Detergent modulates the conformational equilibrium of SARS-CoV-2 Spike during cryo-EM structural determination.

ABSTRACT: The Spike glycoprotein of SARS-CoV-2 mediates viral entry into the host cell via the interaction between its receptor binding domain (RBD) and human angiotensin-converting enzyme 2 (ACE2). Spike RBD has been reported to adopt two primary conformations, a closed conformation in which the binding site is shielded and unable to interact with ACE2, and an open conformation that is capable of binding ACE2. Many structural studies have probed the conformational space of the homotrimeric Spike from SARS-CoV-2. However, how sample buffer conditions used during structural determination influence the Spike conformation is currently unclear. Here, we systematically explored the impact of commonly used detergents on the conformational space of Spike. We show that in the presence of detergent, the Spik

SUBMITTER: Egri SB 

PROVIDER: S-EPMC10154187 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature