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. Author manuscript; available in PMC: 2023 Feb 1.
Published in final edited form as: Nature. 2021 Dec 23;602(7898):664–670. doi: 10.1038/s41586-021-04386-2

Fig. 1. Omicron RBD shows increased binding to human ACE2 and gains binding to murine ACE2.

Fig. 1.

a, Omicron mutations are shown in a primary structure of SARS-CoV-2 S with domains and cleavage sites highlighted. b, Single-cycle kinetics SPR analysis of ACE2 binding to six RBD variants. ACE2 is injected successively at 11, 33, 100, and 300 nM (human) or 33, 100, 300, and 900 nM (mouse). Black curves show fits to a 1:1 binding model. White and gray stripes indicate association and dissociation phases, respectively. c, Quantification of human ACE2 binding data. Reporting average ± standard deviation of three replicates. Asterisks indicate that Delta was measured in a separate experiment with a different chip surface and capture tag; Delta fold-change is calculated relative to affinity of Wuhan-Hu-1 measured in parallel (91 ± 1.6 nM). d, Entry of Wu-Hu-1, Alpha, Beta, Delta, Gamma, Kappa and Omicron VSV pseudoviruses into mouse ACE2 expressing HEK293T cells. Shown are 2 biological replicates (technical triplicates). Lines, geometric mean.