Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species
Open accessAbstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants continue to emerge during the global pandemic and may facilitate escape from current antibody therapies and vaccine protection. Here we showed that the South African variant B.1.351 was the most resistant to current monoclonal antibodies and convalescent plasma from coronavirus disease 2019 (COVID-19)-infected individuals, followed by the Brazilian variant P.1 and the United Kingdom variant B.1.1.7. This resistance hierarchy corresponded with Y144del and 242-244del mutations in the N-terminal domain and K417N/T, E484K, and N501Y mutations in the receptor-binding domain (RBD) of SARS-CoV-2. Crystal structure analysis of the B.1.351 triple mutant (417N-484K-501Y) RBD complexed with the monoclonal antibody P2C-1F11 revealed the molecular basis for antibody neutralization and escape. B.1.351 and P.1 also acquired the ability to use mouse and mink ACE2 receptors for entry. Our results demonstrate major antigenic shifts and potential broadening of the host range for B.1.351 and P.1 variants, which poses serious challenges to current antibody therapies and vaccine protection.
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Reduced sensitivity of SARS-CoV-2 variants to antibody and serum neutralization has been widely observed.
“However, reduced sensitivity of SARS-CoV-2 variants to antibody and serum neutralization has been widely observed (18–21).”
From Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization (2022) · cites this paper as [20]
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References 74 · Cited by 240
- Authors
- Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Chen, P., Liao, H., Feng, Y., Li, X., Shi, X., Zhang, Z., Zhang, F., Ding, Q., Zhang, T., Wang, X., & Zhang, L.
- Affiliations
- Center for Life Sciences (CN)
- Tsinghua University (CN)
- Southern University of Science and Technology (CN)
- Capital Medical University (CN)
- Shenzhen Bay Laboratory (CN)
- Corresponding author
- Zhang, Tong
- Wang, Xinquan
- Zhang, Linqi
- ORCID
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2021-07
- Volume
- 54
- Issue
- 7
- Pages
- 1611-1621.e5
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC8185182
- OpenAlex
- W3170598451
- Cited by
- 240
- References
- 74
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 27 · 2023: 41 · 2022: 118 · 2021: 34
- FWCI
- 17.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 377 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Immunity (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Beijing Advanced Innovation Center for Structural Biology
- Beijing Hospitals Authority
- National Natural Science Foundation of China
- Ministry of Science and Technology of the People's Republic of China
- China Postdoctoral Science Foundation
- Beijing Municipal Science and Technology Commission
- Shenzhen Science and Technology Innovation Committee
- National Science Fund for Distinguished Young Scholars
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2 variants, Beta variant, P.1 variant, B.1.1.7 variant, receptor-binding domain mutations, E484K, N501Y, K417N, ACE2 receptor, antigenic shift, host range expansion, vaccine protection, convalescent plasma
- MeSH terms
- Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Antibodies, Monoclonal, Antigenic Variation, Humans, Mink, Mutation, Protein Binding, Mice, Virus Internalization, Immune Evasion, Antibodies, Neutralizing, Host Specificity, Spike Glycoprotein, Coronavirus
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