D8 (dark gray), and shared (coral) D2 contact residues indicated. (b-c) Fabs RUPA-154 (b) and 10D8 (c) bound to full-length Pfs48/45. RUPA-154 (yellow) and 10D8 (grey) are depicted as ribbons and Pfs48/45 (blue) is represented as a surface. (d) Interfaces between Pfs48/45 (white) and RUPA-58 (pink) shown as ribbons, with D1 residues with polymorphisms labelled. (e-h) BLI binding curves of RUPA-58 bound to D1D2 WT (e) and mutants S90R (f), K101T (g), and N138I (h). Source data for panels e-h are available online.

Source data

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