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. 2022 Mar 17;22(6):813–820. doi: 10.1016/S1473-3099(22)00129-3

Table 2.

Neutralising potency of clinically relevant monoclonal antibodies against the SARS-CoV-2 omicron (B.1.1.529) variant

D614G IC50 (μg/mL) Omicron IC50 (μg/mL) Fold change in IC50 (omicron vs D614G) Mutations*
Casirivimab (REGN-10933)7 0·009 >10 >1100 417, 484, 493, 477, 478
Imdevimab (REGN-10987)7 0·008 >10 >1200 440, 446
Bamlanivimab (LY-CoV555)8 0·007 >10 >1400 484, 493, 478
Etesevimab (LY-CoV16)8 0·04 >10 >270 417, 493, 501, 505, 477
Sotrovimab (S309)9 0·1 0·2 2 339

IC50=50% inhibitory concentration.

*

Mutated amino acid positions modelled on the omicron receptor binding domain, proximal to the antibody interface, are listed.

Functional evidence (from deep mutational scanning data13) for an effect on antibody binding of mutations at that amino acid position.