Extended Data Fig. 5: Comparison of the footprints of the 12B2 and the 1F5 antibody on prefusion F and postfusion F and among HNV F proteins. | Nature Structural & Molecular Biology

Extended Data Fig. 5: Comparison of the footprints of the 12B2 and the 1F5 antibody on prefusion F and postfusion F and among HNV F proteins.

From: Broadly neutralizing antibody cocktails targeting Nipah virus and Hendra virus fusion glycoproteins

Extended Data Fig. 5

a, b, Molecular surface representation of the NiV F prefusion trimer (a) and the homology model of NiV F postfusion (b) showing the 12B2 footprint in orange. c-d, Molecular surface representation of the HeV F prefusion trimer (c) and the homology model of NiV F postfusion (d) showing the 1F5 footprint in purple. The homology model of NiV F postfusion in (b) and (d) was obtained by threading the NiV F sequence onto the human parainfluenza postfusion F structure23 (PDB: 1ZTM). e, Sequence alignment of HNV F glycoproteins (NiV, HeV, GhV: Ghana bat virus; CedV: Cedar virus; MojVF: Mojiang virus). Residues on HNV F constituting the 12B2 or 1F5 epitope are denoted with an orange or purple asterisk, respectively.

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