9JMO

Cryo-EM structure of Japan-BatCoV (Vs-CoV-1) S-trimer

9JMO の概要

• エントリーDOI: 10.2210/pdb9jmo/pdb
• EMDBエントリー: 61608
• 分子名称: Spike glycoprotein,Fibritin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: spike protein, viral protein
• 由来する生物種: Bat coronavirus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 471293.62

構造登録者

Yuan, H.,Xiong, X. (登録日: 2024-09-20, 公開日: 2025-06-18, 最終更新日: 2025-07-23)

主引用文献

Yuan, H.,Wang, J.,Ma, Y.,Li, Z.,Gao, X.,Habib, G.,Liu, B.,Chen, J.,He, J.,Zhou, P.,Shi, Z.L.,Chen, X.,Xiong, X.
Structures and receptor binding activities of merbecovirus spike proteins reveal key signatures for human DPP4 adaptation.
Sci Adv, 11:eadv7296-eadv7296, 2025

PubMed Abstract: Merbecoviruses from bats, pangolins, and hedgehogs pose significant zoonotic threats, with a limited understanding of receptor binding by their spike (S) proteins. Here, we report cryo-EM structures of GD-BatCoV (BtCoV-422) and SE-PangolinCoV (MjHKU4r-CoV-1) RBDs in complex with human DPP4 (hDPP4). These structures exhibit a substantial offset in their hDPP4 interaction interfaces, revealing a conserved hydrophobic cluster as a convergent signature of DPP4 binding within the MERS-HKU4 clade of merbecoviruses. Structure-guided mutagenesis demonstrates that favorable interactions are distributed across multiple receptor binding motif (RBM) regions, working synergistically to confer high-affinity hDPP4 binding. Swapping of the merbecovirus RBM regions indicate limited plasticity and interchangeability among these regions. In addition, we report cryo-EM structures of six merbecovirus S-trimers. Structure-based phylogenetics suggests that hDPP4-binding merbecoviruses undergo convergent evolution, while ACE2-binding merbecoviruses exhibit diversification in their binding mechanisms. These findings offer critical insights into merbecovirus receptor utilization, providing a structural understanding for future surveillance.

PubMed: 40644548
DOI: 10.1126/sciadv.adv7296

実験手法

ELECTRON MICROSCOPY (2.8 Å)