ArticleNature communications2024
Structural basis for VLDLR recognition by eastern equine encephalitis virus.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- LRP4 is an entry receptor for multiple encephalitic alphaviruses.Nature communications · 2026Article
- Design of a neutralizing and protective pan-encephalitic alphavirus receptor decoy protein.Science translational medicine · 2026Article
- Molecular basis of ApoER2-mediated Semliki Forest virus entry.Nature communications · 2025Article
- Structural insights into VLDLR recognition by western equine encephalitis virus.Nature communications · 2025Article
- Chronic Neuroplasticity Changes Following Neurotropic Viral Infection: Mechanisms and Implications.Cellular and molecular neurobiology · 2025Review
- Three positively charged binding sites on the eastern equine encephalitis virus E2 glycoprotein coordinate heparan sulfate- and protein receptor-dependent infection.Nature communications · 2025Article
- Basic patches on the E2 glycoprotein of eastern equine encephalitis virus influence viral vascular clearance and dissemination in mice.Journal of virology · 2025Article
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- Article
- Eastern equine encephalitis virus: Pathogenesis, immune response, and clinical manifestations.Infectious medicine · 2025Review
- Neuropathogenesis of Encephalitic Alphaviruses in Non-Human Primate and Mouse Models of Infection.Pathogens (Basel, Switzerland) · 2025Review
- Advances in molecular regulation and function of LDLR family in viral infection.Frontiers in microbiology · 2025Review
- Structural insights into Semiliki forest virus receptor binding modes indicate novel mechanism of virus endocytosis.PLoS pathogens · 2024Article
- The many ways in which alphaviruses bind to cells.Trends in immunology · 2024Review
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Eastern equine encephalitis virus (EEEV) is the most virulent alphavirus that infects humans, and many survivors develop neurological sequelae, including paralysis and intellectual disability. Alphavirus spike proteins comprise trimers of heterodimers of glycoproteins E2 and E1 that mediate binding to cellular receptors and fusion of virus and host cell membranes during entry. We recently identified very-low density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) as cellular receptors for EEEV and a distantly related alphavirus, Semliki Forest virus (SFV). Here, we use single-particle cryo-electron microscopy (cryo-EM) to determine structures of the EEEV and SFV spike glycoproteins bound to the VLDLR ligand-binding domain and found that EEEV and SFV interact with the same cellular receptor through divergent binding modes. Our studies suggest that the ability of LDLR-related proteins to interact with viral spike proteins through very small footprints with flexible binding modes results in a low evolutionary barrier to the acquisition of LDLR-related proteins as cellular receptors for diverse sets of viruses.
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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.