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. 2022 Jan 20;38(6):110348. doi: 10.1016/j.celrep.2022.110348

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© 2022 The Authors

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Structures of S1-specific antibodies N-612-014 and N-612-004 bound to SARS-CoV-2 S

(A) Cryo-EM structure of the N-612-014-S trimer complex. Inset: top-down view of the complex.

(B) Close-up view of the N-612-014 variable domains (teal green) contacting the NTD (tan surface). The RBD (gray surface) of an adjacent protomer is shown as a reference.

(C) N-612-014 CDR loops (green ribbons) mapped onto the surface of the NTD (tan surface).

(D) Cartoon representation of the N-612-014-NTD interface.

(E) Surface and stick representations of the N-612-014 epitope (light green surface).

(F) Cryo-EM structure of the N-612-004-S1 protomer (inset) rigid body fit with individual S1 domains (cartoon).

(G) Cartoon and surface representations of N-612-004 (purple) recognition of the SD1 domain. Inset: N-612-004 epitope (pink sticks) highlighted on the SD1 surface (orange). Given the low resolution, epitope residues were assigned using a criterion of a distance of ≤7 Å between antibody-antigen Cα atoms.