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8I9E

S-RBD(Omicron BA.3) in complex with PD of ACE2

Summary for 8I9E
Entry DOI10.2210/pdb8i9e/pdb
EMDB information35268
DescriptorProcessed angiotensin-converting enzyme 2, Spike protein S1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordssars-cov-2, viral protein, hydrolase-viral protein complex, hydrolase/viral protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight99229.52
Authors
Li, Y.N.,Shen, Y.P.,Zhang, Y.Y.,Yan, R.H. (deposition date: 2023-02-06, release date: 2024-02-07, Last modification date: 2024-10-23)
Primary citationLi, Y.,Shen, Y.,Zhang, Y.,Yan, R.
Structural Basis for the Enhanced Infectivity and Immune Evasion of Omicron Subvariants.
Viruses, 15:-, 2023
Cited by
PubMed Abstract: The Omicron variants of SARS-CoV-2 have emerged as the dominant strains worldwide, causing the COVID-19 pandemic. Each Omicron subvariant contains at least 30 mutations on the spike protein (S protein) compared to the original wild-type (WT) strain. Here we report the cryo-EM structures of the trimeric S proteins from the BA.1, BA.2, BA.3, and BA.4/BA.5 subvariants, with BA.4 and BA.5 sharing the same S protein mutations, each in complex with the surface receptor ACE2. All three receptor-binding domains of the S protein from BA.2 and BA.4/BA.5 are "up", while the BA.1 S protein has two "up" and one "down". The BA.3 S protein displays increased heterogeneity, with the majority in the all "up" RBD state. The different conformations preferences of the S protein are consistent with their varied transmissibility. By analyzing the position of the glycan modification on Asn343, which is located at the S309 epitopes, we have uncovered the underlying immune evasion mechanism of the Omicron subvariants. Our findings provide a molecular basis of high infectivity and immune evasion of Omicron subvariants, thereby offering insights into potential therapeutic interventions against SARS-CoV-2 variants.
PubMed: 37376697
DOI: 10.3390/v15061398
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

227111

数据于2024-11-06公开中

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