TABLE 1.
IgG3m15 and IgG3m17 anti-FHbp MAbs show binding affinity similar to that of IgG3 and IgG1 anti-FHbp MAbs as measured by SPRa
| MAb | ka (1/Ms) | kd (1/s) | KD | χ2 |
|---|---|---|---|---|
| MAb502 IgG1 | 1.23 E+6 | 0.0063 | 5.12 E−9 | 1.97 |
| MAb502 IgG3 | 1.46 E+6 | 0.0065 | 4.57 E−9 | 3.98 |
| MAb502 IgGm15 | 1.05E+6 | 0.0061 | 5.75 E−9 | 3.06 |
| MAb502 IgG1m17 | 1.06 E+6 | 0.0065 | 6.10 E−9 | 3.77 |
| JAR3 IgG1 | 1.92 E+6 | 0.0007 | 0.36 E−9 | 5.60 |
| JAR3 IgG3 | 1.94 E+6 | 0.0016 | 0.84 E−9 | 0.15 |
| JAR3 IgG3m17 | 2.80 E+6 | 0.0021 | 0.76 E−9 | 2.56 |
a
The data shown are the mean values for 2 replicates performed in two independent experiments. KD, equilibrium dissociation constant; ka, association rate constant; kd, dissociation rate constant; χ2, quality of the fit of a 1:1 binding model to the data. The JAR3 IgG3m15 MAb construct was not expressed by the cell line, and the anti-PorA P1.16 MAbs were not tested because we lacked recombinant PorA that expressed the P1.16 epitope.