9H0B
Crystal structure of the Porcine Hemagglutinating Encephalomyelitis Virus (PHEV) receptor binding domain in complex with porcine DPEP1.
Summary for 9H0B
| Entry DOI | 10.2210/pdb9h0b/pdb |
| Descriptor | Dipeptidase 1, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | rbd receptor spike entry, viral protein |
| Biological source | Sus scrofa (pig) More |
| Total number of polymer chains | 4 |
| Total formula weight | 148531.04 |
| Authors | Fernandez, I.,Rey, F. (deposition date: 2024-10-08, release date: 2025-08-06, Last modification date: 2025-11-12) |
| Primary citation | Dufloo, J.,Fernandez, I.,Arbabian, A.,Haouz, A.,Temperton, N.,Gimenez-Lirola, L.G.,Rey, F.A.,Sanjuan, R. Dipeptidase 1 is a functional receptor for a porcine coronavirus. Nat Microbiol, 10:2981-2996, 2025 Cited by PubMed Abstract: Coronaviruses of the subgenus Embecovirus include several important pathogens, such as the human seasonal coronaviruses HKU1 and OC43, bovine coronavirus and porcine haemagglutinating encephalomyelitis virus (PHEV). While sialic acid is thought to be required for embecovirus entry, protein receptors remain unknown for most of these viruses. Here we show that PHEV does not require sialic acid for entry and instead uses dipeptidase 1 (DPEP1) as a receptor. Cryo-electron microscopy at 3.4-4.4 Å resolution revealed that, unlike other embecoviruses, PHEV displays both open and closed conformations of its spike trimer at steady state. The spike receptor-binding domain (RBD) exhibits extremely high sequence variability across embecoviruses, and we found that DPEP1 usage is specific to PHEV. In contrast, the X-ray structure of the RBD-DPEP1 complex at 2.25 Å showed that the structural elements involved in receptor binding are conserved, highlighting the remarkable versatility of this structural organization in adopting novel receptor specificities. PubMed: 41073662DOI: 10.1038/s41564-025-02111-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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