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Cases Spiking

Structure of Omicron variant explains evasion of antibodies and how mutations affect receptor binding

04 March 2022

Cases Spiking

First reported last November in South Africa, the Omicron variant of SARS-CoV-2, the virus responsible for COVID-19, has since rapidly spread around the world. Key to understanding Omicron’s success is the spike protein, which allows SARS-CoV-2 to penetrate human cells by latching onto a cell surface protein, angiotensin-converting enzyme 2 (ACE2). Compared to the original strain of SARS-CoV-2, Omicron’s spike protein displays 37 mutations, including 15 in its receptor-binding domain, the section that connects with ACE2. Cryogenic electron microscopy reveals how these changes affect the spike protein’s structure (pictured, in purple), and its interactions with ACE2 (in turquoise). Despite its many changes, Omicron’s spike protein strongly binds ACE2, with a similar efficiency to the spike protein of the Delta variant. Conversely, antibodies from patients both vaccinated or recovered from infections with other variants were less successful in neutralising Omicron’s spike protein, suggesting its mutations help it evade the immune response.

Written by Emmanuelle Briolat

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BPoD stands for Biomedical Picture of the Day. Managed by the MRC Laboratory of Medical Sciences until Jul 2023, it is now run independently by a dedicated team of scientists and writers. The website aims to engage everyone, young and old, in the wonders of biology, and its influence on medicine. The ever-growing archive of more than 4000 research images documents over a decade of progress. Explore the collection and see what you discover. Images are kindly provided for inclusion on this website through the generosity of scientists across the globe.

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