Fig. 3: Binding and neutralization of mAbs in terms of affinity, potency and breadth. | Nature Immunology

Fig. 3: Binding and neutralization of mAbs in terms of affinity, potency and breadth.

From: Targeted isolation of diverse human protective broadly neutralizing antibodies against SARS-like viruses

Fig. 3: Binding and neutralization of mAbs in terms of affinity, potency and breadth.

A total of 19 mAbs from donor CC25 and 11 mAbs from donor CC84 were selected to determine specificity, relative affinities and neutralization of sarbecoviruses and SARS-CoV-2 VOCs. a, Heatmap of binding responses (nM) determined by BLI using the SARS-CoV-1 and SARS-CoV-2 spike and S-protein domains and subdomains with IGHV gene usage for each mAb indicated. b, Heatmap of dissociation constants (Kd (M) values) for mAb binding to spike-derived monomeric RBDs from 4 sarbecovirus clades: clade 1b (n = 3); clade 1a (n = 3); clade 2 (n = 4); clade 3 (n = 2). Binding kinetics were obtained using the 1:1 binding kinetics fitting model in the ForteBio Data Analysis software (version 12.0). c, IC50 neutralization of mAbs against SARS-CoV-2, SARS-CoV-1, Pang17, WIV1 and SHC014 determined using pseudotyped viruses. d, Neutralization of 20 bnAbs against SARS-CoV-2 (Wuhan) and 5 major SARS-CoV-2 variants of concern (B.1.1.7 (Alpha), B.1.351 (Beta), P.1 (Gamma), B.1.617.2 (Delta) and B.1.1.529 (Omicron)). The SARS-CoV-2 Abs, CC12.1 and DH1047, and the Dengue Ab, DEN-3, were used as controls. Data are presented as the mean ± s.d. The experiments were performed independently twice and consistent results were obtained.

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