A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants
Open accessAbstract
As severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants continue to emerge and spread around the world, antibodies and vaccines to confer broad and potent neutralizing activity are urgently needed. Through the isolation and characterization of monoclonal antibodies (mAbs) from individuals infected with SARS-CoV-2, we identified one antibody, P36-5D2, capable of neutralizing the major SARS-CoV-2 variants of concern. Crystal and electron cryo-microscopy (cryo-EM) structure analyses revealed that P36-5D2 targeted to a conserved epitope on the receptor-binding domain of the spike protein, withstanding the three key mutations—K417N, E484K, and N501Y—found in the variants that are responsible for escape from many potent neutralizing mAbs, including some already approved for emergency use authorization (EUA). A single intraperitoneal (IP) injection of P36-5D2 as a prophylactic treatment completely protected animals from challenge of infectious SARS-CoV-2 Alpha and Beta. Treated animals manifested normal body weight and were devoid of infection-associated death up to 14 days. A substantial decrease of the infectious virus in the lungs and brain, as well as reduced lung pathology, was found in these animals compared to the controls. Thus, P36-5D2 represents a new and desirable human antibody against the current and emerging SARS-CoV-2 variants.
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P36-5D2 was initially isolated from a convalescent patient and demonstrated reasonably strong potency and breadth against Alpha, Beta, and Gamma but not Delta.
“To demonstrate the utility of our approach, we sought to optimize a human neutralizing antibody P36-5D2, which was initially isolated from a convalescent patient, and demonstrated reasonably strong potency and breadth against Alpha, Beta, and Gamma (33) but not Delta, due to Delta’s L452R but not T478K mutation through computational structure analysis.”
From Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization (2022) · cites this paper as [33]
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Rubio, A. A., Baharani, V. A., Dadonaite, B., Parada, M., Abernathy, M. E., Wang, Z., Lee, Y. E., Eso, M. R., Phung, J. L., Ramos, I., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.05.592584 · Cited by 2 · see citing works
Broadly neutralizing and protective nanobodies against diverse sarbecovirusesPreprint
Li, M., Ren, Y., Aw, Z. Q., Chen, B., Yang, Z., Lei, Y., Cheng, L., Liang, Q., Hong, J., Yang, Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.488087 · Cited by 1 · see citing works
Self-citationPrevalência e reatividade cruzada entre SARS-CoV-2 e HCoVs endêmicos
Lima, A. C. (2023) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.5.2023.tde-07122023-181214
- Authors
- Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., Yu, J., Zhang, Q., Shi, X., Zhang, T., Zhang, Z., Wang, J., Wang, X., Chu, J. J. H., & Zhang, L.
- Affiliations
- Tsinghua University (CN)
- National University of Singapore (SG)
- Center for Life Sciences (CN)
- Southern University of Science and Technology (CN)
- Capital Medical University (CN)
- Shenzhen Bay Laboratory (CN)
- Corresponding author
- Wang, Jianbin
- Wang, Xinquan
- Chu, Justin Jang Hann
- Zhang, Linqi
- ORCID
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2021-12-13
- Volume
- 12
- Pages
- 766821-766821
- ISSN
- 1664-3224 (ISSN-L)
- PMC
- PMC8710476
- OpenAlex
- W4200461445
- Cited by
- 21
- References
- 56
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 7 · 2022: 8
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Immunology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Salt Science Research Foundation (BL17U1)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, neutralizing monoclonal antibodies, spike protein receptor-binding domain, variants of concern, K417N, E484K, N501Y, antibody escape, prophylaxis, COVID-19 pandemic, antibody structure, lung pathology
- MeSH terms
- SARS-CoV-2, COVID-19 Drug Treatment, Animals, Antibodies, Monoclonal, Antibodies, Viral, Humans, Immunization, Passive, Mice, Antibodies, Neutralizing, HEK293 Cells
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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