Fig. 3: Neutralization mechanism of M678F and M688F. | Nature Communications

Fig. 3: Neutralization mechanism of M678F and M688F.

From: Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail

Fig. 3

a Thermal stability of FMDV-M678F, FMDV-M688F and synergistic function of FMDV-M678F-M688F complexes determined by thermofluor PaSTRy using SYTO9 dye to detect RNA release. Source data are provided as a Source Data file. b Acid stability analysis of FMDV-M678F, FMDV-M688F and FMDV-M678F-M688F complexes using TEM. It was repeated independently once with consistent results. c Structural interpretation of antibody stabilization of FMDV. Surface representation of two FMDV pentamers, M678F (light blue) and M688F (magenta) antibodies are displayed in middle of the panel. Two FMDV protomers joined at the 2-fold axis labeled zone 1 (white dotted lines), and a FMDV pentamer labeled zone 2 (orange dotted lines) are zoomed in on the left and right panel, respectively, as indicated by light blue arrows. Epitopes are circled with yellow lines. The axes of rotational symmetry are also marked. d Roadmap showing the relative positions of the VHHs (M678F and M688F) and receptors (αvβ6 and HS) footprints on the viral surface. The footprints of M678F, M688F and αvβ6 are outlined with the color bar shown below. e Superimpositions of FMDV-αvβ6 and FMDV-M678F/ M688F shown in FMDV 146S zone 1 structure from panel (d). The 146S pentamer, M678F, M688F, and receptor subunits αv and β6 are colored as shown by the color bar below. Clashes between M678F/ M688F and receptor subunits are prominent and marked with star symbols.

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