Anti-EDIII of DENV2 [2C8]

Absolute Antibody

Anti-EDIII of DENV2 [2C8]

7

Binding avidity/affinity of both Full length (IgG) and Fab fragments of the antibody to whole virion measured by ELISA. The crystal structure of the Fab fragment in complex with EDIII of DENV2 NGC was determined. Focus reduction neutralization assays showed highly potent neutralization of DENV2 NGC and 16681 for the antibody (IgG2a) with 50% neutralization titers in the sub-nanomolar range (50% FRNT at 0.025 nM). Pre- and postattachment neutralization assays showed the antibody is capable of significantly inhibiting infection after the virus had bound to the cells. The antibody has strong capacity to promote antibody dependent enhancement (ADE). ADE was analysed using U937 cells, the antibody demonstrated typical infection enhancement with peak titers of over 1000-fold enhancement over background and a wide range of concentrations at which enhancement occurred. The humanized version of the antibody (human IgG1) showed enhancement for DENV2/16681 and DENV2/NGC. Surface plasmon resonance assay was performed to evaluate the binding specificity and affinity between the antibody and recombinant EDIII (Kd= 176.7 nM) (Renner et al., 2018; PMID: 30323338).

ELISA, Neutralisation/Blocking, Other Application

ELISA; SPR; Neutralizing; Crystallization

Research Use Only

This chimeric rabbit antibody was made using the variable domain sequences of the original Mouse IgG2a format for improved compatibility with existing reagents assays and techniques.

-20°C,2°C to 8°C

12352203