Fig. 2: Comparison of the CV30 epitope against ACE2 and other neutralizing antibodies.
From: Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

a Structural overlay of ACE2/RBD complex with CV30/RBD complex. ACE2 is shown in sand color and RBD is in pink. The heavy chain of CV30 is shown in dark blue and the light chain is in light blue. b mAb binding to cell surface expressed SARS-CoV-2 S shows that CV30 induces shedding of the S protein. CR3022 is an RBD-binding antibody that does not induce shedding. Data points represent the mean of duplicates. Each experiment was repeated two times independently with similar results. Source data are provided as a Source Data file. c Structural alignment of the variable domains of CV30 (heavy chain is dark blue and light chain is light blue), B38 (heavy chain is dark orange and light chain is light orange), and CB6 (heavy chain is dark green and light chain is light green). d Sequence alignment of SARS-CoV-1 RBD and SARS-CoV-2 RBD. The residues that interact with ACE2 are indicated by the black circles. Residues that interact with CV30, B38, and CB6 are indicated by the colored squares (light chain interactions), circles (heavy chain interactions), or triangles (interactions with both chains). e Surface representation of the RBD with the binding epitope colored. Light chain interactions are the lightest color, heavy chain interactions are next lightest, and CDRH3 specific interactions are darkest, and interacting with both heavy and light chain is purple.