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. 2021 Sep 27;12:747500. doi: 10.3389/fpls.2021.747500

FIGURE 3.

FIGURE 3

RBD-215 glycoforms display binding to ACE2-Fc. (A) ACE2-Fc ELISA. Binding curves of different concentrations of purified RBD-215 glycoforms and HEK293-derived tRBD (tRBD-HEK, positive control, Klausberger et al., 2021) to plates coated with ACE2-Fc. Values represent the mean ± SD (n = 3). (B) BLI analysis. Binding kinetics of the interaction between biotinylated ACE2-Fc loaded on SAX biosensors and SEC-purified monomeric RBD-215 glycoforms at a concentration range of 6.25–200 nM were determined. Representative real-time association and dissociation curves for RBD-215 ΔXF are shown. The individual curves show the association/dissociation at different concentrations of RBD-215 ΔXF. (C) KD values for the interactions between ACE2-Fc and the RBD-215 glycoforms. tRBD-HEK is included for comparison. Values represent the mean ± SEM (n = 3).