Affinity of human IgG subclasses to mouse Fc gamma Receptors

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Affinity of human IgG subclasses to mouse Fc gamma Receptors Supplementary figures and tables for: Affinity of human IgG subclasses to mouse Fc gamma Receptors Gillian Dekkers, Arthur E.H. Bentlage, Tamara C. Stegmann, Heather L. Howie, Suzanne Lissenberg- Thunnissen, James Zimring, Theo Rispens and Gestur Vidarsson

Dekkers et al. supplementary Figure 1 Supplementary Fig. 1 Sensorgram of mouse IgG subclasses binding to mouse FcγR Each mouse IgG subclasses in concentration ranges from 3.9 nM to 1140 nM flown over different spotted mouse FcγR, only the sensorgrams for the highest ligand concentration of the different mouse FcγR are shown; FcgRI 30nM, mFcgRIIb 100nM, FcgRIII 100nM and mFcgIV 30nM.

Dekkers et al. Supplementary Figure 2 Supplementary Fig. 2 Sensorgram of human IgG subclasses binding to mouse FcγR Each human IgG subclasses in concentration ranges from 1.5 nM to 3000 nM for human IgG1 and IgG3, from 15.6 nM to 2000 nM for human IgG2, or from 23.4 nM to 3000 nM for human IgG4, flown over different spotted mouse FcγR, only the sensorgrams for the highest ligand concentration of the different mouse FcγR are shown; FcgRI 30nM, mFcgRIIb 100nM, FcgRIII 100nM and mFcgIV 30nM.

Dekkers et al. Supplementary Figure 3 Supplementary Fig. 3 Binding of human IgG subclasses to mouse FcγR The human IgG1, IgG2 and IgG3 anti-pneumococcal (Gdob1) and IgG4 anti birch antigen (BetV1) were assessed for their binding affinity in KD (M) to the mouse FcγRI, FcγRIIb, FcγRIII and FcγRIV by SPR. -/- denotes no binding detected, * denotes binding > 3 μM, represented by the horizontal dashed line which indicates the maximum concentration of IgG which is used. Data represents means and SEM of n=2.

Dekkers et al. Supplementary Figure 4 Anti-RhD hIgG1 Anti-RhD hIgG2 Anti-RhD hIgG3 Anti-RhD hIgG4 FcγRI 5.2x10-9 -/- 4.5x10-9 7.0x10-9 FcγRIIa131H 9.8x10-8 1.0x10-7 1.9x10-7 1.9x10-6 FcγRIIa131R 6.8x10-8 4.9x10-7 1.7x10-7 3.9x10-7 FcγRIIb 1.3x10-7 * 5.9x10-7 3.1x10-7 FcγRIIIa158F 4.3x10-7 1.1x10-6 * FcγRIIIa158V FcγRIIIb NA1 2.7x10-7 8.7x10-7 FcγRIIIb NA2 7.4x10-7 b Supplementary Fig. 4 Affinity of human IgG subclasses to human FcγR a, b) Affinity in KD (M) of human anti-RhD IgG subclasses to human FcγR family. -/- denotes no binding detected, * denotes binding > 2μM, represented by the horizontal dashed line which indicates the maximum concentration of IgG which is used. Data is single representative of n=3.

Dekkers et al. Supplementary Table 1 Comparison of affinity in KD (μM) of mouse IgG subclasses for mouse FcγRs from this research versus literature. Data obtained in this research in bold type, S.E.M. in brackets behind KD, -/- no binding detected. mFcγRI mFcγRIIb mFcγRIII mFcγRIV mIgG1 -/- 0.15 (0.05) 0.23 (0.03) -/- S1 0.30 S1 3.2 S1 -/- S2 0.83 S2 4.8 S2 -/- S3 0.17 S3 0.32 S3 0.25 S4 2.0 S4 -/- S4 mIgG2a 0.012 (0.002) 0.69 (0.16) 0.34 (0.04) 0.060 (0.020) 0.006 S1 2.4 S1 1.5 S1 0.035 S1 0.026 S2 1.8 S2 0.071 S2 0.018 S3 0.14 S3 0.010 S3 0.033 S5, a 0.022 S6, b 0.0013 S6, c mIgG2b 0.83 (0.14) 0.45 (0.06) 0.12 (0.03) -/- S7 0.45 S1 1.6 S1 0.059 S1 0.91 S2 1.6 S2 0.063 S2 0.26 S4 0.91 S4 0.034 S4 10 S5, a -/- S6, b 0.021 S6, c mIgG3 0.011 S6, c a, As provided in the review of Bruhns and Jönsson S5, original source unknown. b, Affinity for Fc RI.1 (a) allele, as described by Gavin et al. S6. c, Affinity for Fc RI.4 (d) allele, as described by Gavin et al. S6. References: S1. Nimmerjahn F, Bruhns P, Horiuchi K, Ravetch J V. FcyRIV: A novel FcR with distinct IgG subclass specificity. Immunity 2005; 23:41–51. S2. Baudino L, Nimmerjahn F, Shinohara Y, Furukawa J-I, Petry F, Verbeek JS, Nishimura S-I, Ravetch J V, Izui S. Impact of a three amino acid deletion in the CH2 domain of murine IgG1 on Fc-associated effector functions. J Immunol 2008; 181:4107–12. S3. White AL, Chan HTC, Roghanian A, French RR, Mockridge CI, Tutt AL, Dixon S V, Ajona D, Verbeek JS, Al-Shamkhani A, et al. Interaction with FcγRIIB is critical for the agonistic activity of anti-CD40 monoclonal antibody. J Immunol 2011; 187:1754–63. S4. Kaneko Y, Nimmerjahn F, Ravetch J V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313:670–3. S5. Bruhns P, Jönsson F. Mouse and human FcR effector functions. Immunol Rev 2015; 268:25–51. S6. Gavin AL, Leiter EH, Hogarth PM. Mouse FcgammaRI: identification and functional characterization of five new alleles. Immunogenetics 2000; 51:206–11. S7. Nimmerjahn F, Ravetch J V. Divergent immunoglobulin g subclass activity through selective Fc receptor binding. Science 2005; 310:1510–2.