Evidence map›Paper›PMID 33909694›Full record

ArticlePLoS pathogens2021

Structures of Foot-and-mouth Disease Virus with neutralizing antibodies derived from recovered natural host reveal a mechanism for cross-serotype neutralization.

Yong He, Kun Li, Yimei Cao, Zixian Sun, Pinghua Li, Huifang Bao, Sheng Wang, Guoqiang Zhu, Xingwen Bai, Pu Sun and 6 more

Abstract read
In one paragraph

Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  16. The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.Acta crystallographica. Section F, Structural biology communications · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Yong HeState Key Laboratory of Medicinal Chemical Biology and Drug Discovery Center for Infectious Disease, College of Pharmacy, Nankai University, Tianjin, China.ORCID 0000-0002-7460-2691
Kun LiState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Yimei CaoState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Zixian SunMOE Key Laboratory of Protein Science & Collaborative Innovation Center of Biotherapy, School of Medicine and School of Life Sciences, Tsinghua University, Beijing, China.
Pinghua LiState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Huifang BaoState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Sheng WangState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.ORCID 0000-0002-3079-4222
Guoqiang ZhuState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Xingwen BaiState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Pu SunState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Xuerong LiuChina Agricultural Vet Biology and Technology Co. Ltd., Lanzhou, China.
Cheng YangState Key Laboratory of Medicinal Chemical Biology and Drug Discovery Center for Infectious Disease, College of Pharmacy, Nankai University, Tianjin, China.ORCID 0000-0001-9431-290X
Zaixin LiuState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Zengjun LuState Key Laboratory of Veterinary Etiological Biology, National Foot-and-Mouth Diseases Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Zihe RaoState Key Laboratory of Medicinal Chemical Biology and Drug Discovery Center for Infectious Disease, College of Pharmacy, Nankai University, Tianjin, China.
Zhiyong LouMOE Key Laboratory of Protein Science & Collaborative Innovation Center of Biotherapy, School of Medicine and School of Life Sciences, Tsinghua University, Beijing, China.ORCID 0000-0003-2728-881X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of a universal vaccine against foot-and-mouth disease virus (FMDV) is hindered by cross-serotype antigenic diversity and by a lack of knowledge regarding neutralization of the virus in natural hosts. In this study, we isolated serotype O-specific neutralizing antibodies (NAbs) (F145 and B77) from recovered natural bovine hosts by using the single B cell antibody isolation technique. We also identified a serotype O/A cross-reacting NAb (R50) and determined virus-NAb complex structures by cryo-electron microscopy at near-atomic resolution. F145 and B77 were shown to engage the capsid of FMDV-O near the icosahedral threefold axis, binding to the BC/HI-loop of VP2. In contrast, R50 engages the capsids of both FMDV-O and FMDV-A between the 2- and 5-fold axes and binds to the BC/EF/GH-loop of VP1 and to the GH-loop of VP3 from two adjacent protomers, revealing a previously unknown antigenic site. The cross-serotype neutralizing epitope recognized by R50 is highly conserved among serotype O/A. These findings help to elucidate FMDV neutralization by natural hosts and provide epitope information for the development of a universal vaccine for cross-serotype protection against FMDV.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralAntigenic VariationCapsidCattleCryoelectron MicroscopyEpitopesFoot-and-Mouth DiseaseFoot-and-Mouth Disease VirusSerogroupAntibodies, NeutralizingAntibodies, ViralEpitopes

Identifiers

PMID33909694
PMCPMC8081260

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Registered trials

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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.