KA (×105 M−1) of hFcγR ectodomains for monoclonal human IgG1
| . | Anti-CD20 . | KA fold induction . | Anti-RhD . | KA fold induction . | ||
|---|---|---|---|---|---|---|
| CHO . | YB2/0 . | CHO . | YB2/0 . | |||
| FcγRIIAH131 | 14 ± 5 | 11 ± 1 | 0.8 | 27 ± 1 | 23 ± 1 | 0.8 |
| FcγRIIAR131 | 7.3 ± 2.1 | 6.6 ± 0.6 | 0.9 | 19 ± 1 | 22 ± 2 | 1.2 |
| FcγRIIB/C | 2.8 ± 0.5 | 1.8 ± 0.1 | 0.7 | 3.2 ± 0.4 | 2.4 ± 0.7 | 0.8 |
| FcγRIIIAF158 | 11 ± 1 | 28 ± 3 | 2.5 | 27 ± 2 | 60 ± 7 | 2.2 |
| FcγRIIIAV158 | 23 ± 2 | 55 ± 7 | 2.4 | 51 ± 7 | 117 ± 14 | 2.3 |
| FcγRIIIBNA1 | 5.5 ± 1.1 | 8.7 ± 0.5 | 1.6 | 9.2 ± 0.8 | 23 ± 2 | 2.4 |
| FcγRIIIBNA2 | 6.8 ± 0.9 | 12 ± 1 | 1.7 | 10 ± 1 | 28 ± 2 | 2.7 |
| FcγRIIIBSH | 12 ± 3 | 12 ± 1 | 1.0 | 11 ± 1 | 27 ± 3 | 2.4 |
| . | Anti-CD20 . | KA fold induction . | Anti-RhD . | KA fold induction . | ||
|---|---|---|---|---|---|---|
| CHO . | YB2/0 . | CHO . | YB2/0 . | |||
| FcγRIIAH131 | 14 ± 5 | 11 ± 1 | 0.8 | 27 ± 1 | 23 ± 1 | 0.8 |
| FcγRIIAR131 | 7.3 ± 2.1 | 6.6 ± 0.6 | 0.9 | 19 ± 1 | 22 ± 2 | 1.2 |
| FcγRIIB/C | 2.8 ± 0.5 | 1.8 ± 0.1 | 0.7 | 3.2 ± 0.4 | 2.4 ± 0.7 | 0.8 |
| FcγRIIIAF158 | 11 ± 1 | 28 ± 3 | 2.5 | 27 ± 2 | 60 ± 7 | 2.2 |
| FcγRIIIAV158 | 23 ± 2 | 55 ± 7 | 2.4 | 51 ± 7 | 117 ± 14 | 2.3 |
| FcγRIIIBNA1 | 5.5 ± 1.1 | 8.7 ± 0.5 | 1.6 | 9.2 ± 0.8 | 23 ± 2 | 2.4 |
| FcγRIIIBNA2 | 6.8 ± 0.9 | 12 ± 1 | 1.7 | 10 ± 1 | 28 ± 2 | 2.7 |
| FcγRIIIBSH | 12 ± 3 | 12 ± 1 | 1.0 | 11 ± 1 | 27 ± 3 | 2.4 |
Affinity constants were determined from SPR analysis on immobilized FcγR ectodomains using the following concentrations of IgG: 0.866, 0.433, 0.216, 0.108, 0.054, and 0.026 μM. The standard deviation of the KA determination is indicated. KA fold induction = KA(YB2/0 mAb − FcγR)/KA(CHO mAb − FcγR). Values in bold indicate a KA fold induction ≥ 2.