ArticleProceedings of the National Academy of Sciences of the United States of America2018
Molecular basis for the acid-initiated uncoating of human enterovirus D68.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 30 citations in OpenAlex.
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- Comparative immunogenic and structural analysis of virus-like particle and inactivated whole-virion vaccines against enterovirus D68.Molecular therapy. Nucleic acids · 2026Article
- EV-D68 exploits clathrin-mediated endocytosis and compensatory macropinocytosis for cellular entry.Journal of virology · 2026Article
- Pathogens of the human central nervous system-the major viral pathogens.Journal of neurovirology · 2026Review
- Cepharanthine inhibits enterovirus entry by endolysosomal deacidification and exhibits protective activityAntimicrobial agents and chemotherapy · 2025Article
- Antiviral candidates for enterovirus 71: targeting viral proteome and stage-specific lifecycle interventions.Virology journal · 2025Review
- 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
- Structural insights from vaccine candidates for EV-D68.Communications biology · 2025Article
- MFSD6 is an entry receptor for enterovirus D68.Nature · 2025Article
- Discovery of A-967079 as an Enterovirus D68 Antiviral by Targeting the Viral 2C Protein.ACS infectious diseases · 2024Article
- Understanding neurotropic enteric viruses: routes of infection and mechanisms of attenuation.Cellular and molecular life sciences : CMLS · 2024Review
- Enterovirus virus-like-particle and inactivated poliovirus vaccines do not elicit substantive cross-reactive antibody responses.PLoS pathogens · 2024Article
- Enterovirus-D68 - A Reemerging Non-Polio Enterovirus that Causes Severe Respiratory and Neurological Disease in Children.Frontiers in virology (Lausanne, Switzerland) · 2024Article
- Identification of four neutralizing antigenic sites on the enterovirus D68 capsid.Journal of virology · 2023Article
- The Picornaviridae Family: Knowledge Gaps, Animal Models, Countermeasures, and Prototype Pathogens.The Journal of infectious diseases · 2023Article
- Quantitative analysis of protein dynamics using a deep learning technique combined with experimental cryo-EM density data and MD simulations.Biophysics and physicobiology · 2023Article
- Structure of Human Enterovirus 70 and Its Inhibition by Capsid-Binding Compounds.Journal of virology · 2022Article
- Atomic Structures of Coxsackievirus B5 Provide Key Information on Viral Evolution and Survival.Journal of virology · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Enterovirus D68 (EV-D68) belongs to a group of enteroviruses that contain a single positive-sense RNA genome surrounded by an icosahedral capsid. Like common cold viruses, EV-D68 mainly causes respiratory infections and is acid-labile. The molecular mechanism by which the acid-sensitive EV-D68 virions uncoat and deliver their genome into a host cell is unknown. Using cryoelectron microscopy (cryo-EM), we have determined the structures of the full native virion and an uncoating intermediate [the A (altered) particle] of EV-D68 at 2.2- and 2.7-Å resolution, respectively. These structures showed that acid treatment of EV-D68 leads to particle expansion, externalization of the viral protein VP1 N termini from the capsid interior, and formation of pores around the icosahedral twofold axes through which the viral RNA can exit. Moreover, because of the low stability of EV-D68, cryo-EM analyses of a mixed population of particles at neutral pH and following acid treatment demonstrated the involvement of multiple structural intermediates during virus uncoating. Among these, a previously undescribed state, the expanded 1 ("E1") particle, shows a majority of internal regions (e.g., the VP1 N termini) to be ordered as in the full native virion. Thus, the E1 particle acts as an intermediate in the transition from full native virions to A particles. Together, the present work delineates the pathway of EV-D68 uncoating and provides the molecular basis for the acid lability of EV-D68 and of the related common cold viruses.
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