Evidence map›Paper›PMID 42247493›Full record

ArticleScience advances2026

Structural and functional mapping of protective human monoclonal antibodies against enterovirus A71.

Daming Zhou, Abhay Kotecha, James T Kelly, Peng-Nien Huang, Yi-Yin Chen, Thomas S Walter, Helen M E Duyvesteyn, Raymond J Owens, Shu-Yuan Ho, Tzou-Yien Lin and 4 more

Abstract read
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In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Daming ZhouCollege of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0002-7188-5243
Abhay KotechaDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID 0000-0002-4480-5439
James T KellyThe Pirbright Institute, Woking, Surrey, UK.ORCID 0000-0002-8307-507X
Peng-Nien HuangResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.ORCID 0000-0002-7345-2361
Yi-Yin ChenGraduate Institute of Immunology and Department of Pediatrics, National Taiwan University Hospital, College of Medicine, National Taiwan University, Taipei, Taiwan.
Thomas S WalterDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID 0000-0002-0030-7235
Helen M E DuyvesteynDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID 0000-0002-4641-5442
Raymond J OwensDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Shu-Yuan HoDepartment of Laboratory Medicine, National Taiwan University Hospital and National Taiwan University College of Medicine, Taipei, Taiwan.
Tzou-Yien LinDivision of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan, Taiwan.ORCID 0000-0002-6175-2471
Elizabeth E FryDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID 0000-0001-9754-5303
Jingshan RenDivision of Structural Biology, Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID 0000-0003-4015-1404
Kuan-Ying A HuangGraduate Institute of Immunology and Department of Pediatrics, National Taiwan University Hospital, College of Medicine, National Taiwan University, Taipei, Taiwan.ORCID 0000-0001-6891-6945
David I StuartChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.ORCID 0000-0002-3426-4210

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EV-A71 has been responsible for recent severe HFMD outbreaks. We report structures for 12 potently neutralizing human anti-EV-A71 monoclonal antibody Fabs, alone and complexed with virus. Most recognize the native antigenic state with epitopes that span interfaces, together covering 85% of the capsid surface. The majority (8 of 12) bind the canyon, while the others cluster around the icosahedral two- and threefold axes. Blocking SCARB2 receptor binding likely contributes to neutralization for all, and a subset induces empty particles. A predominant gene family (IGHV4-39) does not dictate a common binding pose. Long CDR-H3 loops are frequently key to binding, especially at the canyon, suggesting that antigenicity data based on antibodies with shorter CDR3s (e.g., murine) may be misleading. This dataset reveals neutralization mechanisms for recently circulating EV-A71 genotypes, which will inform immunotherapies. We demonstrate synergy in vitro between canyon binding and both two- and threefold binding antibodies to increase neutralization potency.

Indexed as

Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEnterovirus A, HumanAnimalsEnterovirus InfectionsEpitopesHumansImmunoglobulin Fab FragmentsModels, MolecularProtein BindingAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesImmunoglobulin Fab Fragments

Identifiers

PMID42247493
PMCPMC13240189

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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.