ArticleNature communications2016
Multiple capsid-stabilizing interactions revealed in a high-resolution structure of an emerging picornavirus causing neonatal sepsis.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 48 citations in OpenAlex.
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- New Advances in Small Molecules Targeted at Viral Capsid-Genome Binding.International journal of molecular sciences · 2025Review
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- Enterovirus-like particles encapsidate RNA and exhibit decreased stability due to lack of maturation.PLoS pathogens · 2025Article
- The pseudoknot region and poly-(C) tract comprise an essential RNA packaging signal for assembly of foot-and-mouth disease virus.PLoS pathogens · 2024Article
- Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating.Communications biology · 2024Article
- MYADM binds human parechovirus 1 and is essential for viral entry.Nature communications · 2024Article
- Swin-cryoEM: Multi-class cryo-electron micrographs single particle mixed detection method.PloS one · 2024Article
- The Picornaviridae Family: Knowledge Gaps, Animal Models, Countermeasures, and Prototype Pathogens.The Journal of infectious diseases · 2023Article
- Stability of SARS-CoV-2 and other airborne viruses under different stress conditions.Archives of virology · 2022Article
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
- Article
- Biomechanical Features of Graphene-Augmented Inorganic Nanofibrous Scaffolds and Their Physical Interaction with Viruses.Materials (Basel, Switzerland) · 2020Article
- Viral structural proteins as targets for antivirals.Current opinion in virology · 2020Review
- Assembly of infectious enteroviruses depends on multiple, conserved genomic RNA-coat protein contacts.PLoS pathogens · 2020Article
- Structure of Nora virus at 2.7 Å resolution and implications for receptor binding, capsid stability and taxonomy.Scientific reports · 2020Article
- Development of Monoclonal Antibodies and Antigen-Capture ELISA for Human Parechovirus Type 3.Microorganisms · 2020Article
- Capsid Structure of a Marine Algal Virus of the OrderJournal of virology · 2020Article
- Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The poorly studied picornavirus, human parechovirus 3 (HPeV3) causes neonatal sepsis with no therapies available. Our 4.3-Å resolution structure of HPeV3 on its own and at 15 Å resolution in complex with human monoclonal antibody Fabs demonstrates the expected picornavirus capsid structure with three distinct features. First, 25% of the HPeV3 RNA genome in 60 sites is highly ordered as confirmed by asymmetric reconstruction, and interacts with conserved regions of the capsid proteins VP1 and VP3. Second, the VP0 N terminus stabilizes the capsid inner surface, in contrast to other picornaviruses where on expulsion as VP4, it forms an RNA translocation channel. Last, VP1's hydrophobic pocket, the binding site for the antipicornaviral drug, pleconaril, is blocked and thus inappropriate for antiviral development. Together, these results suggest a direction for development of neutralizing antibodies, antiviral drugs based on targeting the RNA-protein interactions and dissection of virus assembly on the basis of RNA nucleation.
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Registered trials
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