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7WS4

Ultrapotent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational variants

Summary for 7WS4
Entry DOI10.2210/pdb7ws4/pdb
EMDB information32743
DescriptorSpike glycoprotein, 510A5 light chain, 510A5 heavy chain, ... (5 entities in total)
Functional Keywordscovid-19, spike glycoprotein, virus, viral protein, antibody, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2
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Total number of polymer chains5
Total formula weight435240.75
Authors
Guo, H.,Gao, Y.,Ji, X.,Yang, H. (deposition date: 2022-01-28, release date: 2022-06-01)
Primary citationGuo, H.,Gao, Y.,Li, T.,Li, T.,Lu, Y.,Zheng, L.,Liu, Y.,Yang, T.,Luo, F.,Song, S.,Wang, W.,Yang, X.,Nguyen, H.C.,Zhang, H.,Huang, A.,Jin, A.,Yang, H.,Rao, Z.,Ji, X.
Structures of Omicron spike complexes and implications for neutralizing antibody development.
Cell Rep, 39:110770-110770, 2022
Cited by
PubMed Abstract: The emergence of the SARS-CoV-2 Omicron variant is dominant in many countries worldwide. The high number of spike mutations is responsible for the broad immune evasion from existing vaccines and antibody drugs. To understand this, we first present the cryo-electron microscopy structure of ACE2-bound SARS-CoV-2 Omicron spike. Comparison to previous spike antibody structures explains how Omicron escapes these therapeutics. Secondly, we report structures of Omicron, Delta, and wild-type spikes bound to a patient-derived Fab antibody fragment (510A5), which provides direct evidence where antibody binding is greatly attenuated by the Omicron mutations, freeing spike to bind ACE2. Together with biochemical binding and 510A5 neutralization assays, our work establishes principles of binding required for neutralization and clearly illustrates how the mutations lead to antibody evasion yet retain strong ACE2 interactions. Structural information on spike with both bound and unbound antibodies collectively elucidates potential strategies for generation of therapeutic antibodies.
PubMed: 35477022
DOI: 10.1016/j.celrep.2022.110770
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

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