Fig. 1: Cellular receptors of alphaviruses bind to different sites on a E1/E2 spike.
From: LDL receptor in alphavirus entry: structural analysis and implications for antiviral therapy
a Left panel: Schematic presentation of domain organization of E1/E2 dimer is from Wang et al., 20225. Right panel: structure of a GETV E1/E2 trimer (spike) integrated into a virtual lipid bilayer. A surface representation is shown; the capsid protein is colored in wheat, E1 in green, and E2 in cyan. One E1 and one E2 molecule, which form a heterodimer, are colored in light blue and light green, respectively. The figure was created with PyMol software using the cryo-EM structure of a GETV virion (PDB: 7FD2) and integrated into the plasma membrane using https://opm.phar.umich.edu/ppm_server3. b–g Upper parts of panels depict a surface model of one icosahedral asymmetric unit in free form (b) or bound to its receptor (c-g), which are represented using gray spheres and labeled. Amino acids in the fusion loop of E1 that interact with the receptor are shown as red spheres (in this view of the WEEV:MXRA8 complex, these residues are not visible). Lower parts of the panels display a top view of the icosahedral asymmetric unit, with amino acids of E1 and E2 interacting with the receptor shown as orange and magenta spheres, respectively. Panel (b) shows the structure of an icosahedral asymmetric unit of VEEV without a receptor, with individual monomers colored in varying shades of blue (E2) and green (E1). This figure was generated using PyMol software and data from following PDB files: 7N1I (VEEV), 6NK6 (CHIKV:MXRA8), 8DAN (WEEV:MXRA8), 7FFL (VEEV:LDLRAD3-D1), 8UFC (EEEV:VLDLR-LA1 + LA2), and 8IHP (SFV:VLDLR-LA3).
