Fig. 4: Evaluation of SARS-CoV-2 2P DS S thermal stability and protease resistance. | Nature Structural & Molecular Biology

Fig. 4: Evaluation of SARS-CoV-2 2P DS S thermal stability and protease resistance.

From: Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation

Fig. 4: Evaluation of SARS-CoV-2 2P DS S thermal stability and protease resistance.

a,b, Electron microscopy analysis of negatively stained SARS-CoV-2 2P S (a) and SARS-CoV-2 2P DS S (b) incubated for 20 min at 25, 55 and 85 °C. Black arrows highlight particles that appear to be misfolded. Red arrows highlight particles that appear to be in the postfusion conformation. c–e, Binding of human neutralizing antibody S309 to immobilized SARS-CoV-2 2P DS S (green) or SARS-CoV-2 2P S (black) preincubated for 20 min at 25, 55 and 85 °C (c), or for 16 h at 4 °C with 1, 10 or 100 µg ml−1 trypsin (d) or chymotrypsin (e). Graphs show the area under the curve of binding of serially diluted concentrations of the human neutralizing antibody S309; data are shown as mean and s.d. of n = 2 technical replicates, and are representative of one (d and e) or two (c) independent experiments. Data behind graphs are available in Supplementary Data 1.

Back to article page