7YQU

SARS-CoV-2 BA.2.75 S Trimer (3 RBD Down)

7YQU の概要

• エントリーDOI: 10.2210/pdb7yqu/pdb
• EMDBエントリー: 34035
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 433892.30

構造登録者

Wang, L. (登録日: 2022-08-08, 公開日: 2022-10-19, 最終更新日: 2024-11-20)

主引用文献

Cao, Y.,Song, W.,Wang, L.,Liu, P.,Yue, C.,Jian, F.,Yu, Y.,Yisimayi, A.,Wang, P.,Wang, Y.,Zhu, Q.,Deng, J.,Fu, W.,Yu, L.,Zhang, N.,Wang, J.,Xiao, T.,An, R.,Wang, J.,Liu, L.,Yang, S.,Niu, X.,Gu, Q.,Shao, F.,Hao, X.,Meng, B.,Gupta, R.K.,Jin, R.,Wang, Y.,Xie, X.S.,Wang, X.
Characterization of the enhanced infectivity and antibody evasion of Omicron BA.2.75.
Cell Host Microbe, 30:1527-, 2022

PubMed Abstract: Recently emerged SARS-CoV-2 Omicron subvariant, BA.2.75, displayed a growth advantage over circulating BA.2.38, BA.2.76, and BA.5 in India. However, the underlying mechanisms for enhanced infectivity, especially compared with BA.5, remain unclear. Here, we show that BA.2.75 exhibits substantially higher affinity for host receptor angiotensin-converting enzyme 2 (ACE2) than BA.5 and other variants. Structural analyses of BA.2.75 spike shows its decreased thermostability and increased frequency of the receptor binding domain (RBD) in the "up" conformation under acidic conditions, suggesting enhanced low-pH-endosomal cell entry. Relative to BA.4/BA.5, BA.2.75 exhibits reduced evasion of humoral immunity from BA.1/BA.2 breakthrough-infection convalescent plasma but greater evasion of Delta breakthrough-infection convalescent plasma. BA.5 breakthrough-infection plasma also exhibits weaker neutralization against BA.2.75 than BA.5, mainly due to BA.2.75's distinct neutralizing antibody (NAb) escape pattern. Antibody therapeutics Evusheld and Bebtelovimab remain effective against BA.2.75. These results suggest BA.2.75 may prevail after BA.4/BA.5, and its increased receptor-binding capability could support further immune-evasive mutations.

PubMed: 36270286
DOI: 10.1016/j.chom.2022.09.018

実験手法

ELECTRON MICROSCOPY (3.19 Å)