Data from: Conformational dynamics of SARS-CoV-2 spike on a membrane reveals the allosteric effects of furin cleavage and the D614G mutation

By combining HDX-MS with the ability of eVLPs to display full-length
native-like SARS-CoV-2 spike protein, we have determined the energetic and
conformational effects of both the membrane environment and unique
sequence features that are considered incompatible with soluble protein
constructs. We find that eVLP-displayed spike can sample the
open-interface trimer conformation observed in soluble constructs of
spike, including sequences from engineered vaccine constructs and native
viral sequences inaccessible to studies on soluble constructs. Moreover,
the D614G mutation, which arose early in the pandemic, favors the
canonical ‘closed-interface’ prefusion conformation, potentially
mitigating premature S1 shedding in the presence of a cleaved furin site
and providing an evolutionary advantage to the virus. Remarkably, furin
cleavage at the S1/S2 boundary allosterically increases the flexibility of
the S2' site, which may facilitate increased TMPRSS2 processing,
enhancing viral infectivity. The use of eVLPs in HDX-MS studies provides a
powerful platform for studying viral and membrane proteins in near-native
environments.