ArticleProceedings of the National Academy of Sciences of the United States of America2020
Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- The C-terminal T234 residue of VP3 is required for KREMEN1 receptor-dependent infectivity and pathogenesis of coxsackieviruses A10 and A8.Virologica Sinica · 2026Article
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- VP1-141 is a determinant of a Vero cell-adapted Coxsackievirus A10 for vaccine development.PLoS neglected tropical diseases · 2026Article
- A single residue in the VP3 capsid protein governs virulence and informs live-attenuated vaccine design for coxsackievirus A6.Journal of virology · 2026Article
- Neutralizing human monoclonal antibodies to poliovirus map to the receptor binding site.Nature communications · 2026Article
- 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
- Binding ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Pathological characteristics of a murine oral coxsackievirus A10 infection model.Journal of virology · 2025Article
- Article
- Receptors and Host Factors for Enterovirus Infection: Implications for Cancer Therapy.Cancers · 2024Review
- Coxsackievirus A10 impairs nail regeneration and induces onychomadesis by mimicking DKK1 to attenuate Wnt signaling.The Journal of experimental medicine · 2024Article
- The nucleoside analog 4'-fluorouridine suppresses the replication of multiple enteroviruses by targeting 3D polymerase.Antimicrobial agents and chemotherapy · 2024Article
- Virus-Receptor Interactions and Receptor-Mediated Virus Entry into Host Cells.Sub-cellular biochemistry · 2024Review
- Oncolytic virotherapy against lung cancer: key receptors and signaling pathways of viral entry.Frontiers in immunology · 2024Review
- Genomic surveillance reveals low-level circulation of two subtypes of genogroup C coxsackievirus A10 in Nanchang, Jiangxi Province, China, 2015-2023.Frontiers in microbiology · 2024Article
- Article
- 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
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection.
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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.