Recombinant Human Anti-NV VP1 Antibody (5I2) (CAT#: PABC-244)

Figure 1 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 (A) or antigens representing wild-type or mutant recombinant capsid proteins of homologous virus (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. (C) The ligand specificity of mAb-mediated inhibition of NoV VLP binding to a panel of its glycan ligands (H1, H2, H3, tri-A or Le(y)) was evaluated in HBGA blocking assay for three mAbs, 2L8, 3I23 and 5I2.

Sapparapu, G., Czakó, R., Alvarado, G., Shanker, S., Prasad, B. V., Atmar, R. L., ... & Crowe Jr, J. E. (2016). Frequent use of the IgA isotype in human B cells encoding potent norovirus-specific monoclonal antibodies that block HBGA binding. PLoS pathogens, 12(6), e1005719.

Figure 2 Blocking assay

The ligand specificity of mAb-mediated inhibition of NoV VLP binding to a panel of its glycan ligands (H1, H2, H3, tri-A or Le(y)) was evaluated in HBGA blocking assay for mAb 5I2.

Sapparapu, G., Czakó, R., Alvarado, G., Shanker, S., Prasad, B. V., Atmar, R. L., ... & Crowe Jr, J. E. (2016). Frequent use of the IgA isotype in human B cells encoding potent norovirus-specific monoclonal antibodies that block HBGA binding. PLoS pathogens, 12(6), e1005719.