Figure 5 | Scientific Reports

Figure 5

From: Characterization of clostridium botulinum neurotoxin serotype A (BoNT/A) and fibroblast growth factor receptor interactions using novel receptor dimerization assay

Figure 5

FGFR binding preference of rHC/A. (A) BoNT/A binding domain (rHC/A) (green) dimerizes fluorescently tagged FGFR1c with reduced potency compared to fluorescently tagged FGFR3c, EC50 163 nM (95% CI; 131, 202)* vs 27 nM (95% CI; 18, 41) (Fig. 3). A known native FGFR1c ligand, FGF4 (black) (positive control), dimerizes FGFR1c, EC50 = 17 nM [95% CI; 8, 35], while a known native FGFR2b ligand, FGF10 (red), does not. Points represent the average normalized brightness values ± SD from greater than 20 cells collected on 4 independent days. (B) BoNT/A binding domain (rHC/A) (green) dimerizes fluorescently tagged FGFR2b with reduced potency compared to fluorescently tagged FGFR3c, EC50 70 nM (95% CI; 59, 82) vs 27 nM (95% CI; 18, 41) (Fig. 3), respectively. A known native FGFR2b ligand, FGF10 (black) (positive control), dimerizes FGFR2b, EC50 = 19 nM (95% CI; 13, 26), while a known native FGFR1c ligand, FGF4 (red), does not. Points represent the average normalized brightness values ± SD from greater than 30 cells collected on 4 independent days. *Based on 2PL with bottom = 1, top = 2.

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