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An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies
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Abstract
The emergence of the highly transmissible B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is concerning for antibody countermeasure efficacy because of the number of mutations in the spike protein. In this study, we tested a panel of anti-receptor-binding domain monoclonal antibodies (mAbs) corresponding to those in clinical use by Vir Biotechnology (S309, the parent mAb of VIR-7831 (sotrovimab)), AstraZeneca (COV2-2196 and COV2-2130, the parent mAbs of AZD8895 and AZD1061), Regeneron (REGN10933 and REGN10987), Eli Lilly (LY-CoV555 and LY-CoV016) and Celltrion (CT-P59) for their ability to neutralize an infectious B.1.1.529 Omicron isolate. Several mAbs (LY-CoV555, LY-CoV016, REGN10933, REGN10987 and CT-P59) completely lost neutralizing activity against B.1.1.529 virus in both Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells, whereas others were reduced (COV2-2196 and COV2-2130 combination, ~12-fold decrease) or minimally affected (S309). Our results suggest that several, but not all, of the antibodies in clinical use might lose efficacy against the B.1.1.529 Omicron variant. New in vitro data suggest that the new SARS-CoV-2 Omicron variant is likely to escape neutralization by most therapeutic antibodies currently available.
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Cites
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., et al. (2021) · Nature · doi:10.1038/s41586-021-03398-2 · Cited by 2,312
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006
Structural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
Self-citationSARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599
Spike mutation D614G alters SARS-CoV-2 fitness
Plante, J. A., Liu, Y., Liu, J., Xia, H., Johnson, B. A., Lokugamage, K. G., Zhang, X., Muruato, A. E., Zou, J., Fontes-Garfias, C. R., et al. (2021) · Nature · doi:10.1038/s41586-020-2895-3 · Cited by 1,558
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Wang, Z., Schmidt, F., Weisblum, Y., Muecksch, F., Barnes, C. O., Finkin, S., Schaefer-Babajew, D., Cipolla, M., Gaebler, C., Lieberman, J. A., et al. (2021) · Nature · doi:10.1038/s41586-021-03324-6 · Cited by 1,343
Baum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147
Early treatment for Covid-19 with SARS-CoV-2 neutralizing antibody sotrovimab
Gupta, A., Gonzalez-Rojas, Y., Juarez, E., Crespo Casal, M., Moya, J., Falci, D. R., Sarkis, E., Solis, J., Zheng, H., Scott, N., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2107934 · Cited by 1,086
Research works printed but not linked: 30
- Sempowski, G. D., Saunders, K. O., Acharya, P., Wiehe, K. J. & Haynes, B. F. Pandemic preparedness: developing vaccines and therapeutic antibodies for COVID-19. Cell 181, 1458–1463 (2020). · DOI
- Chen, R. E. et al. Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies. Nat. Med. 27, 717–726 (2021). · DOI · Paper page
- Chen, R. E. et al. In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains. Nature 596, 103–108 (2021). · DOI · Paper page
- Callaway, E. & Ledford, H. How bad is Omicron? What scientists know so far. Nature 600, 197–199 (2021). · DOI · Paper page
- Torjesen, I. Covid-19: Omicron may be more transmissible than other variants and partly resistant to existing vaccines, scientists fear. BMJ 375, n2943 (2021). · DOI · Paper page
- Chen, J., Wang, R., Gilby, N. B. & Wei, G. W. Omicron (B.1.1.529): infectivity, vaccine breakthrough, and antibody resistance. Preprint at https://arxiv.org/abs/2112.01318 (2021). · DOI · Paper page
- Pinto, D. et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature 583, 290–295 (2020). · DOI · Paper page
- Gottlieb, R. L. et al. Effect of bamlanivimab as monotherapy or in combination with etesevimab on viral load in patients with mild to moderate COVID-19: a randomized clinical trial. JAMA 325, 632–644 (2021). · DOI · Paper page
- Kim, C. et al. A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein. Nat. Commun. 12, 288 (2021). · DOI · Paper page
- VanBlargan, L. A. et al. A potently neutralizing SARS-CoV-2 antibody inhibits variants of concern by utilizing unique binding residues in a highly conserved epitope. Immunity 54, 2399–2416 (2021). · DOI
- Case, J. B. et al. Neutralizing antibody and soluble ACE2 inhibition of a replication-competent VSV-SARS-CoV-2 and a clinical isolate of SARS-CoV-2. Cell Host Microbe 28, 475–485 (2020). · DOI · Paper page
- Cathcart, A. L. et al. The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2. Preprint at https://www.biorxiv.org/content/10.1101/2021.03.09.434607v8 (2021). · DOI · Paper page
- 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 · Paper page
- Golcuk, M., Yildiz, A. & Gur, M. The Omicron variant increases the interactions of SARS-CoV-2 spike glycoprotein with ACE2. Preprint at https://www.biorxiv.org/content/10.1101/2021.12.06.471377v1 (2021). · doi:10.1101/2021.12.06.471377
- Lempp, F. A. et al. Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies. Nature 598, 342–347 (2021). · DOI · Paper page
- Ford, C. T., Machado, D. J. & Janies, D. A. Predictions of the SARS-CoV-2 Omicron variant (B.1.1.529) spike protein receptor-binding domain structure and neutralizing antibody interactions. Preprint at https://www.biorxiv.org/content/10.1101/2021.12.03.471024v3.full (2021). · DOI · Paper page
- Cameroni, E. et al. Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature https://doi.org/10.1038/d41586-021-03825-4 (2021). · doi:10.1038/d41586-021-03825-4 · Paper page
- Callaway, E. Omicron likely to weaken COVID vaccine protection. Nature 600, 367–368 (2021). · DOI
- Cele, S. et al. SARS-CoV-2 Omicron has extensive but incomplete escape of Pfizer BNT162b2 elicited neutralization and requires ACE2 for infection. Preprint at https://www.medrxiv.org/content/10.1101/2021.12.08.21267417v1 (2021). · DOI · Paper page
- Dejnirattisai, W. et al. Reduced neutralisation of SARS-COV-2 Omicron-B.1.1.529 variant by post-immunisation serum. Preprint at https://www.medrxiv.org/content/10.1101/2021.12.10.21267534v1 (2021). · DOI
- Kim, J. H., Marks, F. & Clemens, J. D. Looking beyond COVID-19 vaccine phase 3 trials. Nat. Med. 27, 205–211 (2021). · DOI · Paper page
- Khoury, D. S. et al. Neutralizing antibody levels are highly predictive of immune protection from symptomatic SARS-CoV-2 infection. Nat. Med. 27, 1205–1211 (2021). · DOI · Paper page
- 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 · Paper page
- Bailey, A. L. & Diamond, M. S. A Crisp(r) new perspective on SARS-CoV-2 biology. Cell 184, 15–17 (2021). · DOI
- Imai, M. et al. Syrian hamsters as a small animal model for SARS-CoV-2 infection and countermeasure development. Proc. Natl Acad. Sci. USA 117, 16587–16595 (2020). · DOI · Paper page
- Zost, S. J. et al. Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein. Nat. Med. 26, 1422–1427 (2020). · DOI · Paper page
- Jones, B. E. et al. The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates. Sci. Trans. Med. 13, eabf1906 (2021). · DOI · Paper page
- Shi, R. et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature 584, 120–124 (2020). · DOI · Paper page
- Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774–797 (2007). · DOI · Paper page
- Goddard, T. D. et al. UCSF ChimeraX: meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018). · DOI · Paper page
Cited by
SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex
Mannar, D., Saville, J. W., Zhu, X., Srivastava, S. S., Berezuk, A. M., Tuttle, K. S., Marquez, A. C., Sekirov, I., & Subramaniam, S. (2022) · Science · doi:10.1126/science.abn7760 · Cited by 630
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535
Self-citationReduced Neutralization of SARS-CoV-2 Omicron Variant by Vaccine Sera and Monoclonal Antibodies
Wilhelm, A., Widera, M., Grikscheit, K., Toptan, T., Schenk, B., Pallas, C., Metzler, M., Kohmer, N., Hoehl, S., Helfritz, F. A., et al. (2021) · doi:10.1101/2021.12.07.21267432 · Cited by 440
Virological characteristics of the SARS-CoV-2 Omicron BA.2 spike
Yamasoba, D., Kimura, I., Nasser, H., Morioka, Y., Nao, N., Ito, J., Uriu, K., Tsuda, M., Zahradnik, J., Shirakawa, K., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.035 · Cited by 380
Antibodies to combat viral infections: development strategies and progress
Pantaleo, G., Correia, B., Fenwick, C., Joo, V. S., & Perez, L. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00495-3 · Cited by 279
Metadata
- Authors
- VanBlargan, L. A., Errico, J. M., Halfmann, P. J., Zost, S. J., Crowe, J. E., Purcell, L. A., Kawaoka, Y., Corti, D., Fremont, D. H., & Diamond, M. S.
- Venue
- Nature Medicine
- Published
- 2022-01-19
- Volume
- 28
- Issue
- 3
- Pages
- 490-495
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W4226087845
- Cited by
- 705
- References
- 22
- FWCI
- 77.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (R01 AI157155, 75N93021C00014, 75N93019C00051, HHSN272201700060C)
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- VanBlargan, L. A., Errico, J. M., Halfmann, P. J., Zost, S. J., Crowe, J. E., Purcell, L. A., Kawaoka, Y., Corti, D., Fremont, D. H., & Diamond, M. S. (2022). An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies. Nature Medicine. https://doi.org/10.1038/s41591-021-01678-y
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