ArticleNature communications2025
Structural basis for engagement of Western Equine Encephalitis Virus with the PCDH10 receptor.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- LRP4 is an entry receptor for multiple encephalitic alphaviruses.Nature communications · 2026Article
- Structural insights into VLDLR recognition by western equine encephalitis virus.Nature communications · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
PCDH10 is a newly identified general receptor for Western equine encephalitis virus (WEEV) members, a group of encephalitic alphaviruses that cause severe diseases in humans and equids. While WEEV typically binds PCDH10 as a receptor, nonpathogenic strains have evolved to lose mammalian PCDH10 binding, retaining only avian PCDH10 affinity. Virulent strains also engage VLDLR and ApoER2 as alternative receptors. Here, we determine the structure of WEEV strain 71V1658 virus-like particles (VLPs) in complex with human PCDH10 extracellular cadherin repeats 1-2 (EC1-EC2) by cryo-electron microscopy at 2.99 Å resolution. EC1 inserts into a cleft clamped by two adjacent E2-E1 heterodimers within a single trimeric spike, whereas EC2 maintains no contact with the WEEV VLP. Mutagenesis studies elucidate the impacts of the interacting residues on PCDH10. And residue 153 of E2 is crucial for PCDH10 binding, and the
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