ArticleNature communications2024
The receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes.
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 18 papers.
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Who cites it
18 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
- Cryo-EM structure of the Rift Valley fever virus envelope protein in complex with a potent neutralization antibody.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- LRP1 Interacts with the Rift Valley Fever Virus Glycoprotein Gn via a Calcium-Dependent Multivalent Electrostatic Mechanism.Biomolecules · 2025Article
- 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
- Residues 27T and 297A in VP2 contribute to the enhanced replication and pathogenicity of raccoon dog parvovirus.Journal of virology · 2025Article
- Eastern Equine Encephalitis Virus Exhibits More Charged Amino Acids in Its Envelope Proteins, Compared to Madariaga Virus.The American journal of tropical medicine and hygiene · 2025Article
- Three positively charged binding sites on the eastern equine encephalitis virus E2 glycoprotein coordinate heparan sulfate- and protein receptor-dependent infection.Nature communications · 2025Article
- Review
- Basic patches on the E2 glycoprotein of eastern equine encephalitis virus influence viral vascular clearance and dissemination in mice.Journal of virology · 2025Article
- Article
- Article
- 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
- Eastern Equine Encephalitis Virus: The Importance of Metabolism and Aging.International journal of molecular sciences · 2024Review
- Structural insights into Semiliki forest virus receptor binding modes indicate novel mechanism of virus endocytosis.PLoS pathogens · 2024Article
- Structural basis for VLDLR recognition by eastern equine encephalitis virus.Nature communications · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of EEEV. Herein, we performed cryo-electron microscopy structural and biochemistry studies on the specific interactions between EEEV and VLDLR. Our results show that VLDLR binds EEEV at three different sites A, B and C through its membrane-distal LDLR class A (LA) repeats. Site A is located in the cleft in between the E1-E2 heterodimers. Site B is located near the connecting β ribbon of E2 and is in proximity to site A, while site C is on the domain B of E2. The binding of VLDLR LAs to EEEV is in complex modes, including the LA1-2 and LA3-5 mediated two major modes. Disruption of the LA1-2 mediated binding significantly affect the cell attachment of EEEV. However, the mutation W132G of VLDLR impairs the binding of LA3, drives the switch of the binding modes, and significantly enhances the attachment of EEEV to the cell. The W132G variant of VLDLR could be identified in human genome and SNP sequences, implying that people with similar mutations in VLDLR may be highly susceptible to EEEV infection.
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