Genomic RNA folding mediates assembly of human parechovirus

Research output: Scientific - peer-reviewArticle

Details

Original languageEnglish
Article number5
Pages (from-to)1-11
Number of pages11
JournalNATURE COMMUNICATIONS
Volume8
Issue number1
StatePublished - 1 Dec 2017
MoE publication typeA1 Journal article-refereed

Researchers

  • Shabih Shakeel
  • Eric C. Dykeman
  • Simon J. White
  • Ari Ora

  • Joseph J B Cockburn
  • Sarah J. Butcher
  • Peter G. Stockley
  • Reidun Twarock

Research units

  • University of York
  • University of Leeds
  • University of Helsinki
  • University of Helsinki Institute of Biotechnology

Abstract

Assembly of the major viral pathogens of the Picornaviridae family is poorly understood. Human parechovirus 1 is an example of such viruses that contains 60 short regions of ordered RNA density making identical contacts with the protein shell. We show here via a combination of RNA-based systematic evolution of ligands by exponential enrichment, bioinformatics analysis and reverse genetics that these RNA segments are bound to the coat proteins in a sequence-specific manner. Disruption of either the RNA coat protein recognition motif or its contact amino acid residues is deleterious for viral assembly. The data are consistent with RNA packaging signals playing essential roles in virion assembly. Their binding sites on the coat proteins are evolutionarily conserved across the Parechovirus genus, suggesting that they represent potential broad-spectrum anti-viral targets.

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