ArticlemBio2025
Completely conserved VP2 residue K140 of KREMEN1-dependent enteroviruses is critical for virus-receptor interactions and viral infection.
Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it.
- 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
- 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
- A single residue in the VP3 capsid protein governs virulence and informs live-attenuated vaccine design for coxsackievirus A6.Journal of virology · 2026Article
- Review
- A conserved VP1-286 epitope governs neutralization and immune escape in Coxsackievirus A6.Frontiers in immunology · 2026Article
- Molecular mechanisms of receptor recognition and antibody neutralization of coxsackievirus A6.Nature communications · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The KREMEN1 (KRM1) protein is a cellular receptor for multiple enteroviruses that cause hand, foot, and mouth disease (HFMD), including coxsackievirus CVA2, CVA3, CVA4, CVA5, CVA6, CVA10, and CVA12. The molecular basis for the broad recognition of these viruses by the KRM1 receptor remains unclear. Here, we report the indispensable role of the completely conserved VP2 capsid protein residue K140 (designated K2140) in mediating receptor recognition and infection by CVA10 and other KRM1-dependent enteroviruses. Residue K2140 not only facilitates receptor recognition, cell attachment, and infection of CVA10 but also contributes to CVA10 pathogenicity IMPORTANCE: Hand, foot, and mouth disease (HFMD) annually affects millions of children worldwide. HFMD is caused by various enteroviruses, such as coxsackieviruses CVA6, CVA16, CVA10, and enterovirus 71 (EV-A71). Licensed inactivated EV-A71 vaccines do not provide cross-protection against other enteroviruses. There are no drugs specifically for HFMD. KREMEN1 (KRM1) serves as the cellular receptor for many HFMD-related enteroviruses, including CVA2-CVA6, CVA10, and CVA12. However, the molecular basis for broad recognition of these enteroviruses by the KRM1 receptor remains elusive. Here, we report that VP2 residue K140 (K2140) is completely conserved among all KRM1-dependent enteroviruses and is essential for virus-receptor binding and viral infection by interacting with residue D90 of KRM1. Overall, our findings provide a deeper understanding of the molecular basis of KRM1-dependent enterovirus infection
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