Table 2.

IgG binding and neutralization characteristics

VirusSpecificityAntibodyK50 for oligomeric gp120 (nM)aNeutralization (ID50) (nM)bRatio (K50/ID50)c
MNCD4bsIgG1 b120.100.01010
F9165 681.0
V3 loopLoop 24.11.62.5
19b3.02.51.2
447-52D0.600.05012
CD4i48d8.01.65.0
Other2G12150 >200<0.80
Hx10d CD4bs15e20 4.84.2
21h20 6.03.3
F918.02.43.3
IgG1 b120.800.07011
C4G3-299>50e 4.1>12
G3-519>50 98>0.50
G3-536>50 270>0.18
G3-508>50 190>0.27
V3110.50.0500.200.25
92840.120.930.13
BAT1230.0800.130.62
110.I0.501.30.38
8/38c67 671.0
V2G3-136>20 7.7>2.6
G3-4>70 44.4>1.6
BAT085>70 133.4>0.52
CD4i48d5.01.33.8
Other2G122.51.31.9
  • a Half-maximal binding of MAbs to oligomeric gp120 was determined as described in Table 1, footnoteb.

  • b Half-maximal neutralization was determined as described in Table 1, footnote c.

  • c The ratio of the concentration yielding 50% MAb binding to 50% neutralizing concentration was determined for each MAb.

  • d Most of this data set is taken from a previous study (42). Data for MAbs F91, IgG1 b12, and 2G12 were obtained in the present study.

  • e Saturation staining was not achieved under the experimental conditions used.