A structural analysis has revealed how the Omicron spike protein maintains binding to the ACE2 receptor. It also illuminated why an antibody that recently completed a phase 1 trial could effectively neutralize the variant, informing antibody drug discovery
In this paper, we report biochemical characterization of the Omicron spike trimer and its binding to ACE2. Our data reveal that the Omicron RBD is less stable and more dynamic than the WT RBD, and the Omicron spike trimer has 6-9 fold increased affinity for binding to ACE2. We further solved the structures of the Omicron spike trimer in the apo state, or bound to ACE2 or an anti-Omicron antibody.
In addition, our structures of antibody-bound Omicron spiker trimer uncover a distinct mode of antibody binding to the spike trimer, in which the unusual RBD-RBD configuration is preserved. The binding epitope of this broad-spectrum antibody is different from previous anti-SARS-CoV-2 antibodies, therefore opening a new venue for antibody drug discovery targeting various strains of SARS-CoV-2, including Omicron.The cryo-EM data were collected at the Shanghai Advanced Electron Microscope Center.
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