Potent SARS-CoV-2 neutralizing antibodies selected from a human antibody library constructed decades ago
Qiang, M.; Ma, P.; Li, Y.; Liu, H.; Harding, A.; Min, C.; Liu, L.; Yuan, M.; Ji, Q.; Tao, P.; Shi, X.; Li, Z.; Wang, F.; Zhang, Y.; Wu, N. C.; Lee, C.-C. D.; Zhu, X.; Gilbert-Jaramillo, J.; Saxena, A.; Huang, X.; Wang, H.; James, W.; Dwek, R. A.; Wilson, I. A.; Yang, G.; Lerner, R. A.
Show abstract
Combinatorial antibody libraries not only effectively reduce antibody discovery to a numbers game, but enable documentation of the history of antibody responses in an individual. The SARS-CoV-2 pandemic has prompted a wider application of this technology to meet the public health challenge of pandemic threats in the modern era. Herein, we used a combinatorial human antibody library constructed 20 years before the COVID-19 pandemic to discover three highly potent antibodies that selectively bind SARS-CoV-2 spike protein and neutralize authentic SARS-CoV-2 virus. Compared to neutralizing antibodies from COVID-19 patients with generally low somatic hypermutation (SHM), these antibodies contain over 13-22 SHMs, many of which are involved in specific interactions in crystal structures with SARS-CoV-2 spike RBD. The identification of these somatically mutated antibodies in a pre-pandemic library raises intriguing questions about the origin and evolution of human immune responses to SARS-CoV-2.
Matching journals
The top 7 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Engineered ACE2-Fc counters murine lethal SARS-CoV-2 infection through direct neutralization and Fc-effector activities 98%
- Emerging SARS-CoV-2 variants of concern evade humoral immune responses from infection and vaccination 96%
- An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants 96%
Similar papers in this journal
- Potent neutralization of SARS-CoV-2 variants of concern by an antibody with a unique genetic signature and structural mode of spike recognition 97%
- Designed miniproteins potently inhibit and protect against MERS-CoV 96%
- Ultrapotent and Broad Neutralization of SARS-CoV-2 Variants by Modular, Tetravalent, Bi-paratopic Antibodies 96%
Similar papers in this journal
Similar papers in this journal
- Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder 96%
- A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyper-activation 96%
- Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies 96%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.