Fig. 4: 1E5 binds to the G head domain in a way that mimics the receptor.
Top (a) and side (b) views of the crystal structure of the NiVBD GHD/1E5 Fab complex. Molecules are shown as ribbon diagrams beneath a transparent surface. The GHD is colored cornflower blue, and the VH and VL of 1E5 are shown in gold and tan, respectively. c Top view of the interface between NiV G and 1E5. The NiV GHD is represented as a molecular surface, and the epitopes of 1E5 are highlighted. The paratopes of 1E5 are shown as ribbons. d Residues and H-bonds at the interface of the NiV G/1E5 complex. Contact residues are shown as stick representations, and H-bonds are shown as dotted black lines. CDRH1-3 is colored gold, CDRL2-3 and FR-L3 are colored tan, the oxygen atoms are colored red, and the nitrogen atoms are colored bright blue. e Interaction of 1E5 CDRH3 with the NiV G central cavity. NiV G is shown as a transparent surface representation, and the other elements are shown as described above. f–h Superimposition of the GHD/1E5 complex with the GHD/EB2 (PDB ID: 2VSM) and GHD/m102.3 (PDB ID: 6CMI) structures. Molecules are shown as surface representations. The GHD, 1E5, EB2, and m102.3 are colored cornflower blue, gold, pale violet red, and dark sea green, respectively. The epitopes of m102.3, EB2, and 1E5 are superimposed in their parent colors on the GHD surface. i, j Relative binding activity of antibodies or EB2 to the mutants and wild-type HeV G. Residues possibly critical for 1E5 binding were mutated to alanine, and the ratio of the area under the curve tested by ELISA was calculated. k Relative binding activity of the 1E5 CDRH3 alanine mutants to HNV G. The ratio of the EC50 of the 1E5 mutants to that of the wild-type was calculated. Source data are provided as a Source Data file.
