Conformational dynamics of SARS-CoV-2 spike on a membrane reveals the allosteric effects of furin cleavage and the D614G mutation - PubMed
4 hours ago
- #conformational dynamics
- #spike protein
- #SARS-CoV-2
- Study combines hydrogen-deuterium exchange mass spectrometry (HDX-MS) with enveloped virus-like particles (eVLPs) to analyze SARS-CoV-2 spike protein dynamics.
- eVLP-displayed spike can sample open-interface trimer conformations, similar to soluble constructs, including vaccine and native viral sequences.
- D614G mutation favors the closed-interface prefusion conformation, potentially reducing premature S1 shedding and providing an evolutionary advantage.
- Furin cleavage at the S1/S2 boundary increases flexibility at the S2' site, possibly enhancing TMPRSS2 processing and viral infectivity.
- eVLPs in HDX-MS studies offer a powerful platform for studying viral and membrane proteins in near-native environments.
- Authors disclose potential conflicts of interest, including patents related to SARS-CoV-2 spike protein conformations and EABR technology.