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. 2024 Feb 5;15:1051. doi: 10.1038/s41467-024-45171-9

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a, b Top and side views of the cryo-EM map of Omicron BA.1 spike trimer with three 17T2 Fab fragments bound to three open RBDs, at 3.46 Å resolution. The core of the spike is shown in gray, the RBDs in pink, and the heavy chain (HC) and light chain (LC) of the 17T2 Fab in green and blue, respectively. c Structure of the RBD and 17T2 Fab after local refinement, at 4.41 Å resolution. The interaction zone between the RBD and the Fab is shown in cartoon representation where the three CDRs from each chain are distinctively colored and the N-glycosylation is indicated in orange. d CDRs that are involved in binding with RBD, specifically, interacting in the region of its left shoulder and neck (front and back view, respectively). e A detailed view of some of the residues involved in the interaction between 17T2 Fab and RBD. The main chains are colored in gray and the side chains of the residues involved in the interaction are shown in green for HC, in blue for LC, and in pink for RBD. f Locations of SARS-CoV-2 variant mutations on RBD relative to 17T2 epitope site that is shown as a black line (front and back view, respectively). The information about the variants and mutated residues can be found in Supplementary Table 4.