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TitleAssembly of infectious enteroviruses depends on multiple, conserved genomic RNA-coat protein contacts.
Journal, issue, pagesPLoS Pathog, Vol. 16, Issue 12, Page e1009146, Year 2020
Publish dateDec 28, 2020
AuthorsRebecca Chandler-Bostock / Carlos P Mata / Richard J Bingham / Eric C Dykeman / Bo Meng / Tobias J Tuthill / David J Rowlands / Neil A Ranson / Reidun Twarock / Peter G Stockley /
PubMed AbstractPicornaviruses are important viral pathogens, but despite extensive study, the assembly process of their infectious virions is still incompletely understood, preventing the development of anti-viral ...Picornaviruses are important viral pathogens, but despite extensive study, the assembly process of their infectious virions is still incompletely understood, preventing the development of anti-viral strategies targeting this essential part of the life cycle. We report the identification, via RNA SELEX and bioinformatics, of multiple RNA sites across the genome of a typical enterovirus, enterovirus-E (EV-E), that each have affinity for the cognate viral capsid protein (CP) capsomer. Many of these sites are evolutionarily conserved across known EV-E variants, suggesting they play essential functional roles. Cryo-electron microscopy was used to reconstruct the EV-E particle at ~2.2 Å resolution, revealing extensive density for the genomic RNA. Relaxing the imposed symmetry within the reconstructed particles reveals multiple RNA-CP contacts, a first for any picornavirus. Conservative mutagenesis of the individual RNA-contacting amino acid side chains in EV-E, many of which are conserved across the enterovirus family including poliovirus, is lethal but does not interfere with replication or translation. Anti-EV-E and anti-poliovirus aptamers share sequence similarities with sites distributed across the poliovirus genome. These data are consistent with the hypothesis that these RNA-CP contacts are RNA Packaging Signals (PSs) that play vital roles in assembly and suggest that the RNA PSs are evolutionarily conserved between pathogens within the family, augmenting the current protein-only assembly paradigm for this family of viruses.
External linksPLoS Pathog / PubMed:33370422 / PubMed Central
MethodsEM (single particle)
Resolution2.23 - 2.6 Å
Structure data

10504

6thd

EMDB-10504, PDB-6thd:
Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E
Method: EM (single particle) / Resolution: 2.23 Å

EMDB-10505:
Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+genome focused classification
Method: EM (single particle) / Resolution: 2.6 Å

10506

6thn

EMDB-10506, PDB-6thn:
Multiple Genomic RNA-Coat Protein Contacts Play Vital Roles in the Assembly of Infectious Enterovirus-E symmetry expansion+2fold focused classification
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-MYR:
MYRISTIC ACID / Myristic acid

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-HOH:
WATER / Water

Source
  • bovine enterovirus (strain vg-5-27)
  • Bovine enterovirus type 1
  • bovine enterovirus strain vg-5-27
KeywordsVIRUS / BEV1 / enterovirus / picornavirus / RNA

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