Fig. 1: Biochemical characterization of the LayV-G protein and binding affinity with Henipavirus receptors ephrinB2 and ephrinB3.
From: The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus
a, b Comparison of gel-filtration profile of LayV-G, human ephrinB2, ephrinB3. After LayV-G co-incubation with human ephrinB2/B3; LayV-G (Red) cannot form a complex with human ephrinB2 (Blue) or ephrinB3 (green) in gel-filtration (Shown on the left panel). The reducing-SDS-PAGE of fractions collected from gel-filtration (Shown on the right panel). c Bio-layer Interferometry (BLI) data of binding affinity of ephrinB2 (left) & ephrinB3 (right) and purified LayV-G and NiV-G. LayV-G (Blue scatter from dark to light) and NiV-G (Orange scatter from dark to light) were used as analytes in solution, with concentrations ranging from 50 nM to 3.125 nM. d ELISA binding of serious diluted soluble recombinant ephrinB2 and ephrinB3 conjugated with HRP to various HNV-G ectodomain (LayV-G (red), MojV-G (green), HeV-G (purple) and NiVM-G (blue)), SARS-CoV-2-WT (grey) served as a negative control. One representative curve of three independent experiments performed in technical duplicate are shown. EphrinB2-HRP and ephrinB3-HRP were separately serial diluted starting with 1:100 and 1:50. Source data are provided as a Source Data file.
