Omicron sars-cov-2 mutations stabilize spike up-rbd conformation and lead to a non-rbm-binding monoclonal antibody escape

HIGHLIGHTS

SUMMARY

The Omicron spike preferentially adopts the one-RBD-up conformation both before and after ACE2 binding, which is in sharp contrast to the orchestrated conformational changes to create more up-RBDs upon ACE2 binding as observed in the prototype and other four variants of concern (VOCs). The interface is maintained by a hydrophobic microenvironment, where residue F486 of the C_RBD is closely surrounded by hydrophobic residues of the A_RBD and forms extensive hydrophobic contacts (Fig 1d), consistent with previous observations15,27. Residue F486 of the C_RBD stacks with F375 of the A_RBD, bridging the . . .

 



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