Figure 6. Enhanced trimer stability and N-terminal domain (NTD) dynamics in Omicron BA.1 S.
(A) Relative fractional uptake (Dex = 10 min) for Omicron BA.1 S mapped onto a wild-type (WT) spike (S) structure with three down receptor-binding domains (RBDs) (PDB ID: 6VXX) coverage maps shown in Figure 6—figure supplement 1). Deuterium exchange heat map (gradient of white (0%) -red (70%) as mapped on WT S structure (PDB ID: 6VXX). (B) Differences in deuterium exchange (ΔRFU) (Dex = 10 min) for Omicron BA.1 S minus Delta S were mapped onto a WT S structure (PDB ID: 6VXX). Shades of blue correspond to negative differences in deuterium exchange and shades of red correspond to a positive difference in deuterium exchange. (C–E) Stacked mass spectra for peptides 92–103, 177–191, and 900–913 with undeuterated reference spectra, 1 min, and 10 min exchange (left to right). For each peptide, the top row contains spectra for Delta S and the bottom row contains spectra for Omicron BA.1 S. Absolute intensities are indicated at the top right of each spectrum. (F) Differences in deuterium exchange (deuterons) mapped at peptide resolution from N to C terminus for Omicron BA.1 S minus Delta S are shown in difference plots for 1-, 2-, 10-, and 30 min exchange. Select peptides showing significant differences in exchange are annotated. Significance was determined by hybrid significance testing (p<0.01, Figure 6—figure supplement 2). Differences are tabulated in Figure 6—source data 1 with corresponding peptide numbers* shown on the x-axis of the difference plot.