ArticleThe Journal of biological chemistry2015
Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
15 citing papers in PubMed.
- Review
- Enterovirus A71 priorities, challenges, and future opportunities in humoral immunity and vaccine development.NPJ vaccines · 2025Review
- Screening of Insertion Sites and Tags on EV-A71 VP1 Protein for Recombinant Virus Construction.Viruses · 2025Article
- Integration of HiBiT into enteroviruses: A universal tool for advancing enterovirus virology research.Virologica Sinica · 2024Article
- Article
- Antivirals blocking entry of enteroviruses and therapeutic potential.Journal of biomedical science · 2021Review
- Advances in Antigenic Peptide-Based Vaccine and Neutralizing Antibodies against Viruses Causing Hand, Foot, and Mouth Disease.International journal of molecular sciences · 2019Review
- Structural Vaccinology for Viral Vaccine Design.Frontiers in microbiology · 2019Review
- Immunocompetent and Immunodeficient Mouse Models for Enterovirus 71 Pathogenesis and Therapy.Viruses · 2018Review
- Characterization of human enterovirus71 virus-like particles used for vaccine antigens.PloS one · 2017Article
- Development of Novel Vaccines against Enterovirus-71.Viruses · 2015Review
- Enhanced enterovirus 71 virus-like particle yield from a new baculovirus design.Biotechnology and bioengineering · 2015Article
- Crystal Structures of Yeast-Produced Enterovirus 71 and Enterovirus 71/Coxsackievirus A16 Chimeric Virus-Like Particles Provide the Structural Basis for Novel Vaccine Design against Hand-Foot-and-Mouth Disease.Journal of virology · 2015Article
- GITRL as a genetic adjuvant enhances enterovirus 71 VP1 DNA vaccine immunogenicity.Immunologic research · 2015Article
- Is a multivalent hand, foot, and mouth disease vaccine feasible?Human vaccines & immunotherapeutics · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hand-foot-and-mouth disease (HFMD) remains a major health concern in the Asia-Pacific regions, and its major causative agents include human enterovirus 71 (EV71) and coxsackievirus A16. A desirable vaccine against HFMD would be multivalent and able to elicit protective responses against multiple HFMD causative agents. Previously, we have demonstrated that a thermostable recombinant EV71 vaccine candidate can be produced by the insertion of a foreign peptide into the BC loop of VP1 without affecting viral replication. Here we present crystal structures of two different naturally occurring empty particles, one from a clinical C4 strain EV71 and the other from its recombinant virus containing an insertion in the VP1 BC loop. Crystal structure analysis demonstrated that the inserted foreign peptide is well exposed on the particle surface without significant structural changes in the capsid. Importantly, such insertions do not seem to affect the virus uncoating process as illustrated by the conformational similarity between an uncoating intermediate of another recombinant virus and that of EV71. Especially, at least 18 residues from the N terminus of VP1 are transiently externalized. Altogether, our study provides insights into vaccine development against HFMD.
Indexed as
Identifiers
What OpenQuestion holds
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.