Structural basis for Fullerene geometry in a human endogenous retrovirus capsid.

摘要: The HML2 (HERV-K) group constitutes the most recently acquired family of human endogenous retroviruses, with many proviruses less than one million years old. Many maintain intact open reading frames and provirus expression together particle formation are observed in early stage embryo development associated pluripotency as well inflammatory disease, cancers HIV-1 infection. Here, we reconstruct core structural protein (CA) an retrovirus, assemble particles vitro employ single cryogenic electron microscopy (cryo-EM) to determine structures four classes CA Fullerene shell assemblies. These icosahedral capsular assemblies reveal at high-resolution molecular interactions that allow form both pentamers hexamers show how invariant structurally plastic associate unique polyhedral found retroviral cores. In capsid forms a surrounding viral core. Here authors combine cryo-electron NMR X-ray crystallography examine structure from retrovirus closed shells basis assembly.