Functional characterization of IFNAR1 variants in terms of the response to type I IFNs. (A–D) IFNAR1-deficient HEK293T cells transiently transfected with WT or mutant IFNAR1 cDNA constructs were stimulated with IFN-α subtypes (1,000 U/ml, A), glycosylated IFN-α2a or IFN-α14 (1,000 U/ml, B), non-glycosylated or glycosylated IFN-ω (1 ng/ml, C), or non-glycosylated or glycosylated IFN-β (100 U/ml) for 24 h, and luciferase activity was measured relative to WT. (E) Luciferase signal readings across a range of titrated concentrations of non-glycosylated or glycosylated IFN-β. The graphs show the mean ± SEM of two independent experiments.
Figure S2.

Functional characterization of IFNAR1 variants in terms of the response to type I IFNs. (A–D) IFNAR1-deficient HEK293T cells transiently transfected with WT or mutant IFNAR1 cDNA constructs were stimulated with IFN-α subtypes (1,000 U/ml, A), glycosylated IFN-α2a or IFN-α14 (1,000 U/ml, B), non-glycosylated or glycosylated IFN-ω (1 ng/ml, C), or non-glycosylated or glycosylated IFN-β (100 U/ml) for 24 h, and luciferase activity was measured relative to WT. (E) Luciferase signal readings across a range of titrated concentrations of non-glycosylated or glycosylated IFN-β. The graphs show the mean ± SEM of two independent experiments.

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