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
Tags
SARS-CoV-2
Alpha variant
Beta variant
spike glycoprotein
ACE2 binding
transmissibility
structural biology
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