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7YQY

SARS-CoV-2 BA.2.75 S Trimer in complex with S309 (state2)

Summary for 7YQY
Entry DOI10.2210/pdb7yqy/pdb
EMDB information34039
DescriptorSpike glycoprotein, S309 light chain, S309 heavy chain, ... (6 entities in total)
Functional Keywordssars-cov-2, ba.2.75, spike, s309, structural protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
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Total number of polymer chains9
Total formula weight550718.09
Authors
Wang, L. (deposition date: 2022-08-08, release date: 2022-10-19, Last modification date: 2024-10-09)
Primary citationCao, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.74 Å)
Structure validation

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