Medicine and Health

Evolution of the SARS-CoV-2 spike protein in the human host

A. G. Wrobel, D. J. Benton, et al.

This study by Antoni G. Wrobel and colleagues uncovers how recent SARS-CoV-2 variants, specifically the Alpha and Beta variants, have evolved through critical spike protein substitutions. Discover how enhanced ACE2 binding correlates with increased human transmissibility and the intricate structural changes that these variants showcase.

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Playback language: English

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Abstract

Recently emerged SARS-CoV-2 variants exhibit spike glycoprotein substitutions linked to increased transmission and antibody resistance. This study examines the Alpha and Beta variant spike proteins' structure and receptor binding, revealing that the N501Y substitution enhances ACE2 binding, particularly with the D614G substitution. Alpha variant spikes show increased stability upon ACE2 binding due to a more basic S1–S2 furin site, enabling near-complete cleavage. Beta variant spikes, with the K417N substitution (also in Omicron), exhibit a more open trimer conformation crucial for receptor binding. These findings suggest evolutionary adaptations for increased human transmissibility.

Publisher

Nature Communications

Published On

Mar 01, 2022

Authors

Antoni G. Wrobel, Donald J. Benton, Chloë Roustan, Annabel Borg, Saira Hussain, Stephen R. Martin, Peter B. Rosenthal, John J. Skehel, Steven J. Gamblin

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