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. 1998 Sep 21;188(6):1159–1171. doi: 10.1084/jem.188.6.1159

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Receptor-binding of the 89.6 and KB9 gp120 envelope glycoproteins. (A) The binding of the 89.6 and KB9 gp120 glycoproteins to human sCD4 absorbed onto the surface of an ELISA plate is shown. Values represent the mean and standard deviations from two independent experiments, each containing four replicate samples. (B) The ability of the 89.6 and KB9 gp120 glycoproteins to compete with MIP-1β binding to mouse cells expressing human CCR5 was assessed in the presence of 100 nM sCD4. The results shown are representative of two independent experiments, each performed with duplicate samples at each concentration of competitor. Relative inhibitory constants for MIP-1β (positive control), 89.6 gp120, and KB9 gp120 were 0.20 nM, 39.0 nM, and 4.4 nM, respectively. The YU2ΔV1/2/3 glycoprotein, which lacks the V3 loop and thus is unable to bind CCR5 (19), was included as a negative control.

Receptor-binding of the 89.6 and KB9 gp120 envelope glycoproteins. (A) The binding of the 89.6 and KB9 gp120 glycoproteins to human sCD4 absorbed onto the surface of an ELISA plate is shown. Values represent the mean and standard deviations from two independent experiments, each containing four replicate samples. (B) The ability of the 89.6 and KB9 gp120 glycoproteins to compete with MIP-1β binding to mouse cells expressing human CCR5 was assessed in the presence of 100 nM sCD4. The results shown are representative of two independent experiments, each performed with duplicate samples at each concentration of competitor. Relative inhibitory constants for MIP-1β (positive control), 89.6 gp120, and KB9 gp120 were 0.20 nM, 39.0 nM, and 4.4 nM, respectively. The YU2ΔV1/2/3 glycoprotein, which lacks the V3 loop and thus is unable to bind CCR5 (19), was included as a negative control.