Visualization of protein-RNA interactions in cytoplasmic polyhedrosis virus

J Virol. 1999 Feb;73(2):1624-9. doi: 10.1128/JVI.73.2.1624-1629.1999.

Abstract

Unlike the multiple-shelled organization of other Reoviridae members, cytoplasmic polyhedrosis virus (CPV) has a single-shelled capsid. The three-dimensional structures of full and empty CPV by electron cryomicroscopy show identical outer shells but differ inside. The outer surface reveals a T=1 icosahedral shell decorated with spikes at its icosahedral vertices. The internal space of the empty CPV is unoccupied except for 12 mushroom-shaped densities attributed to the transcriptional enzyme complexes. The ordered double-stranded RNA inside the full capsid forms spherical shells spaced 25 A apart. The RNA-protein interactions suggest a mechanism for RNA transcription and release.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bombyx / virology
  • Cryoelectron Microscopy
  • RNA, Double-Stranded / metabolism*
  • RNA, Viral / metabolism*
  • Reoviridae / ultrastructure*
  • Viral Proteins / metabolism*
  • Virion / ultrastructure

Substances

  • RNA, Double-Stranded
  • RNA, Viral
  • Viral Proteins