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These interactions appear to compensate for other Omicron mutations such as the substitution of asparagine for lysine at position 417 (K417N) that are known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for the Delta and Omicron variants. Neutralization assays show that pseudoviruses that display the Omicron spike protein exhibit increased antibody evasion. The increase in antibody evasion and the retention of strong interactions at the ACE2 interface thus represent important molecular features that likely contribute to the rapid spread of the Omicron variant.<\/jats:p>","DOI":"10.1126\/science.abn7760","type":"journal-article","created":{"date-parts":[[2022,1,20]],"date-time":"2022-01-20T18:59:05Z","timestamp":1642705145000},"page":"760-764","source":"Crossref","is-referenced-by-count":627,"title":["SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein\u2013ACE2 complex"],"prefix":"10.1126","volume":"375","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7154-8677","authenticated-orcid":true,"given":"Dhiraj","family":"Mannar","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, 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