Evidence map›Paper›PMID 42638709›Full record

ArticleFrontiers in immunology2026

A conserved VP1-286 epitope governs neutralization and immune escape in Coxsackievirus A6.

Jia-Hui Wu, Yi-Hao Sun, Ya-Xin Du, Jie Wu, Hui Wang, Wen-Hui Wang, Jing Guo, Sha-Sha Qian, Xiao-Qi Chen, Shuo Shen

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

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Jia-Hui Wu *Wuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Yi-Hao Sun *Wuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Ya-Xin DuWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Jie WuWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Hui WangWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Wen-Hui WangWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Jing GuoWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Sha-Sha QianWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Xiao-Qi ChenWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.
Shuo ShenWuhan Institute of Biological Products Co., Ltd., Wuhan, Hubei, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Coxsackievirus A6 (CVA6) has emerged as a predominant pathogen of hand, foot, and mouth disease (HFMD) globally. However, the neutralizing epitopes that govern protective immunity, receptor-associated entry, and immune escape remain incompletely defined. This study aimed to identify potent neutralizing monoclonal antibodies (mAbs) against CVA6 and characterize the critical epitope determinants involved in viral neutralization and adaptation. Methods: Neutralizing mAbs were generated using hybridoma technology and evaluated against representative CVA6 clinical isolates by Results: Two conformational neutralizing mAbs, 5A6 and 6D12, exhibited broad neutralizing activity against most tested CVA6 isolates. Both antibodies recognized conformational capsid epitopes and conferred dose-dependent protection Conclusion: This study identifies VP1-A286 as a conserved and functionally important neutralizing epitope determinant in CVA6. Neutralizing mAbs 5A6 and 6D12 recognize overlapping conformational epitopes centered on this residue and inhibit infection through coordinated interference with receptor-associated entry and capsid conformational dynamics. These findings provide new insight into CVA6 antigenicity and immune escape and support the development of structure-guided vaccines and antibody-based therapeutics against CVA6.

Indexed as

Antibodies, NeutralizingAntibodies, ViralCapsid ProteinsCoxsackievirus InfectionsEnterovirus A, HumanEpitopesImmune EvasionAnimalsAntibodies, MonoclonalFemaleHumansMiceMice, Inbred BALB CNeutralization TestsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsEpitopesCoxsackievirus A6immune escapeKREMEN1neutralizing monoclonal antibodyviral entryVP1 epitope

Identifiers

PMID42638709
PMCPMC13500566

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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.