HMAb measured by biolayer interferometry. Label free, real time binding analysis between the HMAbs 2.3D, 3.6D and 4.8A and purified, recombinant E protein from each DENV serotype to measure binding affinity was performed. The affinities of 2.3D and 3.6D for DENV 3 or 4 E proteins could not be measured due to Ab aggregation at the higher concentrations needed to detect lower affinity binding. A: Association rate constants (kon) for Ab:E protein interactions. B: Dissociation rate constants (koff) for Ab:E protein interactions. C: Equilibrium dissociation constants (Kd) for HMAb:E protein complexes.