ArticleProceedings of the National Academy of Sciences of the United States of America2020
Cryo-EM structure of eastern equine encephalitis virus in complex with heparan sulfate analogues.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- The residue 86 of the Getah virus E2 glycoprotein mediates both glycosaminoglycan- and LDLR-dependent infection.PLoS pathogens · 2026Article
- LRP4 is an entry receptor for multiple encephalitic alphaviruses.Nature communications · 2026Article
- Informed mutation of western equine encephalitis virus to heparan sulfate binding: Implications for rational design of alphavirus live attenuated vaccines.PLoS pathogens · 2026Article
- Novel HIV-1 fusion peptide immunogens using glycan-engineered alphavirus-like particles.NPJ vaccines · 2025Article
- Structural elucidation of a unique binding mode by an intact alphavirus human IgG molecule to a quaternary epitope.Nature communications · 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
- A detailed kinetic model of Eastern equine encephalitis virus replication in a susceptible host cell.PLoS computational biology · 2025Article
- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
- The VLDLR entry receptor is required for the pathogenesis of multiple encephalitic alphaviruses.Cell reports · 2024Article
- The receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes.Nature communications · 2024Article
- Phagocyte-expressed glycosaminoglycans promote capture of alphaviruses from the blood circulation in a host species-specific manner.PNAS nexus · 2024Article
- Structural and functional basis of VLDLR receptor usage by Eastern equine encephalitis virus.bioRxiv : the preprint server for biology · 2023Article
- Structural constraints link differences in neutralization potency of human anti-Eastern equine encephalitis virus monoclonal antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- SARS-CoV-2 Omicron Subvariants Balance Host Cell Membrane, Receptor, and Antibody Docking via an Overlapping Target Site.Viruses · 2023Article
- Early Genomic Surveillance and Phylogeographic Analysis of Getah Virus, a Reemerging Arbovirus, in Livestock in China.Journal of virology · 2023Article
- Cryo-EM structures of alphavirus conformational intermediates in low pH-triggered prefusion states.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022Review
- Glycosaminoglycan binding by arboviruses: a cautionary tale.The Journal of general virology · 2022Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Eastern equine encephalitis virus (EEEV), a mosquito-borne icosahedral alphavirus found mainly in North America, causes human and equine neurotropic infections. EEEV neurovirulence is influenced by the interaction of the viral envelope protein E2 with heparan sulfate (HS) proteoglycans from the host's plasma membrane during virus entry. Here, we present a 5.8-Å cryoelectron microscopy (cryo-EM) structure of EEEV complexed with the HS analog heparin. "Peripheral" HS binding sites were found to be associated with the base of each of the E2 glycoproteins that form the 60 quasi-threefold spikes (q3) and the 20 sites associated with the icosahedral threefold axes (i3). In addition, there is one HS site at the vertex of each q3 and i3 spike (the "axial" sites). Both the axial and peripheral sites are surrounded by basic residues, suggesting an electrostatic mechanism for HS binding. These residues are highly conserved among EEEV strains, and therefore a change in these residues might be linked to EEEV neurovirulence.
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