ArticleProceedings of the National Academy of Sciences of the United States of America2013
Uncoating of common cold virus is preceded by RNA switching as determined by X-ray and cryo-EM analyses of the subviral A-particle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 65 citations in OpenAlex.
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- Extracellular uncoating of bacteriophage MS2.Journal of molecular biology · 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
- Clicking viruses-with chemistry toward mechanisms in infection.Journal of virology · 2025Review
- Development of a novel EV-A71 monoclonal antibody for monitoring vaccine potency.PLoS neglected tropical diseases · 2025Article
- DMSO might impact ligand binding, capsid stability, and RNA interaction in viral preparations.Scientific reports · 2024Article
- Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating.Communications biology · 2024Article
- Endosome rupture enables enteroviruses from the family Picornaviridae to infect cells.Communications biology · 2024Article
- Broadly therapeutic antibody provides cross-serotype protection against enteroviruses via Fc effector functions and by mimicking SCARB2.Nature microbiology · 2024Article
- The Basic Architecture of Viruses.Sub-cellular biochemistry · 2024Review
- Conventional Electron Microscopy, Cryogenic Electron Microscopy, and Cryogenic Electron Tomography of Viruses.Sub-cellular biochemistry · 2024Review
- A human monoclonal antibody binds within the poliovirus receptor-binding site to neutralize all three serotypes.Nature communications · 2023Article
- Stabilization of the Quadruplex-Forming G-Rich Sequences in the Rhinovirus Genome Inhibits Uncoating-Role of NaViruses · 2023Article
- Structural Studies Reveal that Endosomal Cations Promote Formation of Infectious Coxsackievirus A9 A-Particles, Facilitating RNA and VP4 Release.Journal of virology · 2022Article
- Review
- ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Virion structure andJournal of virology · 2021Article
- Capsid opening enables genome release of iflaviruses.Science advances · 2021Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
During infection, viruses undergo conformational changes that lead to delivery of their genome into host cytosol. In human rhinovirus A2, this conversion is triggered by exposure to acid pH in the endosome. The first subviral intermediate, the A-particle, is expanded and has lost the internal viral protein 4 (VP4), but retains its RNA genome. The nucleic acid is subsequently released, presumably through one of the large pores that open at the icosahedral twofold axes, and is transferred along a conduit in the endosomal membrane; the remaining empty capsids, termed B-particles, are shuttled to lysosomes for degradation. Previous structural analyses revealed important differences between the native protein shell and the empty capsid. Nonetheless, little is known of A-particle architecture or conformation of the RNA core. Using 3D cryo-electron microscopy and X-ray crystallography, we found notable changes in RNA-protein contacts during conversion of native virus into the A-particle uncoating intermediate. In the native virion, we confirmed interaction of nucleotide(s) with Trp(38) of VP2 and identified additional contacts with the VP1 N terminus. Study of A-particle structure showed that the VP2 contact is maintained, that VP1 interactions are lost after exit of the VP1 N-terminal extension, and that the RNA also interacts with residues of the VP3 N terminus at the fivefold axis. These associations lead to formation of a well-ordered RNA layer beneath the protein shell, suggesting that these interactions guide ordered RNA egress.
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