Table 2.
Overview of binding and affinity of top eight mAbs with RBD mutant antigens
| mAb | 1A10 | 1C1 | 1C11 | 2B11 | 2B2 | 2D6 | 3B8 | 3E6 | |
|---|---|---|---|---|---|---|---|---|---|
| ELISA antigen binding | Wuhan | + | + | + | + | + | + | + | + |
| N439K | + | + | + | + | + | + | + | + | |
| L452R | + | + | + | ± | + | + | + | + | |
| Y453F | + | + | + | + | + | + | + | + | |
| E484K | + | + | + | / | + | + | + | + | |
| E484Q | + | + | + | + | + | + | + | + | |
| N501Y | + | + | + | + | + | + | + | + | |
| L452R;E484Q | + | + | / | / | + | + | + | + | |
| K417N, E484K, N501Y | + | + | + | / | + | + | + | + | |
| 1A10 | 1C1 | 1C11 | 2B11 | 2B2 | 2D6 | 3B8 | 3E6 | ||
| Affinity KD(pM) | Wuhan | 199 ± 58 | 41 ± 12 | 87 ± 24 | 48 ± 21 | 31 ± 7 | 31 ± 6 | 234 ± 104 | 373 ± 295 |
| N439K | 379 ± 120 | 28 ± 14 | 107 ± 51 | 42 ± 13 | 16 ± 5 | 43 ± 51 | 144 ± 57 | 299 ± 295 | |
| L452R | 118 ± 19 | 9 ± 1 | 2940 ± 2020 | 3146 ± 737 | 145 ± 10 | 18 ± 1 | 56 ± 3 | 178 ± 75 | |
| Y453F | 170 ± 61 | 36 ± 18 | 142 ± 143 | 29 ± 12 | 23 ± 3 | 20 ± 6 | 136 ± 49 | 281 ± 173 | |
| E484K | 106 ± 33 | 23 ± 7 | 382 ± 116 | – | 450 ± 37 | 22 ± 7 | 119 ± 11 | 122 ± 86 | |
| E484Q | 101 ± 22 | 14 ± 3 | 167 ± 7 | 647 ± 347 | 174 ± 18 | 18 ± 2 | 105 ± 6 | 87 ± 49 | |
| N501Y | 151 ± 64 | 33 ± 19 | 118 ± 80 | 32 ± 17 | 19 ± 5 | 18 ± 5 | 159 ± 60 | 162 ± 159 |
Antigen binding was evaluated for RBD mutant antigens via ELISA and SPR. Affinity (KD; in pM) was determined via SPR, mean ± SD of minimum three replicates is given. + = maximal signal obtained at mAb concentration of 1 μg/mL or lower; ± = ± 50% of the maximal signal was obtained at 1 μg/mL; / = no signal was obtained at mAb concentration of 1 μg/mL; - = no binding at RBD antigen concentration of 80 nM. See also Table S2.