ArticleScience advances2016
The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs.
Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- Enterovirus D68 receptor usage: from static attachment to dynamic entry.Journal of virology · 2026Review
- Asymmetric isopeptide bond steers directional genomic RNA egress from icosahedral virus.Science advances · 2025Article
- Insights into the AAV packaging mechanism: Cryo-EM Structure of the AAV2 Rep-Capsid Packaging Complex.bioRxiv : the preprint server for biology · 2025Article
- Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 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
- Oversized nanodiscs for combined structural and functional investigation of multicomponent membrane protein systems.Scientific reports · 2025Article
- Endosome rupture enables enteroviruses from the family Picornaviridae to infect cells.Communications biology · 2024Article
- Structural basis of the recognition of adeno-associated virus by the neurological system-related receptor carbonic anhydrase IV.PLoS pathogens · 2024Article
- A human monoclonal antibody binds within the poliovirus receptor-binding site to neutralize all three serotypes.Nature communications · 2023Article
- Exosomes mediate Coxsackievirus B3 transmission and expand the viral tropism.PLoS pathogens · 2023Article
- Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future.Biophysical reviews · 2022Review
- Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses.Viruses · 2022Article
- Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion.Communications biology · 2022Article
- Structural and dynamic asymmetry in icosahedrally symmetric virus capsids.Current opinion in virology · 2020Review
- Large nanodiscs going viral.Current opinion in structural biology · 2020Review
- Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10.Nature communications · 2020Article
- Transferrin receptor binds virus capsid with dynamic motion.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Many nonenveloped viruses engage host receptors that initiate capsid conformational changes necessary for genome release. Structural studies on the mechanisms of picornavirus entry have relied on in vitro approaches of virus incubated at high temperatures or with excess receptor molecules to trigger the entry intermediate or A-particle. We have induced the coxsackievirus B3 entry intermediate by triggering the virus with full-length receptors embedded in lipid bilayer nanodiscs. These asymmetrically formed A-particles were reconstructed using cryo-electron microscopy and a direct electron detector. These first high-resolution structures of a picornavirus entry intermediate captured at a membrane with and without imposing icosahedral symmetry (3.9 and 7.8 Å, respectively) revealed a novel A-particle that is markedly different from the classical A-particles. The asymmetric receptor binding triggers minimal global capsid expansion but marked local conformational changes at the site of receptor interaction. In addition, viral proteins extrude from the capsid only at the site of extensive protein remodeling adjacent to the nanodisc. Thus, the binding of the receptor triggers formation of a unique site in preparation for genome release.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.