Journal
IMMUNITY
Volume 54, Issue 7, Pages 1611-+Publisher
CELL PRESS
DOI: 10.1016/j.immuni.2021.06.003
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Funding
- National Key Plan for Scientific Research and Development of China [2020YFC0848800, 2020YFC0849900]
- National Natural Science Foundation [81530065, 91442127, 32000661]
- Beijing Municipal Science and Technology Commission [D171100000517, Z201100005420019]
- Science and Technology Innovation Committee of Shenzhen Municipality [202002073000002]
- COVID-19 Science and Technology Project of Beijing Hospitals Authority [YGZX-C1]
- Beijing Advanced Innovation Center for Structural Biology
- Tsinghua University Scientific Research Program [20201080053, 2020Z99CFG004]
- Tencent Foundation
- Shuidi Foundation
- National Science Fund for Distinguished Young Scholars [82025022]
- China Postdoctoral Science Foundation [2020T130062ZX]
- TH Capital
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Research shows that the South African B.1.351 variant exhibits the highest resistance to current monoclonal antibodies and convalescent plasma from COVID-19-infected individuals, and the molecular basis for this resistance and potential antibody escape has been identified.
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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