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8XSD

BA.5 Spike complex with CR9

Summary for 8XSD
Entry DOI10.2210/pdb8xsd/pdb
EMDB information38616
DescriptorSpike glycoprotein, CR9 heavy chain, CR9 light chain (3 entities in total)
Functional Keywordssars-cov-2, cr9, spike, viral protein, viral protein-protein binding complex, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains9
Total formula weight500673.15
Authors
Feng, L.L. (deposition date: 2024-01-09, release date: 2025-02-12)
Primary citationChen, Z.,Feng, L.,Wang, L.,Zhang, L.,Zheng, B.,Fu, H.,Li, F.,Liu, L.,Lv, Q.,Deng, R.,Xu, Y.,Hu, Y.,Zheng, J.,Qin, C.,Bao, L.,Wang, X.,Jin, Q.
A broadly neutralizing antibody against the SARS-CoV-2 Omicron sub-variants BA.1, BA.2, BA.2.12.1, BA.4, and BA.5.
Signal Transduct Target Ther, 10:14-14, 2025
Cited by
PubMed Abstract: The global spread of Severe Acute Respiratory Syndrome Coronavirus 2. (SARS-CoV-2) and its variant strains, including Alpha, Beta, Gamma, Delta, and now Omicron, pose a significant challenge. With the constant evolution of the virus, Omicron and its subtypes BA.1, BA.2, BA.3, BA.4, and BA.5 have developed the capacity to evade neutralization induced by previous vaccination or infection. This evasion highlights the urgency in discovering new monoclonal antibodies (mAbs) with neutralizing activity, especially broadly neutralizing antibodies (bnAbs), to combat the virus.In the current study, we introduced a fully human neutralizing mAb, CR9, that targets Omicron variants. We demonstrated the mAb's effectiveness in inhibiting Omicron replication both in vitro and in vivo. Structural analysis using cryo-electron microscopy (cryo-EM) revealed that CR9 binds to an epitope formed by RBD residues, providing a molecular understanding of its neutralization mechanism. Given its potency and specificity, CR9 holds promise as a potential adjunct therapy for treating Omicron infections. Our findings highlight the importance of continuous mAb discovery and characterization in addressing the evolving threat of COVID-19.
PubMed: 39800731
DOI: 10.1038/s41392-024-02114-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.55 Å)
Structure validation

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