Figure 4.
Affinity of VHH-Fc single-chain antibodies to RBD domains of SARS-CoV and SARS-CoV-2. (a) Bio-Layer Interferometry analysis of VHH-Fc immobilized proteins on anti-human Fc biosensors. Apparent binding kinetics of interaction between the VHH-Fc and the various RBD domains from SARS-CoV variants were evaluated in real time. Binding curves were fitted using a global 1:1 model. (b) Isoaffinity graph representation of kon and koff values for engineered clones and selected single, double and triple mutants, compared to the parental antibody and rimteravimab.
Alt Text: Affinity of VHH-Fc single-chain antibodies to RBD domains of SARS-CoV and SARS-CoV-2. (a) Table indicating the affinities of the VHH72 variants for the tested antigens. (b) graph representation of kon (x-axis) and koff (y-axis) values for engineered clones and selected single, double and triple mutants, compared to the parental antibody and rimteravimab. Engineered clones have much higher affinities, i.e., lower koff.
