7VPP

Structures of a deltacoronavirus spike protein bound to porcine and human receptors indicate the risk of virus adaptation to humans

7VPP の概要

• エントリーDOI: 10.2210/pdb7vpp/pdb
• 分子名称: Aminopeptidase, Spike protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: porcine deltacoronavirus, receptor, cross-species transmission, viral protein, hydrolase-viral protein complex, hydrolase/viral protein
• 由来する生物種: Sus scrofa (Pig); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 227874.62

構造登録者

Ji, W.,Xu, Y.,Zhang, S. (登録日: 2021-10-17, 公開日: 2022-03-16, 最終更新日: 2024-10-30)

主引用文献

Ji, W.,Peng, Q.,Fang, X.,Li, Z.,Li, Y.,Xu, C.,Zhao, S.,Li, J.,Chen, R.,Mo, G.,Wei, Z.,Xu, Y.,Li, B.,Zhang, S.
Structures of a deltacoronavirus spike protein bound to porcine and human receptors.
Nat Commun, 13:1467-1467, 2022

PubMed Abstract: Porcine deltacoronavirus (PDCoV) can experimentally infect a variety of animals. Human infection by PDCoV has also been reported. Consistently, PDCoV can use aminopeptidase N (APN) from different host species as receptors to enter cells. To understand this broad receptor usage and interspecies transmission of PDCoV, we determined the crystal structures of the receptor binding domain (RBD) of PDCoV spike protein bound to human APN (hAPN) and porcine APN (pAPN), respectively. The structures of the two complexes exhibit high similarity. PDCoV RBD binds to common regions on hAPN and pAPN, which are different from the sites engaged by two alphacoronaviruses: HCoV-229E and porcine respiratory coronavirus (PRCoV). Based on structure guided mutagenesis, we identified conserved residues on hAPN and pAPN that are essential for PDCoV binding and infection. We report the detailed mechanism for how a deltacoronavirus recognizes homologous receptors and provide insights into the cross-species transmission of PDCoV.

PubMed: 35304871
DOI: 10.1038/s41467-022-29062-5

実験手法

X-RAY DIFFRACTION (2.69 Å)