Nature Communications· 2026Q1
Two distinct α2β1 integrin glycan interactions mediate cell entry of a picornavirus
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- 2026year
Short summary
Equine rhinitis A virus (ERAV) enters cells via two distinct interactions with integrin α2β1: one with the receptor's protein surface and another with specific glycans (high-mannose on α2 N112 and sialylated on β1 N269).
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Key points
- Integrin α2β1 is identified as the protein receptor for equine rhinitis A virus (ERAV).
- ERAV binds to the β-propeller domain of the α2 chain of integrin α2β1.
- ERAV also interacts with a high-mannose glycan at α2 N112 and a sialylated glycan at β1 N269.
- These glycan interactions are critical for ERAV's entry into host cells.
AI-generated from the title and abstract; the full text is not read.
Abstract
Abstract Equine rhinitis A virus (ERAV), a picornavirus closely related to foot-and-mouth disease virus, causes respiratory infections in horses. We performed a HEK293T CRISPRi screen and identified integrin α2β1 as a protein receptor for ERAV. Using knock-out cells and pretreating cells with an antibody or soluble receptor, we confirmed the importance of this integrin for infection of multiple cell types, including equine fibroblasts. Cryo-EM and glycoproteomics analyses revealed that ERAV binds integrin α2β1 in its closed conformation by attaching to the β-propeller of the α2 chain, independent of divalent cations, as well as to a high-mannose glycan on α2 N112 and a sialylated glycan on β1 N269. Using glycan knockout and knock-in cells and by reconstituting integrin α2β1-depleted cells with mutant receptors, we demonstrated the importance of these glycans for virus entry. Our results identify a hitherto unseen combination of protein and glycan interactions between a virus and its receptor.
The authors' abstract, as published at the source. Nature Communications, 2026 · DOI ↗
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Field: Immunology and Allergy
Immunology and AllergyMedicine