Fig. 6: Affinity characterization and neutralizing ability of bsAb15 against mutant pseudoviruses. | Nature Immunology

Fig. 6: Affinity characterization and neutralizing ability of bsAb15 against mutant pseudoviruses.

From: An engineered bispecific human monoclonal antibody against SARS-CoV-2

Fig. 6: Affinity characterization and neutralizing ability of bsAb15 against mutant pseudoviruses.

a, SPR kinetics analysis of the binding of antibodies to SARS-CoV-2 RBD mutants. Antibody was immobilized on protein A chips and then exposed to diluted SARS-CoV-2 RBD WT or mutants (K417N, N460S, E484K, E484A, N501Y or K417N/E484K/N501Y). The KD values are the mean ± s.d. in triplicate. b, In vitro neutralization activity of antibodies against WT and mutant pseudoviruses in Vero E6 cells. The curves were fit by the log (inhibitor) response of nonlinear regression and displayed as the means ± s.d. (n = 3). c, The RBD residues mutated in the different variants are indicated as red (K417 and N501), yellow (N460), orange (E484) and magenta (L452 and T478) spheres on the S trimer structure. The RBD (blue) and epitope of B38 (green) are shown in surface representation. d, Neutralization activity of antibodies against authentic Delta virus. The curves were fit by the log (inhibitor) response of nonlinear regression and are displayed as the means ± s.d. (n = 1).

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