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. 2019 Feb 5;36(3):47. doi: 10.1007/s11095-019-2574-y

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© The Author(s) 2019

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 1 — SPR binding analysis of soluble FcγRs to IgG. (a) Scheme depicting the assay setup. First, extracellular domains of HER2 were coated on a CM5 sensor chip. Then, HER2 specific human (blue structures) and porcine (orange structures) antibodies were captured on different flow cells. Their interactions with soluble porcine or human FcγRs were measured. The drawing shows low affinity FcγRs with two and the high affinity FcγRIa with three extracellular domains (oval shapes). (b) The graph shows the maximum response of 600 nM porcine (black bars) and human (grey bars) FcγRs obtained with huIgG1. (c) Real-time sensorgrams from SPR analysis. Interaction of IgG to poFcγRs is shown in the upper row and to huFcγRs in the lower row whereas the respective FcγRs are named above. Binding of 600 nM soluble FcγRs to trastuzumab (huIgG1, blue line), poIgG1a-HER2 (orange line), and poIgG3-HER2 (yellow line) is shown. Only the highest concentration of the titration with 600, 200, and 66.7 nM of soluble FcγRs is shown for clarity. (d) Interaction Map analysis resulting from trastuzumab binding to all concentrations of porcine and human FcγRs is shown in the upper and lower row, respectively. The binding is separated in several parallel interactions with unique kinetics, as displayed by spots on a graph with k_d on the x-axis and k_a on the y-axis. The heat map is a measure of the contribution from red = high to blue = low of each interaction to the total binding. No interaction was detected with poFcγRIIIa; therefore, it could not be analyzed (N/A).