9H0B

Crystal structure of the Porcine Hemagglutinating Encephalomyelitis Virus (PHEV) receptor binding domain in complex with porcine DPEP1.

9H0B の概要

• エントリーDOI: 10.2210/pdb9h0b/pdb
• 分子名称: 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)
• 機能のキーワード: rbd receptor spike entry, viral protein
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 148531.04

構造登録者

Fernandez, I.,Rey, F. (登録日: 2024-10-08, 公開日: 2025-08-06, 最終更新日: 2025-11-12)

主引用文献

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

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: 41073662
DOI: 10.1038/s41564-025-02111-7

実験手法

X-RAY DIFFRACTION (2.25 Å)