8XSD
BA.5 Spike complex with CR9
Summary for 8XSD
Entry DOI | 10.2210/pdb8xsd/pdb |
EMDB information | 38616 |
Descriptor | Spike glycoprotein, CR9 heavy chain, CR9 light chain (3 entities in total) |
Functional Keywords | sars-cov-2, cr9, spike, viral protein, viral protein-protein binding complex, viral protein-immune system complex, viral protein/immune system |
Biological source | Severe acute respiratory syndrome coronavirus 2 More |
Total number of polymer chains | 9 |
Total formula weight | 500673.15 |
Authors | |
Primary citation | Chen, 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: 39800731DOI: 10.1038/s41392-024-02114-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.55 Å) |
Structure validation
Download full validation report
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