Figure 4 | Scientific Reports

Figure 4

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

Figure 4

GT1b augments rHC/A-induced FGFR3c dimerization. BoNT/A binding domain (rHC/A) is more effective at dimerizing fluorescently tagged FGFR3c in the presence of exogenous ganglioside (GT1b) (green vs black, EC50 = 27 nM [95% CI; 18, 41] vs EC50 = 44 nM [95% CI; 36, 54]), and a BoNT/A binding domain (rHC/A) ganglioside mutant variant (W1266L;Y1267S) has further reduced ability to dimerize FGFR3c (red) (EC50 = 143 nM [95% CI; 127, 161]). Points represent the average normalized brightness values ± SD from greater than 30 cells collected on 4 independent days.

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