Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice.
Angiotensin-Converting Enzyme 2
/ antagonists & inhibitors
Animals
Antibodies, Bispecific
/ immunology
Antibodies, Monoclonal
/ immunology
Antibodies, Neutralizing
/ immunology
Body Weight
COVID-19
/ immunology
Dependovirus
/ genetics
Disease Models, Animal
Epitopes, B-Lymphocyte
/ chemistry
Female
Humans
Immune Evasion
/ genetics
Immunoglobulin G
/ immunology
Mice
Mice, Inbred C57BL
SARS-CoV-2
/ genetics
Spike Glycoprotein, Coronavirus
/ antagonists & inhibitors
COVID-19 Drug Treatment
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
received:
07
01
2021
accepted:
16
03
2021
pubmed:
27
3
2021
medline:
22
5
2021
entrez:
26
3
2021
Statut:
ppublish
Résumé
Neutralizing antibodies that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein are among the most promising approaches against COVID-19
Identifiants
pubmed: 33767445
doi: 10.1038/s41586-021-03461-y
pii: 10.1038/s41586-021-03461-y
doi:
Substances chimiques
Antibodies, Bispecific
0
Antibodies, Monoclonal
0
Antibodies, Neutralizing
0
Epitopes, B-Lymphocyte
0
Immunoglobulin G
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
ACE2 protein, human
EC 3.4.17.23
Angiotensin-Converting Enzyme 2
EC 3.4.17.23
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
424-428Subventions
Organisme : NIAID NIH HHS
ID : U01 AI151698
Pays : United States
Organisme : NIH HHS
ID : P01-AI138398-S1
Pays : United States
Organisme : NIH HHS
ID : 2U19AI111825
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NIAID NIH HHS
ID : P50 AI150464
Pays : United States
Organisme : NIAID NIH HHS
ID : R37 AI064003
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI078788
Pays : United States
Commentaires et corrections
Type : ErratumIn
Références
DeFrancesco, L. COVID-19 antibodies on trial. Nat. Biotechnol. 38, 1242–1252 (2020).
doi: 10.1038/s41587-020-0732-8
pubmed: 33087898
Klasse, P. J. & Moore, J. P. Antibodies to SARS-CoV-2 and their potential for therapeutic passive immunization. eLife 9, e57877 (2020).
doi: 10.7554/eLife.57877
pubmed: 32573433
pmcid: 7311167
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
pubmed: 32555388
pmcid: 7442695
Ecker, D. M. & Seymour, P. in CPhI Annual Report 2020: Postulating the Post-COVID Pharma Paradigm, 43–49 (Informamarkets, 2020).
Baum, A. et al. REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters. Science 370, 1110–1115 (2020).
doi: 10.1126/science.abe2402
pubmed: 33037066
pmcid: 7857396
Schäfer, A. et al. Antibody potency, effector function, and combinations in protection and therapy for SARS-CoV-2 infection in vivo. J. Exp. Med. 218, e20201993 (2021).
doi: 10.1084/jem.20201993
pubmed: 33211088
Schlake, T. et al. mRNA: a novel avenue to antibody therapy? Mol. Ther. 27, 773–784 (2019).
doi: 10.1016/j.ymthe.2019.03.002
pubmed: 30885573
pmcid: 6453519
Tiwari, P. M. et al. Engineered mRNA-expressed antibodies prevent respiratory syncytial virus infection. Nat. Commun. 9, 3999 (2018).
doi: 10.1038/s41467-018-06508-3
pubmed: 30275522
pmcid: 6167369
Barnes, C. O. et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020).
doi: 10.1038/s41586-020-2852-1
pubmed: 33045718
pmcid: 8092461
Schaefer, W. et al. Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies. Proc. Natl Acad. Sci. USA 108, 11187–11192 (2011).
doi: 10.1073/pnas.1019002108
pubmed: 21690412
pmcid: 3131342
Walls, A. C. et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181, 281–292.e6 (2020).
doi: 10.1016/j.cell.2020.02.058
pubmed: 32155444
pmcid: 7102599
Kemp, S. et al. Recurrent emergence and transmission of a SARS-CoV-2 spike deletion ΔH69/V70. Preprint at https://doi.org/10.1101/2020.12.14.422555 (2020).
Tegally, H. et al. Emergence and rapid spread of a new severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) lineage with multiple spike mutations in South Africa. Preprint at https://doi.org/10.1101/2020.12.21.20248640 (2020).
Weisblum, Y. et al. Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants. eLife 9, e61312 (2020).
doi: 10.7554/eLife.61312
pubmed: 33112236
pmcid: 7723407
Schmidt, F. et al. Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses. J. Exp. Med. 217, e20201181 (2020).
doi: 10.1084/jem.20201181
pubmed: 32692348
pmcid: 7372514
Benton, D. J. et al. The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2. Proc. Natl Acad. Sci. USA 118, e2022586118 (2021).
doi: 10.1073/pnas.2022586118
pubmed: 33579792
pmcid: 7936381
Han, K. et al. Lung expression of human ACE2 sensitizes the mouse to SARS-CoV-2 infection. Am. J. Respir. Cell Mol. Biol. 64, 79–88 (2021).
doi: 10.1165/rcmb.2020-0354OC
pubmed: 32991819
pmcid: 7781002
Hassan, A. O. et al. A SARS-CoV-2 infection model in mice demonstrates protection by neutralizing antibodies. Cell 182, 744–753.e4 (2020).
doi: 10.1016/j.cell.2020.06.011
pubmed: 32553273
pmcid: 7284254
Sun, J. et al. Generation of a broadly useful model for COVID-19 pathogenesis, vaccination, and treatment. Cell 182, 734–743.e5 (2020).
doi: 10.1016/j.cell.2020.06.010
pubmed: 32643603
pmcid: 7284240
Sun, S. H. et al. A mouse model of SARS-CoV-2 infection and pathogenesis. Cell Host Microbe 28, 124–133.e4 (2020).
doi: 10.1016/j.chom.2020.05.020
pubmed: 32485164
pmcid: 7250783
Deshmukh, V., Motwani, R., Kumar, A., Kumari, C. & Raza, K. Histopathological observations in COVID-19: a systematic review. J. Clin. Pathol. 74, 76–83 (2021).
doi: 10.1136/jclinpath-2020-206995
pubmed: 32817204
Greaney, A. J. et al. Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies. Cell Host Microbe 29, 463–476 (2021).
doi: 10.1016/j.chom.2021.02.003
pubmed: 33592168
pmcid: 7869748
Chen, J., Wang, R., Wang, M. & Wei, G. W. Mutations strengthened SARS-CoV-2 infectivity. J. Mol. Biol. 432, 5212–5226 (2020).
doi: 10.1016/j.jmb.2020.07.009
pubmed: 32710986
pmcid: 7375973
Sabino, E. C. et al. Resurgence of COVID-19 in Manaus, Brazil, despite high seroprevalence. Lancet 397, 452–455 (2021).
doi: 10.1016/S0140-6736(21)00183-5
pubmed: 33515491
pmcid: 7906746
Dong, J. et al. Development of humanized tri-specific nanobodies with potent neutralization for SARS-CoV-2. Sci. Rep. 10, 17806 (2020).
doi: 10.1038/s41598-020-74761-y
pubmed: 33082473
pmcid: 7576208
Saunders, K. O. Conceptual approaches to modulating antibody effector functions and circulation half-life. Front. Immunol. 10, 1296 (2019).
doi: 10.3389/fimmu.2019.01296
pubmed: 31231397
pmcid: 6568213
Dejnirattisai, W. et al. Cross-reacting antibodies enhance dengue virus infection in humans. Science 328, 745–748 (2010).
doi: 10.1126/science.1185181
pubmed: 20448183
Yip, M. S. et al. Antibody-dependent infection of human macrophages by severe acute respiratory syndrome coronavirus. Virol. J. 11, 82 (2014).
doi: 10.1186/1743-422X-11-82
pubmed: 24885320
pmcid: 4018502
Yip, M. S. et al. Antibody-dependent enhancement of SARS coronavirus infection and its role in the pathogenesis of SARS. Hong Kong Med. J. 22 (Suppl 4), 25–31 (2016).
pubmed: 27390007
Klein, C. et al. Engineering therapeutic bispecific antibodies using CrossMab technology. Methods 154, 21–31 (2019).
doi: 10.1016/j.ymeth.2018.11.008
pubmed: 30453028
Bardelli, M. et al. A bispecific immunotweezer prevents soluble PrP oligomers and abolishes prion toxicity. PLoS Pathog. 14, e1007335 (2018).
doi: 10.1371/journal.ppat.1007335
pubmed: 30273408
pmcid: 6181439
Fu, B. et al. ALMOST: an all atom molecular simulation toolkit for protein structure determination. J. Comput. Chem. 35, 1101–1105 (2014).
doi: 10.1002/jcc.23588
pubmed: 24676684
Yang, J. et al. The I-TASSER suite: protein structure and function prediction. Nat. Methods 12, 7–8 (2015).
doi: 10.1038/nmeth.3213
pubmed: 25549265
pmcid: 4428668
Schrodinger. The PyMOL Molecular Graphics System, Version 1.8 (Schrodinger 2015).
Van Der Spoel, D. et al. GROMACS: fast, flexible, and free. J. Comput. Chem. 26, 1701–1718 (2005).
doi: 10.1002/jcc.20291
Wang, Z. et al. mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants. Nature (2021).
Percivalle, E. et al. West Nile or Usutu virus? A three-year follow-up of humoral and cellular response in a group of asymptomatic blood donors. Viruses 12, 157 (2020).
doi: 10.3390/v12020157
pmcid: 7077259
Zolotukhin, S. et al. Recombinant adeno-associated virus purification using novel methods improves infectious titer and yield. Gene Ther. 6, 973–985 (1999).
doi: 10.1038/sj.gt.3300938
pubmed: 10455399
Aurnhammer, C. et al. Universal real-time PCR for the detection and quantification of adeno-associated virus serotype 2-derived inverted terminal repeat sequences. Hum. Gene Ther. Methods 23, 18–28 (2012).
doi: 10.1089/hgtb.2011.034
pubmed: 22428977
De Madrid, A. T. & Porterfield, J. S. A simple micro-culture method for the study of group B arboviruses. Bull. World Health Organ. 40, 113–121 (1969).
pubmed: 4183812
pmcid: 2554446