Fig. 3: The EEEV spike protein engages multiple LA repeats.
From: Structural basis for VLDLR recognition by eastern equine encephalitis virus
a Top view of the cryo-EM structure of the EEEV spike protein in complex with VLDLR LA1. E2 residues that contact VLDLR as determined by Adams et al.18 are labeled and highlighted in yellow. b Top (left panel) and side (right panel) views of the cryo-EM structure of the EEEV spike protein (unliganded) determined in this study, fitted with VLDLR LA repeats bound to the EEEV spike as determined by Adams et al. (PDB: 8UFB)18. In (a, b), the spike protein is shown in surface representation and LA repeats are shown as ribbon diagrams. Ca2+ ions are shown as green spheres. c Schematic depiction of VLDLR and ApoER2 isoform 2 (ApoER2 iso2). LA repeats are numbered from the N terminus. d, e K562 cells expressing human VLDLR and ApoER2 iso2 were infected with wild-type or mutant GFP-expressing RVPs for EEEV FL91-469 or EEEV PE6. Infection was monitored by flow cytometry. f Embryonic day 17 murine cortical neurons were infected with GFP-expressing wild-type or mutant EEEV FL91-469 RVPs. Infection was quantified using a live cell imaging system (see “Methods” for additional information). Representative GFP images and merged images of GFP and bright field are shown. Scale bars are 100 μm. g Quantification of neuronal infection in (f). Data are mean ± s.d. from three experiments performed in triplicates (n = 3 independent experiments) (d, e) or two experiments performed in triplicates (n = 2 independent experiments) (g). Two-way ANOVA with Dunnett’s multiple comparisons test, ****p < 0.0001 (d, e). Source data are provided as a Source Data file.
