Exploring the Intrinsic Structural Plasticity and Conformational Dynamics of Human Beta Coronavirus Spike Glycoproteins.

ABSTRACT: The spike (S) glycoprotein of human beta coronaviruses (HCoVs) is central to viral entry, receptor engagement, and immune evasion. Here, we present an in-depth computational analysis of spike conformational dynamics across HCoVs, with a focus on SARS-CoV-2 and its variants. Leveraging a large cryo-EM structural ensemble and integrative modeling approaches, we dissect the intrinsic plasticity and variant-specific motions of the spike protein. Our results show that, despite substantial sequence divergence, HCoV spikes retain the ability to sample open and closed receptor-binding domain (RBD) states. For SARS-CoV-2, a hinge-like RBD opening motion dominates the conformational landscape, modulating ACE2 accessibility. Ensemble and single-structure normal modes revealed conserved dynamic domain

SUBMITTER: Ferreira E Silva Y 

PROVIDER: S-EPMC12308813 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature