Evidence map›Paper›PMID 39389971›Full record

ArticleNature communications2024

Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail.

Haozhou Li, Pan Liu, Hu Dong, Aldo Dekker, Michiel M Harmsen, Huichen Guo, Xiangxi Wang, Shiqi Sun

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. EngineeringMicroorganisms · 2026
    Article
  3. Review
  4. Article
  5. Article
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  8. Article
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  15. Article
  16. Application ofVeterinary sciences · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Haozhou Li *State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.ORCID http://orcid.org/0000-0002-3017-5819
Pan Liu *CAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Hu Dong *State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Aldo DekkerWageningen Bioveterinary Research, Wageningen University & Research, Lelystad, The Netherlands.
Michiel M HarmsenWageningen Bioveterinary Research, Wageningen University & Research, Lelystad, The Netherlands.ORCID http://orcid.org/0000-0003-4366-5187
Huichen GuoState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China. guohuichen@caas.cn.ORCID http://orcid.org/0000-0003-0539-497X
Xiangxi WangCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. xiangxi@ibp.ac.cn.ORCID http://orcid.org/0000-0003-0635-278X
Shiqi SunState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China. sunshiqi@caas.cn.ORCID http://orcid.org/0000-0003-4975-739X

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32072847,32072859, 32301127Natural Science Foundation of Gansu Province 22JR5RA032, 23JRRA551
6 · The paper itself

Abstract

Unlike most other picornaviruses, foot-and-mouth disease (FMD) intact virions (146S) dissociate easily into small pentameric subunits (12S). This causes a dramatically decreased immunogenicity by a mechanism that remains elusive. Here, we present the high-resolution structures of 12S (3.2 Å) and its immune complex of a single-domain antibody (VHH) targeting the particle interior (3.2 Å), as well as two 146S-specific VHHs complexed to distinct sites on the 146S capsid surface (3.6 Å and 2.9 Å). The antigenic landscape of 146S is depicted using 13 known FMD virus-antibody complexes. Comparison of the immunogenicity of 146S and 12S in pigs, focusing on the resulting antigenic sites and incorporating structural analysis, reveals that dissociation of 146S leads to structural alteration and destruction of multiple epitopes, resulting in significant differences in antibody profiles/lineages induced by 12S and 146S. Furthermore, 146S generates higher synergistic neutralizing antibody titers compared to 12S, whereas both particles induce similar total FMD virus specific antibody titers. This study can guide the structure-based rational design of novel multivalent and broad-spectrum recombinant vaccines for protection against FMD.

Indexed as

Antibodies, NeutralizingAntibodies, ViralAntigens, ViralFoot-and-Mouth DiseaseFoot-and-Mouth Disease VirusAnimalsCapsidCapsid ProteinsEpitopesModels, MolecularSingle-Domain AntibodiesSwineViral VaccinesVirionAntibodies, NeutralizingAntibodies, ViralAntigens, ViralCapsid ProteinsEpitopesSingle-Domain AntibodiesViral Vaccines

Identifiers

PMID39389971
PMCPMC11467346

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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Registered trials

None linked

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.