Efficient discovery of SARS-CoV-2-neutralizing antibodies via B cell receptor sequencing and ligand blocking.
Journal
Nature biotechnology
ISSN: 1546-1696
Titre abrégé: Nat Biotechnol
Pays: United States
ID NLM: 9604648
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
received:
02
06
2021
accepted:
24
01
2022
pubmed:
5
3
2022
medline:
16
8
2022
entrez:
4
3
2022
Statut:
ppublish
Résumé
Although several monoclonal antibodies (mAbs) targeting severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have been approved for coronavirus disease 2019 (COVID-19) therapy, development was generally inefficient, with lead generation often requiring the production and testing of numerous antibody candidates. Here, we report that the integration of target-ligand blocking with a previously described B cell receptor-sequencing approach (linking B cell receptor to antigen specificity through sequencing (LIBRA-seq)) enables the rapid and efficient identification of multiple neutralizing mAbs that prevent the binding of SARS-CoV-2 spike (S) protein to angiotensin-converting enzyme 2 (ACE2). The combination of target-ligand blocking and high-throughput antibody sequencing promises to increase the throughput of programs aimed at discovering new neutralizing antibodies.
Identifiants
pubmed: 35241839
doi: 10.1038/s41587-022-01232-2
pii: 10.1038/s41587-022-01232-2
pmc: PMC9378442
mid: NIHMS1778607
doi:
Substances chimiques
Antibodies, Neutralizing
0
Antibodies, Viral
0
Ligands
0
Receptors, Antigen, B-Cell
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Peptidyl-Dipeptidase A
EC 3.4.15.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1270-1275Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM008320
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI152693
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI157155
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK058404
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI131722
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY008126
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA068485
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI127521
Pays : United States
Organisme : NCRR NIH HHS
ID : UL1 RR024975
Pays : United States
Organisme : NCATS NIH HHS
ID : UL1 TR002243
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI142785
Pays : United States
Organisme : NIAID NIH HHS
ID : 75N93019C00074
Pays : United States
Organisme : NIAID NIH HHS
ID : T32 AI007392
Pays : United States
Organisme : NCRR NIH HHS
ID : G20 RR030956
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI142790
Pays : United States
Commentaires et corrections
Type : UpdateOf
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Nature America, Inc.
Références
Jiang, S., Hillyer, C. & Du, L. Neutralizing antibodies against SARS-CoV-2 and other human coronaviruses. Trends Immunol. 41, 355–359 (2020).
doi: 10.1016/j.it.2020.03.007
Zost, S. J. et al. Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature 584, 443–449 (2020).
doi: 10.1038/s41586-020-2548-6
Chi, X. et al. A neutralizing human antibody binds to the N-terminal domain of the spike protein of SARS-CoV-2. Science 369, 650–655 (2020).
doi: 10.1126/science.abc6952
Brouwer, P. J. M. et al. Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability. Science 369, 643–650 (2020).
doi: 10.1126/science.abc5902
Rogers, T. F. et al. Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model. Science 369, 956–963 (2020).
doi: 10.1126/science.abc7520
Hansen, J. et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail. Science 369, 1010–1014 (2020).
doi: 10.1126/science.abd0827
Krammer, F. SARS-CoV-2 vaccines in development. Nature 586, 516–527 (2020).
doi: 10.1038/s41586-020-2798-3
Wec, A. Z. et al. Broad neutralization of SARS-related viruses by human monoclonal antibodies. Science 369, 731–736 (2020).
doi: 10.1126/science.abc7424
Cohen, M. S. Monoclonal antibodies to disrupt progression of early Covid-19 infection. N. Engl. J. Med. 384, 289–291 (2021).
doi: 10.1056/NEJMe2034495
Ju, B. et al. Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature 584, 115–119 (2020).
doi: 10.1038/s41586-020-2380-z
Robbiani, D. F. et al. Convergent antibody responses to SARS-CoV-2 in convalescent individuals. Nature 584, 437–442 (2020).
doi: 10.1038/s41586-020-2456-9
Shi, R. et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature 584, 120–124 (2020).
doi: 10.1038/s41586-020-2381-y
Setliff, I. et al. High-throughput mapping of B cell receptor sequences to antigen specificity. Cell 179, 1636–1646 (2019).
doi: 10.1016/j.cell.2019.11.003
Alamyar, E., Duroux, P., Lefranc, M. P. & Giudicelli, V. IMGT tools for the nucleotide analysis of immunoglobulin (IG) and T cell receptor (TR) V-(D)-J repertoires, polymorphisms, and IG mutations: IMGT/V-QUEST and IMGT/HighV-QUEST for NGS. Methods Mol. Biol. 882, 569–604 (2012).
doi: 10.1007/978-1-61779-842-9_32
Gupta, N. T. et al. Change-O: a toolkit for analyzing large-scale B cell immunoglobulin repertoire sequencing data. Bioinformatics 31, 3356–3358 (2015).
doi: 10.1093/bioinformatics/btv359
Gilchuk, P. et al. Integrated pipeline for the accelerated discovery of antiviral antibody therapeutics. Nat. Biomed. Eng. 4, 1030–1043 (2020).
doi: 10.1038/s41551-020-0594-x
Suryadevara, N. et al. Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. Cell 184, 2316–2331 (2021).
doi: 10.1016/j.cell.2021.03.029
Hsieh, C. L. et al. Structure-based design of prefusion-stabilized SARS-CoV-2 spikes. Science 369, 1501–1505 (2020).
doi: 10.1126/science.abd0826
Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
doi: 10.1016/j.jsb.2005.07.007
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
doi: 10.1038/nmeth.4169