Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-016-0011-z
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Funding
- Universities of Helsinki, Leeds and York
- Academy of Finland [139178, 275199]
- Sigrid Juselius Foundation
- Helsinki Graduate Programme in Biotechnology and Molecular Biology
- Wellcome Trust [062164, 090932/Z/09/Z, 097827/Z/11/Z, 110145]
- Royal Society Leverhulme Trust Senior Research Fellowship [LT130088]
- Leverhulme Trust Research Fellowship [ECF2013-019]
- Wellcome Trust [097827/Z/11/Z, 090932/Z/09/Z] Funding Source: Wellcome Trust
- EPSRC [EP/K028286/1] Funding Source: UKRI
- Royal Society [LT130088] Funding Source: Royal Society
- Academy of Finland (AKA) [139178, 139178] Funding Source: Academy of Finland (AKA)
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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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