Table 1.
Binding affinities and kinetics of mAbs for BoNT/B and BoNT/E and their mAb-specific LC-HN domains. The equilibrium binding constant (KD) was measured by flow fluorimetry in a KinExA.
| BoNT/B LC-HN mAb specific domain | BoNT/B Holotoxin | ||
|---|---|---|---|
| mAb | Domain | KD (pM) | KD (pM) |
| mAb B-a | B-LC-HN-a | 0.18 | 0.34 |
| mAb B-b | B-LC-HN-b | 60.81 | 56.88 |
| mAb B-c | B-LC-HN-c | 39.08 | 38.07 |
| BoNT/E LC-HN mAb specific domain | BoNT/E Holotoxin | ||
|---|---|---|---|
| mAb | Domain | KD (pM) | KD (pM) |
| mAb E-a | E-LC-HN-a | 22.09 | 11.52 |
| mAb E-b | E-LC-HN-b | 6.71 | 35.11 |
| mAb E-c | E-LC-HN-c | 115.6 | 730.30 |