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Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
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Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
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Journal Article
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
2022
Overview
The omicron variant of SARS-CoV-2 has been spreading rapidly across the globe. The virus-surface spike protein plays a critical role in the cell entry and immune evasion of SARS-CoV-2. Here we determined the 3.0 Å cryo-EM structure of the omicron spike protein ectodomain. In contrast to the original strain of SARS-CoV-2 where the receptor-binding domain (RBD) of the spike protein takes a mixture of open (“standing up”) and closed (“lying down”) conformations, the omicron spike molecules are predominantly in the open conformation, with one upright RBD ready for receptor binding. The open conformation of the omicron spike is stabilized by enhanced inter-domain and inter-subunit packing, which involves new mutations in the omicron strain. Moreover, the omicron spike has undergone extensive mutations in RBD regions where known neutralizing antibodies target, allowing the omicron variant to escape immune surveillance aimed at the original viral strain. The stable open conformation of the omicron spike sheds light on the cell entry and immune evasion mechanisms of the omicron variant.
This study determined the structure of the spike protein of the SARS-CoV-2 omicron variant, revealing a predominantly open conformation of the molecule that may help omicron infect cells more efficiently than do previous variants.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Antibodies, Neutralizing - immunology
/ Antibodies, Viral - immunology
/ Binding
/ COVID-19
/ Humanities and Social Sciences
/ Humans
/ Mutation
/ Protein Domains - immunology
/ Protein Interaction Domains and Motifs - genetics
/ Protein Interaction Domains and Motifs - immunology
/ Proteins
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Spike Glycoprotein, Coronavirus - chemistry
/ Spike Glycoprotein, Coronavirus - genetics
