ArticleNature structural & molecular biology2015
Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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
64 citing papers in PubMed, 105 citations in OpenAlex.
- Novel Thermostabilizing Formulation for Enhanced Stability of Foot-and-Mouth Disease Virus During Storage and Environmental Stress.Microorganisms · 2026Article
- Performance of prototype serological immunoassays for foot-and-mouth disease virus using G-H loop peptides and stabilized virus-like particles.Microbiology spectrum · 2026Article
- Bioinformatics based design of thermostable virus-like particles-based vaccine for foot-and-mouth disease serotype A andFrontiers in cellular and infection microbiology · 2026Article
- Article
- Article
- Article
- Single-Domain Antibodies That Specifically Recognize Intact Capsids of Multiple Foot-and-Mouth Disease Serotype O Strains.Vaccines · 2025Article
- Cost-effective suspension adaptation of BHK-21 cells for scalable FMD vaccine production in resource-limited settings.Open veterinary journal · 2025Article
- Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail.Nature communications · 2024Article
- A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids.The Journal of general virology · 2024Article
- Review
- Exploring the Effects of Intersubunit Interface Mutations on Virus-Like Particle Structure and Stability.Biochemistry · 2024Article
- Foot-and-mouth disease virus VP1 degrades YTHDF2 through autophagy to regulate IRF3 activity for viral replication.Autophagy · 2024Article
- Calcium Chloride as a Novel Stabilizer for Foot-and-Mouth Disease Virus and Its Application in the Vaccine Formulation.Vaccines · 2024Article
- Computational Methods in Immunology and Vaccinology: Design and Development of Antibodies and Immunogens.Journal of chemical theory and computation · 2023Review
- B and T Cell Epitopes of the Incursionary Foot-and-Mouth Disease Virus Serotype SAT2 for Vaccine Development.Viruses · 2023Review
- Synthesis of a crystalline zeolitic imidazole framework-8 nano-coating on single environment-sensitive viral particles for enhanced immune responses.Nanoscale advances · 2023Article
- Thermostable negative-marker foot-and-mouth disease virus serotype O induces protective immunity in guinea pigs.Applied microbiology and biotechnology · 2023Article
- Article
- Investigation of foot and mouth disease virus and other animal pathogens in cattle, buffaloes and goats at the interface with Akagera National Park 2017 - 2020.BMC veterinary research · 2022Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors at 6 institutions in 3 countries.
Funding
Abstract
Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical pentameric protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of protein-protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.
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.