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. 2023 Feb 14;56(2):420–432.e7. doi: 10.1016/j.immuni.2023.01.013

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© 2023 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

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Structural delineation of antibodies bound to low-potency Pfs230 D1+ epitopes

(A) Overall structure of Pfs230 D1+ (gray) bound by Fab of RUPA-38 (orange).

(B–D) The RUPA-38 epitope on Pfs230 D1+ is colored in orange. Overall structures of Pfs230 D1+ (white) bound by (C) Fab 15C5 (green) and (D) Fab LMIV230-02 (pink).

(E) Adjacent (green and pink) and partially overlapping (black) residues on Pfs230 D1+ are shown. All epitope residues from (B) and (E) are labeled, and side chains are shown as stick representation. SNPs occurring within the epitopes are labeled along with their allele frequency (Table 1).

(F–I) The high-resolution structure of Pfs230 D1+ (2.0 Å) from the LMIV230-02 complex and (G) a theoretical model of Pfs230 domains 1 (D1) and 2 (D2) (residues 552–889) generated using RoseTTAfold.²⁷ Superposition of Fabs (H) 15C5 and (I) LMIV230-02 on the model of Pfs230 D1D2, based on the binding sites shown in (C) and (D), shows clear clashing between the Fabs and D2. See also Figures S3 and S6.