Fab and MAb binding to DENV-1 RVPs.

<p>(<b>A</b>) E106 MAb binding to DENV-1 RVPs by bio-layer interferometry. E106 MAb binds with high apparent affinity to DENV-1 RVPs (K_Dapp of 13±2 nM) with a slow dissociation (t_1/2>400 sec). Raw data is in red and fits are in gray. (<b>B</b>) Direct binding of E106 Fab to DENV-1 RVPs. Results are representative of several independent experiments that showed low affinity binding (K_D of >1 µM) and fast off-rate kinetics (t_1/2<2 sec). Raw data is in salmon and fits are in gray. BLI determined binding of the control E103 (<b>C</b>) MAb and (<b>D</b>) Fab to DENV-1 RVPs. E103 MAb and Fab binding to DENV-1 RVPs are comparable, with a calculated apparent K_Dapp of 0.8±0.1 nM and K_D of 7±1 nM, respectively, as expected for a predominantly monovalent interaction. Raw data is in blue (E103 MAb) and purple (E103 Fab) and fits are in gray. Results are representative of at least two independent experiments.