Fig. 2: Cryo-EM structures of 5B11 bound RSV A2 and B18537 DS-Cav1s.

a, b Cryo-EM density maps of the A2 DS-Cav1:5B11 complex viewed from side view (a) and top view (b). The pre-F trimer is colored in dark gray (protomer 1), light gray (protomer 2), and turquoise (protomer 3), respectively. Each 5B11 fab is bound to one protomer, and the density of light and heavy chain of 5B11 are colored in crimson and sandy brown, respectively. The glycans density on pre-F are shown in pink. c Atomic model of A2 DS-Cav1:5B11 is presented as a surface representation, with one protomer and the 5B11 Fab shown in cartoon representation. The decorated glycans on A2 DS-Cav1 are depicted as pink sticks and surface. d, e Cryo-EM density maps of B18537 sc9-10 DS-Cav1: h5B11complex viewed from side view (d). The atomic model of B18537 sc9-10 DS-Cav1: h5B11 is also presented as cartoon and surface representation. To distinguish from A2 pre-F, protomer 3’ is colored deep sky blue. f The epitope comparison of 5B11 with seven other previously published antibodies: nirsevimab (site Ø, purple line), palivizumab (site II, green line), MPE8 (site III, pink line), RB1 (site IV, brown line), CR9501 (site V, cyan line), hRSV90 (site VIII, yellow line) and AM14 (blue line) on A2 pre-F trimer. The 5B11 epitope is highlighted in red and depicted with black solid lines. g, h Surface mapping of the 5B11 epitope on A2 DS-Cav1 (turquoise) and B18537 sc9-10 DS-Cav1 (deep sky blue), with the same color as in (c) and (e). Residues common to the light and heavy chain of 5B11 are colored orange red.