Cryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses

J Virol. 2012 Aug;86(15):8314-8. doi: 10.1128/JVI.00802-12. Epub 2012 May 16.

Abstract

Cryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical core, indicative of gene duplication. This unusual organization is common to chrysoviruses. The arrangement of many of these putative α-helices is conserved in the totivirus L-A capsid protein, suggesting a shared motif. Our results indicate that a 120-subunit T=1 capsid is a conserved architecture that optimizes dsRNA replication and organization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid Proteins / chemistry*
  • Capsid Proteins / metabolism
  • Protein Folding*
  • Protein Structure, Secondary
  • RNA Viruses / chemistry*
  • RNA Viruses / physiology
  • RNA, Double-Stranded / biosynthesis
  • RNA, Viral / biosynthesis
  • Sordariales / virology*
  • Virus Replication / physiology

Substances

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