Fig. 3: 5B11 recognizes a conserved epitope on the RSV pre-F.

a The interaction details between 5B11 and A2 DS-Cav1. In the upper panel, antibody 5B11 is shown as a cartoon and colored in white. The CDRH1, CDRH3, and FR2 involved in the interaction are colored in crimson and CDRL3 is colored in orange. The A2 pre-F antigen is shown as cartoon and surface representations and colored in turquoise. In the lower panel, hydrogen bond and salt bridge interactions are shown as yellow and green dashed lines, respectively. The residues involved in hydrogen bond and salt bridge interactions are shown as stick and labeled as indicated. All interactions shown are from the same perspective. b The interaction details between h5B11 and B18537 sc9-10 DS-Cav1. The B18537 pre-F antigen is colored in deep sky blue. c Structural comparison of the interactions of 5B11:A2 DS-Cav1 and h5B11:B18537 sc9-10 DS-Cav1. Changes in the binding angle of the h5B11 light chain caused by B18537 pre-F N169 are indicated by black dashed arrows. d The sequence conservation of 2074 full-length RSV F genes in the last decade downloaded from GenBank. The percent conservation of each amino acid within the binding region was calculated and represented as color-coded bars: Hydrophilic amino acid in purple, Neutral amino acid in orange, Hydrophobic amino acid in green. F sequences of RSV A2, A Long, B18537, B9320 with highlighted footprint of 5B11. Simultaneously shows the sequence conservation of nirsevimab and palivizumab antibody epitopes.