Fig. 1: Interprotomer disulfide substitution stabilizes S2-only constructs in a covalently linked trimer.
From: Prefusion-stabilized SARS-CoV-2 S2-only antigen provides protection against SARS-CoV-2 challenge
a Side view of HexaPro (PDB ID: 6XKL). The S1 subunits are shown as a transparent molecular surface. The S2 subunit of each protomer is shown as a ribbon diagram. Each inset corresponds to a zoomed view of interprotomer disulfide designs. Side chains in each inset are shown as sticks with sulfur atoms in yellow. b Reducing (top) and non-reducing (bottom) SDS-PAGE analysis of each interprotomer disulfide variant. The molecular weight standards in kDa are indicated at the left. The position of monomer, dimer and trimer bands are indicated at the right. The SDS-PAGE analysis was performed once. c Size-exclusion chromatography and d, differential scanning fluorimetry analysis of each interprotomer disulfide variant. The vertical dotted line indicates (c) the peak retention volume and (d) the melting temperature for the HexaPro-S2 containing no disulfide substitution. Source data are provided as a Source Data file.
