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7F7E

SARS-CoV-2 S protein RBD in complex with A5-10 Fab

Summary for 7F7E
Entry DOI10.2210/pdb7f7e/pdb
DescriptorHeavy chain of A5-10 Fab, Light chain of A5-10 Fab, Spike protein S1, ... (4 entities in total)
Functional Keywordsantibody, sars-cov-2, virus, viral protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight68665.65
Authors
Dou, Y.,Wang, X.,Wang, K.,Liu, P.,Lu, B. (deposition date: 2021-06-29, release date: 2022-02-02, Last modification date: 2024-10-16)
Primary citationWang, F.,Li, L.,Dou, Y.,Shi, R.,Duan, X.,Liu, H.,Zhang, J.,Liu, D.,Wu, J.,He, Y.,Lan, J.,Lu, B.,Feng, H.,Yan, J.
Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants.
Emerg Microbes Infect, 11:548-551, 2022
Cited by
PubMed Abstract: The neutralizing antibody is a potential therapeutic for the ongoing COVID-19 pandemic. As an antiviral agent, numerous mAbs recognize the epitopes that overlap with ACE2-binding sites in the SARS-CoV-2-RBD. Some studies have shown that residual changes on the spike protein can significantly decrease the efficiency of neutralizing antibodies. To address this issue, a therapeutic cocktail could be an effective countermeasure. In the present study, we isolated a fully human neutralizing antibody, JS026, from a convalescent patient. The comparative analysis revealed that JS026 binding to SARS-CoV-2-RBD mainly located between epitopes for class 2 and class 3 mAbs as opposed to that of class 1 (etesevimab) antibodies. A cocktail of etesevimab and JS026 increased neutralizing efficacy against both wild-type SARS-CoV-2 and the recent emergence of Alpha, Beta, Gamma, and Delta variants. JS026 and the cocktail reduced virus titers in the infected lungs of hACE2 transgenic mice and relieved pathological changes. These findings would benefit antibody-based therapeutic countermeasures in the treatment of COVID-19.
PubMed: 35060840
DOI: 10.1080/22221751.2022.2032374
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.49 Å)
Structure validation

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