8XM5

Cryo-EM structure of SARS-CoV-2 Omicron EG.5 spike protein(6P), RBD-closed state

8XM5 の概要

• エントリーDOI: 10.2210/pdb8xm5/pdb
• EMDBエントリー: 38463
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: sars-cov-2, omicron, eg.5, spike protein, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 429172.87

構造登録者

Li, L.J.,Gu, Y.H.,Shi, K.Y.,Qi, J.X.,Gao, G.F. (登録日: 2023-12-27, 公開日: 2024-07-03, 最終更新日: 2024-10-23)

主引用文献

Li, L.,Shi, K.,Gu, Y.,Xu, Z.,Shu, C.,Li, D.,Sun, J.,Cong, M.,Li, X.,Zhao, X.,Yu, G.,Hu, S.,Tan, H.,Qi, J.,Ma, X.,Liu, K.,Gao, G.F.
Spike structures, receptor binding, and immune escape of recently circulating SARS-CoV-2 Omicron BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 sub-variants.
Structure, 32:1055-1067.e6, 2024

PubMed Abstract: The recently emerged BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 variants have a growth advantage. In this study, we explore the structural bases of receptor binding and immune evasion for the Omicron BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 sub-variants. Our findings reveal that BA.2.86 exhibits strong receptor binding, whereas its JN.1 sub-lineage displays a decreased binding affinity to human ACE2 (hACE2). Through complex structure analyses, we observed that the reversion of R493Q in BA.2.86 receptor binding domain (RBD) plays a facilitating role in receptor binding, while the L455S substitution in JN.1 RBD restores optimal affinity. Furthermore, the structure of monoclonal antibody (mAb) S309 complexed with BA.2.86 RBD highlights the importance of the K356T mutation, which brings a new N-glycosylation motif, altering the binding pattern of mAbs belonging to RBD-5 represented by S309. These findings emphasize the importance of closely monitoring BA.2.86 and its sub-lineages to prevent another wave of SARS-CoV-2 infections.

PubMed: 39013463
DOI: 10.1016/j.str.2024.06.012

実験手法

ELECTRON MICROSCOPY (2.61 Å)