Fig. 6: The extended outer loop β1S2-β1S3 of G inserts into the two pockets on the apical region of F to trigger fusion.
a Validation of the preliminary screened reactive peptides. Data are presented as mean ± s.d. of five replicates from one test. In Dunnett’s multiple comparisons test, the MD, CI, and P values between P59 and control were 58.17, 43.25 to 73.10, and P < 0.0001, respectively. b Interaction affinity between P-59 and sF determined by microscale thermophoresis. The experiments were performed twice, and similar results were obtained. Data are presented as mean ±s.d. of three replicates from one representative experiment. c Fusion rate and relative EB2 binding of P-59 related single-site mutants (see also Supplementary Fig. 9h, i). Data are presented as the means of three replicates from one representative experiment. d Fusion rate and EB2 relative binding of wild type or K246G/A mutants of NiV or HeV G. Data are presented as mean ±s.d. of three replicates from one representative experiment. e Side view of the top 1 pose of docked GHD-sF structures. Molecules are shown as surface representations. GHD is colored sky blue, and the chains A/B/C of sF are colored plum, light gray, and misty rose, respectively. f The zoomed view of the interface between GHD and sF. P-59 is shown as a ribbon diagram colored slate blue. The epitope of P-59 is highlighted and colored hot pink. Contact residues are shown as stick representations in parent colors, and H-bonds are shown as dotted black lines. g Contact residues at the interface of 5B3 and sF. The HCDR and LCDR of 5B3 are shown in dark and light green, respectively. Epitopes specific to 5B3 are shown in brown, and the residues shared by 5B3 and P-59 are shown in hot pink. h Fusion rate of the T5F mutant cotransfected with full-length of G. Data are presented as mean ±s.d. of five replicates from one representative experiment. i Relative binding of the mutants and wild-type of NiV T5F to two noncompetitive F-specific antibodies (see also Supplementary Fig. 9l). Data are the means of three replicates from one representative experiment. j Conservation of critical residues for G-F interactions among henipaviruses. k A new model for virus invasion and antibody neutralization. Source data are provided as a Source Data file.
