Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function-Reference-Cited by-同舟云学术

Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function

Published:2021-08-12 Issue:9 Volume:28 Page:731-739
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Yang Tzu-Jing^ORCID,Yu Pei-Yu^ORCID,Chang Yuan-Chih^ORCID,Liang Kang-Hao,Tso Hsian-Cheng,Ho Meng-Ru,Chen Wan-Yu,Lin Hsiu-Ting,Wu Han-Chung^ORCID,Hsu Shang-Te Danny^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

https://www.nature.com/articles/s41594-021-00652-z.pdf

Reference45 articles.

1. Galloway, S. E. et al. Emergence of SARS-CoV-2 B.1.1.7 Lineage – United States, December 29, 2020–January 12, 2021. MMWR Morb. Mortal. Wkly Rep. 70, 95–99 (2021).

2. Volz, E. et al. Transmission of SARS-CoV-2 lineage B.1.1.7 in England: insights from linking epidemiological and genetic data. Preprint at https://doi.org/10.1101/2020.12.30.20249034 (2021).

3. Hoffmann, M. et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181, 271–280 e8 (2020).

4. Zhou, T. et al. Cryo-EM structures of SARS-CoV-2 spike without and with ACE2 reveal a pH-dependent switch to mediate endosomal positioning of receptor-binding domains. Cell Host Microbe 28, 867–879 e5 (2020).

5. 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).

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