Fig. 2: Biochemical characterization of designed variants.
From: A general computational design strategy for stabilizing viral class I fusion proteins
a Size-exclusion chromatography (SEC) of monodispersed RSV F variants. R-1b expression levels were compared to the RSV vaccine DS-Cav1. b Binding of design R-1b to the prefusion-specific antibody D25 compared to DS-Cav1 and the postfusion RSV A2 F (post). c Differential scanning fluorimetry (DSF) of design R-1b and DS-Cav1. DS-Cav1 was used to compare the stability of R-1b as the parental sequence of the latter is not prefusion-stabilized. d SEC of hMPV F variants. The expression levels of designs M-104 and M-305 were compared to their parent construct, 115-BV, and the next-generation immunogens DS-CavEs and DS-CavEs228. e Binding of designed hMPV F variants to the prefusion-specific antibody MPE8 compared to 115-BV, DS-CavEs, DS-CavEs2, and the postfusion hMPV B2 F (post). f DSF of designed hMPV F variants, 115-BV, DS-CavEs, and DS-CavEs2. g SEC of SARS-CoV-2 S designs. Expression levels of designed proteins were compared to their parent construct, S-2P, and the next-generation immunogen HexaPro21. h Binding of designed SARS-CoV-2 S variants to ACE2 compared to S-2P and HexaPro. i DSF of designed SARS-CoV-2 S variants, S-2P, and HexaPro. Antibody binding assays show in grey the raw data, in colors the fitted curves, and in dotted lines the end of the association time. Binding constants are summarized in Supplementary Tables 2–4. Source data for all panels are provided as a Source Data file.
