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. 2019 Jun 26;11(6):1012–1024. doi: 10.1080/19420862.2019.1624464

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© 2019 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 2. — Binding of model BsAbs of different IgG subclasses to Fc receptors.

The binding to FcRn and FcγRI of was determined by AlphaScreen^TM competition assay in comparison to a WT huIgG1 (grey stars). In such assays, a higher IC₅₀ value translates to a weaker binding to the tested FcR. A: Dose-response of FcRn binding. Curves show the competition of CD19xCD3 BsAbs of one representative experiment (single measurement per concentration). The error bars represent the SD of the WT-control which was measured on multiple plates.B: IC₅₀ values of FcRn binding. CD19xCD3 (open circles), CD19xRSV (open squares) and RSVxCD3 (open diamonds) BsAbs were grouped by Fc and individual values are plotted from two independent experiments. Lines represent the mean IC₅₀ ± standard deviation (SD) through all tested molecules per Fc.C: Dose-response of FcγRI binding. Curves show the competition of CD19xCD3 BsAbs of one representative experiment (single measurement per concentration). The error bars represent the SD of the WT-control which was measured on multiple plates.D: IC₅₀ values of FcγRI binding. CD19xCD3 (open circles), CD19xRSV (open squares) and RSVxCD3 (open diamonds) BsAbs were grouped by Fc and individual values are plotted from two independent experiments. Lines represent the mean IC₅₀ ± standard deviation (SD) through all tested molecules per Fc.n. c.: no competition for binding to FcγRI was observed at the highest applied concentration (2666 nM) for BsAbs containing an IgG2 σ1 Fc.