Fig. 1: HuMab006-11 discovery and characterization.

a HuMAb006-11 binding specificity was assessed at 5 μg/mL against live virus, recombinant HBsAg-S, and recombinant PreS1/2 protein. b The neutralizing potential of HuMAb006-11 & HBIG was tested via an in vitro assay utilizing HBV (genotype D) and the HepG2-hNTCP cell line. c The binding potential of HuMAb006-11 to the four most common HBV genotypes was tested by ELISA, statistical analysis was performed using the t-test, *p < 0.05 (Sequence data, Supplementary data—Table 1). All data were expressed as mean ± SEM, N = 4 independent experiments. d Binding of HuMAb006-11 to HBsAg virus-like-particles interferes with/reduces detection by Bio-Plex mAbs specific for the loop-2 regions (antibodies 8 and 17). A reduction >0.5-fold in comparison to the control indicates that the epitope recognition is substantially reduced for the tested bio-plex mAbs due to the binding of HuMab006-11. The y-axis reports ± fold-change with respect to the HBsAg standard with 95% CI ± 0.5-fold relative to the HBsAg standard. e Predicted HBsAg structural data (I-Tasser) with highlighted loop-2 region indicating the broad binding region of HuMAb006-11. f Heavy and light chains of HuMAb006-11 for the four principle IgG subclasses were resolved on polyacrylamide gel under reducing and non-reducing conditions. g Affinity and B_max measurements of HuMAb006-11 subclasses by QCM using recombinant HBsAg as target (mean ± s.e.m., N = 3 independent experiments). The dissociation equilibrium constant (K_D) and B_max for each subclass are indicated at the top right-hand corner. Neutralization data comparing the four principle subclasses of HuMAb006-11 and HBIG based on h Secreted HBsAg, i secreted HBeAg. j intracellular HBcAg (representative flow data for quantification used to plot the HBcAg neutralization curve found in Supplementary Fig. 3c). All blots were derived from the same experiment and processed in parallel. All data were expressed as mean ± SEM, N = 3 independent experiments.