ArticleThe Journal of general virology2022
Thermal stabilization of enterovirus A 71 and production of antigenically stabilized empty capsids.
Article in The Journal of general virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
8 citing papers in PubMed, 8 citations in OpenAlex.
- Structural and functional mapping of protective human monoclonal antibodies against enterovirus A71.Science advances · 2026Article
- Viral vector-driven trans-encapsidation of replicon RNAs as a rapid approach for the development of safe and economically attractive anti-enterovirus vaccines.bioRxiv : the preprint server for biology · 2025Article
- Development of enterovirus transencapsidation assays as tools to understand viral entry.The Journal of general virology · 2025Article
- Enterovirus-like particles encapsidate RNA and exhibit decreased stability due to lack of maturation.PLoS pathogens · 2025Article
- Substitution of Coxsackievirus A16 VP1 BC and EF Loop Altered the Protective Immune Responses in Chimera Enterovirus A71.Vaccines · 2023Article
- Production of antigenically stable enterovirus A71 virus-like particles inThe Journal of general virology · 2023Article
- Production of antigenically stable enterovirus A71 virus-like particles inbioRxiv : the preprint server for biology · 2023Article
- Molecular Determinants of Human Rhinovirus Infection, Assembly, and Conformational Stability at Capsid Protein Interfaces.Journal of virology · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Enterovirus A71 (EVA71) infection can result in paralysis and may be fatal. In common with other picornaviruses, empty capsids are produced alongside infectious virions during the viral lifecycle. These empty capsids are antigenically indistinguishable from infectious virus, but at moderate temperatures they are converted to an expanded conformation. In the closely related poliovirus, native and expanded antigenic forms of particle have different long-term protective efficacies when used as vaccines. The native form provides long-lived protective immunity, while expanded capsids fail to generate immunological protection. Whether this is true for EVA71 remains to be determined. Here, we selected an antigenically stable EVA71 virus population using successive rounds of heating and passage and characterized the antigenic conversion of both virions and empty capsids. The mutations identified within the heated passaged virus were dispersed across the capsid, including at key sites associated with particle expansion. The data presented here indicate that the mutant sequence may be a useful resource to address the importance of antigenic conformation in EVA71 vaccines.
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Registered trials
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.