Extended Data Fig. 2: Broad binding affinity of 76E1.
From: Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2

a, Schematic of mutations landscape in SARS-CoV-2 VOCs, variants of concern. del, deletion; ins, insertion. b, Binding kinetics of 76E1 to multiple soluble S-ECD proteins of SARS-CoV-2 variants as measured by BLI. 76E1 was loaded on Octet AHC sensor and tested for real-time association and dissociation of the serial diluted S-ECD proteins from SARS-CoV-2 variants as determined by BLI. 76E1 retained higher affinity to all the variants tested. c, Binding kinetics of 76E1 to multiple soluble S-ECD proteins of α- and β-coronaviruses as measured by BLI. Serial diluted S proteins were immersed into the immortalized 76E1 on AHC sensors, the association and disassociation kinetics were recorded and shown. d, Binding curves of 76E1 to a panel of S-ECD proteins representative of α- and β-coronaviruses as measured by ELISA. e, 76E1 recognize a continuous epitope within spike protein. ELISA-based binding curves of 76E1 to SARS-CoV-2 S-ECD protein that was 100 °C-denatured in the presence of DTT and SDS versus untreated S-ECD. A SARS-CoV-2 RBD antibody 76F6 was used as a control. Data are shown as the mean values of duplicates (d,e). Representative data from two independent experiments were shown.