Fig. 2: A chimeric platform facilitates high-resolution structure determination of flaviviruses particles. | Nature Communications

Fig. 2: A chimeric platform facilitates high-resolution structure determination of flaviviruses particles.

From: A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses

Fig. 2

a, b Cryo-EM reconstructions of a WNVKUN and b the chimeric viruses bWNVKUN, bMVEV and bDENV-2 coloured by local resolution in a rainbow gradient from high (red) to low (blue). c The asymmetric unit of WNVKUN is composed of three copies of E (green, pink and blue) and M (not visible). Ellipses, triangles and pentagons represent the 2-, 3- and 5-fold icosahedral axes, respectively. d Asymmetric unit displayed as a cartoon and coloured by domain. Each E protein is labelled according to its proximity to the icosahedral symmetry axes. e A cartoon representation of the WNVKUN structure coloured by domain according to the domain diagram below: E ectodomain 1 (DI, red) containing an N-linked glycan at Asn154 (cyan); E ectodomain 2 (DII, yellow) containing a fusion loop (FL, green); E ectodomain 3 (DIII, blue); E membrane domain (purple) consisting of a stem of three membrane-proximal helices (E-H1, E-H2 and E-H3) and two transmembrane helices (E-T1 and E-T2); M membrane domain (magenta) consisting of a stem helix (M-H1) and two transmembrane helices (M-T1 and M-T2).

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