Skip to main content
. 2017 Apr 26;292(24):10197–10219. doi: 10.1074/jbc.M117.788919

Table 2.

KD values for the binding of various OD fragments displayed on the yeast surface to VRC01 antibody, determined by FACS titrations

KD indicates equilibrium dissociation constant; S.D. is standard deviation for the data from two independent experiments.

Construct name KD ±S.D.
nm
ODYCO (fully glycosylated) >300–400
ΔG4-ODYCO (partially glycan-free) 27 ± 3
ΔG14-ODYCO (completely glycan-free) 10 ± 1
ΔG14-ODYCO-D368Ra (completely glycan-free negative control) >700
WT core gp120 (positive control) 24.3 ± 0.4

a D368R mutation is known to decrease the binding of gp120 with CD4-binding site antibodies such as VRC01.