Structure-based evidence for the enhanced transmissibility of the dominant SARS-CoV-2 B.1.1.7 variant (Alpha)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry
Link
https://www.nature.com/articles/s41421-021-00349-z.pdf
Reference14 articles.
1. Hoffmann, M. et al. SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies. Cell 184, 2384–2393 (2021).
2. Washington, N. L. et al. Emergence and rapid transmission of SARS-CoV-2 B.1.1.7 in the United States. Cell 184, 2587–2594.e7 (2021).
3. Zhu, X. et al. Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies. PLoS Biol. 19, e3001237 (2021).
4. Socher, E. et al. Mutations in the B.1.1.7 SARS-CoV-2 spike protein reduce receptor-binding affinity and induce a flexible link to the fusion peptide. Biomedicines 9, 525 (2021).
5. Niu, Z. et al. N501Y mutation imparts cross-species transmission of SARS-CoV-2 to mice by enhancing receptor binding. Signal Transduct. Target. Ther. 6, 284 (2021).
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