Molecular basis of receptor binding and antibody neutralization of Omicron

• Published in: Nature (London) Vol. 604; no. 7906; pp. 546 - 552
• Main Authors: Hong, Qin, Han, Wenyu, Li, Jiawei, Xu, Shiqi, Wang, Yifan, Xu, Cong, Li, Zuyang, Wang, Yanxing, Zhang, Chao, Huang, Zhong, Cong, Yao
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.04.2022; Nature Publishing Group
• Subjects: 101/28; 631/250/590/2294; 631/535/1258/1259; 96/1; ACE2; Angiotensin-Converting Enzyme 2; Antibodies; Antibodies, Viral; Bonding strength; COVID-19; COVID-19 Vaccines; Cryoelectron Microscopy; Electron microscopy; Humanities and Social Sciences; Humans; Hydrogen; Hydrogen bonding; Hydrogen bonds; Microscopy; multidisciplinary; Mutation; Neutralization; Population; Proteins; Receptors; SARS-CoV-2; Science; Science (multidisciplinary); Severe acute respiratory syndrome coronavirus 2; Spike Glycoprotein, Coronavirus; Surface properties

The SARS-CoV-2 Omicron variant exhibits striking immune evasion and is spreading rapidly worldwide. Understanding the structural basis of the high transmissibility and enhanced immune evasion of Omicron is of high importance. Here, using cryo-electron microscopy, we present both the closed and the o...