Recombinant Humanized Anti-Norovirus Antibody (512) (CAT#: HPAB-2429LY)

Figure 1 Fab 512 binds tightly to NV P domain.

BLI analysis of Fab 512 binding to NV P domain. P domain-Fab 512 association-dissociation curves were obtained through serial twofold dilutions of Fab 512 (0.5-0.015 μM) plus buffer controls by using Octet acquisition software. Sensograms for all concentrations are shown and labeled accordingly. The calculated KD, Kon, and Koff are shown in a tabular form.

Shanker, S., Czakó, R., Sapparapu, G., Alvarado, G., Viskovska, M., Sankaran, B.,... & Prasad, B. V. (2016). Structural basis for norovirus neutralization by an HBGA blocking human IgA antibody. Proceedings of the National Academy of Sciences, 113(40), E5830-E5837.

Figure 2 Binding and blocking characteristics of purified monoclonal antibodies.

Purified IgG (red) or IgA (blue) antibodies were tested for binding to NV VLP in ELISA (FIG. A) or for blocking VLP-glycan interaction (FIG. B). Each of the IgG antibodies bound to VLPs with lower EC50 values than IgA antibodies, while in contrast the concentrations needed for blocking were similar for IgG and IgA. The blocking of murine mAb 8812 is shown in black.

Figure 3 Specificity of human mAbs.

The binding (mean absorbance at 450 nm + SD) of purified mAbs at 20 μg/mL to VLPs representing homologous virus (NoV GI.I) or heterologous human NoVs of different genotypes (FIG. A) or antigens representing wild-type or mutant recombinant capsid proteins of homologous virus (FIG. B) were assessed by ELISA to evaluate genotype specificity and to infer the subdomain of major capsid protein bound by anti norovirus mAbs. The data shown in each figure summarizes the results from 2 independent experiments.

Figure 4 The ligand specificity of mAb-mediated inhibition of NoV VLP binding to a panel of its glycan ligands (HI, H2, H3, tri-A or Le(y)) was evaluated in HBGA blocking assay for three mAbs, 2L8, 3123 and 512.

Figure 5 Representative curves for blocking assays with isotype switch variants for each of the antibody clones.

IgG or monomeric (mlgA) or dimeric (dig A) forms of IgA were used in the HBGA blocking assay. Results are shown with concentration of Ab as loglO nM combining sites).