Fig. 2: Enhanced avidity binding and virus neutralization for 14-H-06. | Nature Communications

Fig. 2: Enhanced avidity binding and virus neutralization for 14-H-06.

From: Engineering SARS-CoV-2 specific cocktail antibodies into a bispecific format improves neutralizing potency and breadth

Fig. 2

a A diagram showing the binding models of 14-H-06 to tethered RBD antigen at the concentrations of 40 ng/ml (left), 200 ng/ml (middle) and 1,000 ng/ml (right). The avidity effects manifest as multivalent interactions between an antibody and multiple RBDs. b Summary of the association (Kon), dissociation (Kdis) and avidity (KD) of indicated antibodies at indicated concentrations RBD. c The plots of relative association, dissociation and avidity for each antibody. The relative values for each antibody were obtained by normalizing the values of 1/KD, Kon and 1/Kdis at RBD concentrations of 200 ng/ml and 1000 ng/ml against the corresponding values at RBD concentration of 40 ng/ml. d Neutralization titrations of indicated antibodies against live SARS-CoV-2 on Vero E6 cell. Data points are from duplicate wells. e Antibody blocking of RBD interaction with ACE2 determined by the BLI assay.

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