6B7N

Cryo-electron microscopy structure of porcine delta coronavirus spike protein in the pre-fusion state

6B7N の概要

• エントリーDOI: 10.2210/pdb6b7n/pdb
• EMDBエントリー: 7063
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: Spike protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: delta coronavirus, spike, pre-fusion, cryo-em, viral protein
• 由来する生物種: Deltacoronavirus PDCoV/USA/Ohio137/2014
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 379116.38

構造登録者

Shang, J.,Zheng, Y.,Yang, Y.,Liu, C.,Geng, Q.,Tai, W.,Du, L.,Zhou, Y.,Zhang, W.,Li, F. (登録日: 2017-10-04, 公開日: 2017-10-25, 最終更新日: 2024-10-30)

主引用文献

Shang, J.,Zheng, Y.,Yang, Y.,Liu, C.,Geng, Q.,Tai, W.,Du, L.,Zhou, Y.,Zhang, W.,Li, F.
Cryo-Electron Microscopy Structure of Porcine Deltacoronavirus Spike Protein in the Prefusion State
J. Virol., 92:-, 2018

PubMed Abstract: Coronavirus spike proteins from different genera are divergent, although they all mediate coronavirus entry into cells by binding to host receptors and fusing viral and cell membranes. Here, we determined the cryo-electron microscopy structure of porcine deltacoronavirus (PdCoV) spike protein at 3.3-Å resolution. The trimeric protein contains three receptor-binding S1 subunits that tightly pack into a crown-like structure and three membrane fusion S2 subunits that form a stalk. Each S1 subunit contains two domains, an N-terminal domain (S1-NTD) and C-terminal domain (S1-CTD). PdCoV S1-NTD has the same structural fold as alpha- and betacoronavirus S1-NTDs as well as host galectins, and it recognizes sugar as its potential receptor. PdCoV S1-CTD has the same structural fold as alphacoronavirus S1-CTDs, but its structure differs from that of betacoronavirus S1-CTDs. PdCoV S1-CTD binds to an unidentified receptor on host cell surfaces. PdCoV S2 is locked in the prefusion conformation by structural restraint of S1 from a different monomeric subunit. PdCoV spike possesses several structural features that may facilitate immune evasion by the virus, such as its compact structure, concealed receptor-binding sites, and shielded critical epitopes. Overall, this study reveals that deltacoronavirus spikes are structurally and evolutionally more closely related to alphacoronavirus spikes than to betacoronavirus spikes; it also has implications for the receptor recognition, membrane fusion, and immune evasion by deltacoronaviruses as well as coronaviruses in general. IMPORTANCE In this study, we determined the cryo-electron microscopy structure of porcine deltacoronavirus (PdCoV) spike protein at a 3.3-Å resolution. This is the first atomic structure of a spike protein from the deltacoronavirus genus, which is divergent in amino acid sequences from the well-studied alpha- and betacoronavirus spike proteins. Here, we described the overall structure of the PdCoV spike and the detailed structure of each of its structural elements. Moreover, we analyzed the functions of each of the structural elements. Based on the structures and functions of these structural elements, we discussed the evolution of PdCoV spike protein in relation to the spike proteins from other coronavirus genera. This study combines the structure, function, and evolution of PdCoV spike protein and provides many insights into its receptor recognition, membrane fusion, and immune evasion.

PubMed: 29070693
DOI: 10.1128/JVI.01556-17

実験手法

ELECTRON MICROSCOPY (3.3 Å)