Fig. 6: Characterisation of bYFVES504 T380R.
a Cryo-EM reconstruction of bYFVES504 T380R with I3 symmetry applied and coloured according to its local resolution. b Cryo-EM reconstruction and atomic model of bYFVES504 T380R ASU. The density map was obtained by symmetry expanded ASU reconstruction using cisTEM2 and is shown in grey, with the atomic model shown in red (E-DI), yellow (E-DII) and blue (E-DIII). In (a) and (b) the pentagons, triangles, and ovals represent the icosahedral five-, three- and two-fold axes, respectively. c Atomic model of bYFVES504 T380R E monomer with R380 highlighted in dark pink and the fusion loop highlighted in orange. d Contacts between the five-fold (blue), three-fold (dark purple) and two-fold (light purple) axes E protein R380 residues and the adjacent E proteins. Bonds are depicted by blue dotted lines. e Comparison of the bYFVES504 T380R and bYFVES504/DIII17D (in grey) ASU atomic models, aligned at the five-fold axis E protein. Below is a comparison of the three-fold axis E protein. f Serum neutralising titres of human YFV17D vaccinees (n = 14) against the bYFV DIII chimeras. Neutralisation was determined using FRNTs on C6/36 (Aedes albopictus) cells. Significance was determined using two-tailed Wilcoxon matched-pairs signed rank test on GraphPad Prism 9.0. ***p ≤ 0.0002, **p ≤ 0.002, *p ≤ 0.03. p = 0.0001 (17D vs 17D/DIIIES504), p = 0.0004 (17D vs. 17D R380T), p = 0.009 (ES504 vs. ES504/DIII17D), p = 0.017 (ES504 vs. ES504 T380R). LOD = limit of detection. Source data is provided as a Source Data file. LOD limit of detection.
