Key mechanistic features of the trade-off between antibody escape and host cell binding in the SARS-CoV-2 Omicron variant spike proteins

ABSTRACT: Since SARS-CoV-2 Omicron variant emerged, it is constantly evolving into multiple sub-variants, including BF.7, BQ.1, BQ.1.1, XBB, XBB.1.5 and recently-emerging BA.2.86 and JN.1. Receptor binding and immune evasion are recognized as two major drivers for evolution of receptor binding domain (RBD) of the spike(S) protein. However, the underlying mechanism of interplay between two factors remains elusive. Herein, we determined the structures of human ACE2 complexed with BF.7, BQ.1, BQ.1.1, XBB and XBB.1.5 RBDs. From the ACE2/RBD structures of these sub-variants, in comparison with the known complex structures as well, we found that R493 but not Q493 was regulated by R346T substitution through long-range conformation alterations. Furthermore, we found that R493Q and F486V exert a balanced imp

SUBMITTER: Mr. Weiwei Li 

PROVIDER: S-SCDT-10_1038-S44318-024-00062-Z | biostudies-other |

REPOSITORIES: biostudies-other