tetano
Editor, Senior Moderator
Cell Rep
. 2022 Feb 7;110428.
doi: 10.1016/j.celrep.2022.110428. Online ahead of print.
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti[SUP] 1 [/SUP], Yicheng Guo[SUP] 2 [/SUP], Lihong Liu[SUP] 3 [/SUP], Liyuan Liu[SUP] 4 [/SUP], Zhening Zhang[SUP] 5 [/SUP], Yang Luo[SUP] 3 [/SUP], Yiming Huang[SUP] 4 [/SUP], Harris H Wang[SUP] 4 [/SUP], David D Ho[SUP] 6 [/SUP], Zizhang Sheng[SUP] 7 [/SUP], Lawrence Shapiro[SUP] 8 [/SUP]
Affiliations
Abstract
The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 Å-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies.
Keywords: B.1.1.529; COVID-19; NTD; Omicron; RBD; SARS-CoV-2; cryo-EM; neutralizing antibody; spike; variant of concern.
. 2022 Feb 7;110428.
doi: 10.1016/j.celrep.2022.110428. Online ahead of print.
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti[SUP] 1 [/SUP], Yicheng Guo[SUP] 2 [/SUP], Lihong Liu[SUP] 3 [/SUP], Liyuan Liu[SUP] 4 [/SUP], Zhening Zhang[SUP] 5 [/SUP], Yang Luo[SUP] 3 [/SUP], Yiming Huang[SUP] 4 [/SUP], Harris H Wang[SUP] 4 [/SUP], David D Ho[SUP] 6 [/SUP], Zizhang Sheng[SUP] 7 [/SUP], Lawrence Shapiro[SUP] 8 [/SUP]
Affiliations
- PMID: 35172173
- DOI: 10.1016/j.celrep.2022.110428
Abstract
The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 Å-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies.
Keywords: B.1.1.529; COVID-19; NTD; Omicron; RBD; SARS-CoV-2; cryo-EM; neutralizing antibody; spike; variant of concern.