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
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