ArticleCommunications biology2024
Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Target-Based Antiviral Drug Development Against Human Respiratory Viruses.Pathogens (Basel, Switzerland) · 2026Review
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Different mechanisms for human rhinovirus survival in the presence of deleterious amino acid substitutions at virion protein-protein or RNA-protein interfaces.Journal of virology · 2026Article
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling.Virology journal · 2025Article
- New rhinovirus uncoating intermediate reveals how sodium versus potassium ions influence RNA release.Scientific reports · 2025Article
- Cryo-EM structure of the Seneca Valley virus A-particle and related structural states.Journal of virology · 2025Article
- New Advances in Small Molecules Targeted at Viral Capsid-Genome Binding.International journal of molecular sciences · 2025Review
- Clinical Significance of Rhinoviruses and Progress Toward Vaccination.Allergy, asthma & immunology research · 2025Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The cryo-EM structure of the human rhinovirus B14 determined in this study reveals 13-bp RNA duplexes symmetrically bound to regions around each of the 30 two-fold axes in the icosahedral viral capsid. The RNA duplexes (~12% of the ssRNA genome) define a quasi-dodecahedral cage that line a substantial part of the capsid interior surface. The RNA duplexes establish a complex network of non-covalent interactions with pockets in the capsid inner wall, including coulombic interactions with a cluster of basic amino acid residues that surround each RNA duplex. A direct comparison was made between the cryo-EM structure of RNA-filled virions and that of RNA-free (empty) capsids that resulted from genome release from a small fraction of viruses. The comparison reveals that some specific residues involved in capsid-duplex RNA interactions in the virion undergo remarkable conformational rearrangements upon RNA release from the capsid. RNA release is also associated with the asynchronous opening of channels at the 30 two-fold axes. The results provide further insights into the molecular mechanisms leading to assembly of rhinovirus particles and their genome uncoating during infection. They may also contribute to development of novel antiviral strategies aimed at interfering with viral capsid-genome interactions during the infectious cycle.
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