Fig. 2: Cryo-EM of bYFV17D and bYFVES504 complexed with 5A and 2C9 Fabs. | Nature Communications

Fig. 2: Cryo-EM of bYFV17D and bYFVES504 complexed with 5A and 2C9 Fabs.

From: A single residue in the yellow fever virus envelope protein modulates virion architecture and antigenicity

Fig. 2

a Representative micrographs of bYFV17D and bYFVES504 with and without complexing with 5A or 2C9 Fab. Viruses and Fabs were combined in a 1:1 ratio and incubated overnight at 4 °C prior to vitrification. b Cryo-EM density maps of bYFV17D and bYFVES504 complexed with either 5A Fab or 2C9 Fab with I3 symmetry applied. Maps are radially coloured according to the following: 0-150 Å red, 151-195 Å yellow, 196-210 Å green, 211-225 Å cyan, 226-240 Å blue Å, 241-255 Å orchid. c Cryo-EM density map and atomic model of bYFV17D complexed with 2C9 Fab. The density map was obtained via symmetry expanded ASU reconstruction and is shown in grey (E) and blue (variable region of 2C9 Fab), with the atomic model shown in red (E-DI), yellow (E-DII), blue (E-DIII) and grey (2C9 Fab). The N151 glycan is shown in green. d Top view of bYFV17D:2C9 E dimer atomic model. e Comparison of the bYFV17D:2C9 cryo-EM near-atomic resolution model and the YFV17D X-ray crystal structure (PDB:6IW4) in pink. Dotted lines are illustrating the E protein curvature differences between these two models.

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