The 3.0 Angstrom resolution crystal structure of Pariacoto virus (PaV) reve
als extensive interactions between portions of the viral RNA genome and the
icosahedral capsid. Under the protein shell of the T = 3 quasi equivalent
capsid lies a dodecahedral cage composed of RNA duplex that accounts for si
milar to 35% of the single-stranded RNA genome. The highly basic N-terminal
regions (residues 7-54) of the subunits, forming pentamers (A subunits) ar
e clearly visible in the density map and make numerous interactions with th
e RNA cage. The C-terminal segments (residues 394-401) of the A subunits li
e in channels near the quasi three-fold axes. Electron cryo-microscopy and
image reconstruction of PaV particles clearly show the dodecahedral RNA cag
e.