Chrysovirus structure: repeated helical core as evidence of gene duplication

Adv Virus Res. 2013:86:87-108. doi: 10.1016/B978-0-12-394315-6.00004-0.

Abstract

Chrysoviruses are double-stranded RNA viruses with a multipartite genome. Structure of two fungal chrysoviruses, Penicillium chrysogenum virus and Cryphonectria nitschkei chrysovirus 1, has been determined by three-dimensional cryo-electron microscopy analysis and in hydrodynamic studies. The capsids of both viruses are based on a T=1 lattice containing 60 subunits, remain structurally undisturbed throughout the viral cycle, and participate in genome metabolism. The capsid protein is formed by a repeated α-helical core, indicative of gene duplication. Whereas the chrysovirus capsid protein has two motifs with the same fold, most dsRNA virus capsid subunits consist of dimers of a single protein with similar folds. The arrangement of the chrysovirus α-helical core is conserved in the totivirus L-A capsid protein, suggesting a shared basic fold. The encapsidated genome is organized in concentric shells; whereas inner dsRNA shells are diffuse, the outermost layer is organized into a dodecahedral cage beneath the protein capsid. This genome ordering could constitute a framework for dsRNA transcription in the capsid interior and/or have a structural role for capsid stability.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Ascomycota / virology*
  • Capsid / ultrastructure
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics*
  • Cryoelectron Microscopy
  • Gene Duplication*
  • Imaging, Three-Dimensional
  • Protein Conformation
  • Protein Folding
  • RNA Viruses / genetics*
  • RNA Viruses / isolation & purification
  • RNA Viruses / ultrastructure*

Substances

  • Capsid Proteins