Fig. 4 | Nature Communications

Fig. 4

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

Fig. 4

Affinity and thermal stability trade-off in the CH103 bnAb lineage. a Apparent affinity (Kd, circles) and kinetic association (ka, triangles) and dissociation rates (kd, diamonds) of CH103 lineage mAbs binding to HIV-1 Env B.63521 gp120 (heterologous Env) show changes in kinetic rates during affinity maturation. CH106 and CH103 mAbs bound to Env with high affinity (Kd < 20 nM) and demonstrated breadth in neutralization24. b The initial improvement in the association rate (ka, y2-axis, closed triangles) for binding to heterologous Env (B.63521) occurs at the I8–I4 transition and coincides with the observed reduction in antibody thermal stability (Tm, y1-axis, open circles). Data are plotted as the mean and standard deviation from a minimum of two replicate measurements. Certain error bars are smaller than the data markers at this scale. Boxes depict the neutralization breadth and the geometric mean potency (IC50, μg/mL) calculated from previously published data24. A value of 50 was used for those with IC50 > 50. An “A” for the neutralization breadth indicates the antibody neutralizes autologous virus only

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