Fig. 2: Antigenic characterization of the ShAb molecules.
From: Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity
a ShAb RBD-competition assay assessed by Bio-Layer Interferometry (BLI). BLI measurements are performed with immobilized SARS-CoV-2 RBD and ShAb in solution. ShAb01 (top) or ShAb02 (bottom) are bound to the RBD molecule followed by incubation with other ShAbs. b Epitope binning of the ShAb molecules. Values represent the % residual binding of the indicated second molecule (ShAb01, ShAb02, ACE2, or CR3022) after saturation of the antigen (WA-1 RBD) with the indicated first antibody (left column). Shading from dark to light indicates competition strength ranging from strong competition (0–33%), to reduced competition (> 50%). Competition groups are indicated by black boxes. Human ACE2-Fc and CR3022 were used as controls. c RBD kinetic binding constants, and neutralization IC50 titers of SARS-CoV-2 viral VoC and SARS-CoV-1 pseudoviruses by ShAb01 and ShAb02. n/d indicates no binding was detected. d ShAb01 and ShAb02 binding assays performed by BLI with immobilized ShAbs and SARS-CoV-1 RBD and SARS-CoV-2 RBD, or clade 1b bat sarbecovirus trimeric S molecules in solution. Source data are provided as a Source Data file.
