Extended Data Fig. 6: Comparison of antibody epitopes of our current study and previously reported antibodies against the S protein harboring the N501Y mutation at RBD.
From: Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function
Left panel. RBD is shown in surface representation with the residues that are in contact with the light chain and heavy chain of RBD-chAb15 (Ab15) colored in lime and forest green, respectively. The residues that are in contact with the light chain and heavy chain of RBD-chAb45 (Ab45) colored in light yellow and gold, respectively. Middle panel. RBD is shown in surface representation with the residues that are in contact with the VH ab8 (PDB ID: 7MJI) colored in steel blue. Right panel. RBD is shown in surface representation with the residues that are in contact with the light chain and heavy chain of Fab ab1 (PDB ID: 7MJL) colored in light blue and steel blue, respectively. In all cases, N501Y is color in red to highlight how these antibodies bypass the mutation to retain their binding to RBD. The number of RBD-up or RBD-down conformation within the trimeric S protein structure is indicated within parentheses below. In our structure, two nAbs binding simultaneously to the same RBD while in the work by Subramanian and colleagues, the two antibodies bind separately the one RBD3.
