
The study revealed insights into the structural dynamics of the SARS-CoV-2 spike protein (S), responsible for viral entry into host cells. Cryo-electron microscopy (cryo-EM) imaging showed that the S protein can adopt different perfusion conformations, categorized as locked, closed, and open. However, locked conformations, featuring incompatible structural elements with the receptor-binding domain (RBD) in the "up" position, remain poorly understood for SARS-CoV-1. By introducing specific disulfide bonds into SARS-CoV-1 S, researchers were able to preserve rare locked conformations and visualize them using cryo-EM. This study also identified bound cofactors and structural features associated with locked conformations, comparing them to other SARS-related coronaviruses.
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