Supplementary Figure 5: Thermostability of engineered A22 recombinant empty capsids.
From: Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design
Purified capsids were left untreated or heated to 56ËšC for 2 h and sedimented on 15-45% sucrose density gradients. Fractions were taken from the bottom of the gradients and analysed by western blot. Capsid proteins were detected using an anti-FMDV A22 polyclonal antibody. Heated H93F capsids remained intact and migrated to fractions 3-4, as did untreated capsids, whereas wild-type capsids dissociated upon heating, remaining near the top of the gradient.
