ArticleJournal of virology2017
Beta-Propiolactone Inactivation of Coxsackievirus A16 Induces Structural Alteration and Surface Modification of Viral Capsids.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Antigen anisotropy: The overlooked geometric determinant of vaccine immunogenicity and fidelity.Human vaccines & immunotherapeutics · 2026Review
- Atomic force microscopy-based topographical imaging of SARS-CoV-2 as part of a tripartite strategy for RNA virus characterization.Journal of translational medicine · 2025Article
- Strain-release alkylation of Asp12 enables mutant selective targeting of K-Ras-G12D.Nature chemical biology · 2024Article
- Development of an Antigen Detection Kit Capable of Discriminating the Omicron Mutants of SARS-CoV-2.Vaccines · 2023Article
- Antigenicity and immunogenicity of chikungunya virus-like particles from mosquito cells.Applied microbiology and biotechnology · 2023Article
- Umbilical cord-mesenchymal stem cells induce a memory phenotype in CD4Frontiers in immunology · 2023Article
- Molecular mechanism of antibody neutralization of coxsackievirus A16.Nature communications · 2022Article
- Comparison of Physical and Biochemical Characterizations of SARS-CoV-2 Inactivated by Different Treatments.Viruses · 2022Article
- Influence of SARS-CoV-2 inactivation by different chemical reagents on the humoral response evaluated in a murine model.Molecular immunology · 2022Article
- An Overview of Veterinary Viral Diseases and Vaccine Technologies.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Inactivation of SARS-CoV-2 by β-propiolactone causes aggregation of viral particles and loss of antigenic potential.Virus research · 2021Article
- Balancing the influenza neuraminidase and hemagglutinin responses by exchanging the vaccine virus backbone.PLoS pathogens · 2021Article
- Expecting the unexpected with COVID-19 vaccines.The Lancet. Infectious diseases · 2021Article
- Identification of Antibodies with Non-overlapping Neutralization Sites that Target Coxsackievirus A16.Cell host & microbe · 2020Article
- Advances in Antigenic Peptide-Based Vaccine and Neutralizing Antibodies against Viruses Causing Hand, Foot, and Mouth Disease.International journal of molecular sciences · 2019Review
- Gas chromatography-mass spectrometry method for determination ofJournal of pharmaceutical analysis · 2018Article
- Microbiology catches the cryo-EM bug.Current opinion in microbiology · 2018Review
- A 3.0-Angstrom Resolution Cryo-Electron Microscopy Structure and Antigenic Sites of Coxsackievirus A6-Like Particles.Journal of virology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Beta-propiolactone (BPL) is an inactivating agent that is widely used in the vaccine industry. However, its effects on vaccine protein antigens and its mechanisms of action remain poorly understood. Here we present cryo-electron microscopy (cryo-EM) structures of BPL-treated coxsackievirus A16 (CVA16) mature virions and procapsids at resolutions of 3.9 Å and 6.5 Å, respectively. Notably, both particles were found to adopt an expanded conformation resembling the 135S-like uncoating intermediate, with characteristic features including an opened 2-fold channel, the externalization of the N terminus of VP1 capsid protein, and the absence of pocket factor. However, major neutralizing epitopes are very well preserved on these particles. Further biochemical analyses revealed that BPL treatment impairs the abilities of CVA16 particles to bind to the attachment receptor heparan sulfate and to a conformation-dependent monoclonal antibody in a BPL dose-dependent manner, indicating that BPL is able to modify surface-exposed amino acid residues. Taken together, our results demonstrate that BPL treatment may induce alteration of the overall structure and surface properties of a nonenveloped viral capsid, thus revealing a novel mode of action of BPL.
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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.