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" ... It seems, however, that the B6 antibody is capable of binding in SARS-CoV and SARS-CoV-2 to what the researchers label a cryptic epitope. Why, then, does the binding and neutralization fall off? To examine this, the researchers used cryo-electron microscopy to see exactly where the antibody was binding. In A and C clade viruses, the cryo visual of the region to which the antibody bound was clear (Figure 3). In SARS-CoV and SARS-CoV-2, however, the binding was disordered. This is surprising as this is usually a highly ordered area. They investigated the hidden binding by taking higher resolution pictures of the unusual binding between B6 and SARS-CoV-2. ... "
" ... The set of antibodies was also tested for its ability to bind to spike proteins, each of which carried a single mutation on the spike found in many variants of concern. The heat map of figure 5 summarizes the decrease in binding affinity of each antibody to each variant spike protein, the deeper the red coloration the greater the decrease in binding. Two of the tested antibodies, BG10-19 and BG1-28, are largely unaffected by any single mutation and bind to both SARS-1 and the WIV1 spike proteins. Sequence conservation at the BG10-19 epitope explains the cross-neutralization against SARS-1, as 23 of 29 residues are conserved between SARS-1 and SARS-CoV-2 RBDs. Notably, despite strong binding to the WIV1 spike protein, there is little neutralizing activity, despite a highly parallel amino acid sequence to SARS-1. Again, BG10-19 was selected for further study as it binds and neutralizes SARS-CoV-2 much with a much lower IC50 than does BG-1-28 (Figure 5). ... "