Genomic RNA folding mediates assembly of human parechovirus

Reidun Twarock, Eric Charles Dykeman, Shabih Shakeel, Simon White, Ari Ora, Joseph Cockburn, Sarah Butcher, Peter Stockley

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Article number5
Number of pages11
JournalNature Communications
Publication statusPublished - 23 Feb 2017

Bibliographical note

© 2017, The Authors.


  • Amino Acid Motifs
  • Base Pairing
  • Binding Sites
  • Capsid Proteins/genetics
  • Computational Biology
  • Conserved Sequence
  • Gene Expression
  • Genome, Viral
  • Humans
  • Models, Molecular
  • Parechovirus/genetics
  • Protein Binding
  • RNA Folding
  • RNA, Viral/genetics
  • Reverse Genetics
  • SELEX Aptamer Technique
  • Virion/genetics
  • Virus Assembly

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