ArticleNature communications2022
Molecular mechanism of antibody neutralization of coxsackievirus A16.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.
- Historical evolution, research hotspots and emerging trends of pediatric hand, foot, and mouth disease: a bibliometric worldview since the 21st century.Frontiers in medicine · 2025Pooled it
- Potent neutralization of Rift Valley fever virus mediated by monoclonal antibodies via concurrent inhibition of attachment and fusion.Emerging microbes & infections · 2026Article
- Calycosin targets the MAPK-EGR1 signaling axis to inhibit enterovirus 71 replication in cells and human colonic organoids.Virulence · 2026Article
- The SARS-CoV-2 S2'-helix compared to stem helix confers higher genetic barrier to antibody resistance.PLoS pathogens · 2026Article
- The C-terminal T234 residue of VP3 is required for KREMEN1 receptor-dependent infectivity and pathogenesis of coxsackieviruses A10 and A8.Virologica Sinica · 2026Article
- Neurotropism and interferon-dominated immune responses in a mouse-adapted coxsackievirus A16 infection model.Journal of virology · 2026Article
- Molecular characterization and whole-genome sequencing-based genetic evolution of coxsackievirus A16 in Taiyuan City, 2023-2025.Archives of virology · 2026Article
- Highly sensitive and rapid determination of Coxsackievirus A16 using restriction endonuclease-mediated reverse transcription multiple cross displacement amplification.BMC microbiology · 2026Article
- Article
- A conserved VP1-286 epitope governs neutralization and immune escape in Coxsackievirus A6.Frontiers in immunology · 2026Article
- Identification of key amino acids defining conformational neutralizing epitopes of coxsackievirus A5 using monoclonal antibody escape mutants.Frontiers in immunology · 2026Article
- Molecular mechanisms of receptor recognition and antibody neutralization of coxsackievirus A6.Nature communications · 2025Article
- Post-attachment neutralization of HPV16 by antibodies derived from Gardasil-vaccinated women.NPJ vaccines · 2025Article
- Article
- Broadly therapeutic antibody provides cross-serotype protection against enteroviruses via Fc effector functions and by mimicking SCARB2.Nature microbiology · 2024Article
- Identification of four neutralizing antigenic sites on the enterovirus D68 capsid.Journal of virology · 2023Article
- VP2 residue N142 of coxsackievirus A10 is critical for the interaction with KREMEN1 receptor and neutralizing antibodies and the pathogenicity in mice.PLoS pathogens · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus A16 (CVA16) causes hand, foot and mouth disease in infants and young children. However, no vaccine or anti-viral agent is currently available for CVA16. Here, the functions and working mechanisms of two CVA16-specific neutralizing monoclonal antibodies (MAbs), 9B5 and 8C4, are comprehensively investigated. Both 9B5 and 8C4 display potent neutralization in vitro and prophylactic and therapeutic efficacy in a mouse model of CVA16 infection. Mechanistically, 9B5 exerts neutralization primarily through inhibiting CVA16 attachment to cell surface via blockade of CVA16 binding to its attachment receptor, heparan sulfate, whereas 8C4 functions mainly at the post-attachment stage of CVA16 entry by interfering with the interaction between CVA16 and its uncoating receptor SCARB2. Cryo-EM studies show that 9B5 and 8C4 target distinct epitopes located at the 5-fold and 3-fold protrusions of CVA16 capsids, respectively, and exhibit differential binding preference to three forms of naturally occurring CVA16 particles. Moreover, 9B5 and 8C4 are compatible in formulating an antibody cocktail which displays the ability to prevent virus escape seen with individual MAbs. Together, our work elucidates the functional and structural basis of CVA16 antibody-mediated neutralization and protection, providing important information for design and development of effective CVA16 vaccines and antibody therapies.
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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.