Table 2 Apparent affinity of the CH103 UCA mutant and lineage mAbs for transmitted founder (TF) and heterologous HIV-1 Env

From: Selection of immunoglobulin elbow region mutations impacts interdomain conformational flexibility in HIV-1 broadly neutralizing antibodies

mAb C.CH505TF
gp120 (Kd × 10−9 M)
C.CH505TF
SOSIP.664.v4.1 (Kd × 10−9 M)
B.63521 D11
gp120 (Kd × 10−9 M)
UCA 430 ± 20 1,500 ± 300 NB
UCA-P14S 370 ± 30 1,700 ± 400 NB
UCA-S30G 400 ± 10 1,800 ± 100 NB
UCA-S30G/S31G 440 ± 20 800 ± 100 NB
I4 53 ± 5 60 ± 20 14,000 ± 3,000
I3 9.53 ± 0.06 ND 4200 ± 100
CH106 9.3 ± 0.8 5 ± 1 14.2 ± 0.9
CH103 40 ± 10 16 ± 3 1.1 ± 1.0
  1. Apparent dissociation constants (Kd) for each mAb were calculated from SPR kinetic analyses for autologous C.CH505TF gp120 and heterologous B.63521 D11 gp120 and from BLI kinetic analysis for autologous C.CH505TF.SOSIP.664.v4.1 as described in Methods. Data are shown as the mean and standard deviation from a minimum of two replicate measurements
  2. NB no binding, ND not determined