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. 2023 Jun 5;120(24):e2216612120. doi: 10.1073/pnas.2216612120

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Copyright © 2023 the Author(s). Published by PNAS.

This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).

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Fig. 6. — Structural validation of on-yeast epitope binning. (A) Binding of LM18 and Nb-C2-136 with respect to antibodies representing the three epitopes used for FACS-based binding. Nanobodies were displayed as ribbons and binning epitope antibodies as transparent surfaces. Comparison of (B) LM18-, (C) Nb-C2-136-, and (D) Nb-C4-255-binding sites on RBD with representative neutralizing antibodies (space-filled structures). Nanobody atoms predicted to clash with representative antibodies are colored in yellow. (E) Three different classes of nanobodies (LM18, Nb-C2-136, and Nb-C4-255) in complex with RBD. (F) NGS analysis and CDRH3 sequences from competitive sorts with CC12.1, CR3022, and CC6.30. Counts for C and NC population with the three antibodies are indicated.