Extended Data Fig. 4: CoV-X2 binds with low-nanomolar affinity to S mutants, including some mutants that are not recognized by the parental monoclonal antibodies C121 and C135. | Nature

Extended Data Fig. 4: CoV-X2 binds with low-nanomolar affinity to S mutants, including some mutants that are not recognized by the parental monoclonal antibodies C121 and C135.

From: Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice

Extended Data Fig. 4: CoV-X2 binds with low-nanomolar affinity to S mutants, including some mutants that are not recognized by the parental monoclonal antibodies C121 and C135.The alternative text for this image may have been generated using AI.

a, SPR-derived binding affinities of CoV-X2, C121 IgG and C135 IgG to several S trimer mutants. b, Mutations tested in a are indicated by yellow spheres on the surface representation of the S trimer. The epitopes of C121 (green) and C135 (blue) are shown.

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