7TNW

Structural and functional impact by SARS-CoV-2 Omicron spike mutations

Summary for 7TNW

• Entry DOI: 10.2210/pdb7tnw/pdb
• EMDB information: 26021
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2
• Total number of polymer chains: 3
• Total formula weight: 446964.41

Authors

Zhang, J.,Xiao, T.S.,Cai, Y.F.,Peng, H.Q.,Volloch, S.R.,Chen, B. (deposition date: 2022-01-21, release date: 2022-02-16, Last modification date: 2024-10-09)

Primary citation

Zhang, J.,Cai, Y.,Lavine, C.L.,Peng, H.,Zhu, H.,Anand, K.,Tong, P.,Gautam, A.,Mayer, M.L.,Rits-Volloch, S.,Wang, S.,Sliz, P.,Wesemann, D.R.,Yang, W.,Seaman, M.S.,Lu, J.,Xiao, T.,Chen, B.
Structural and functional impact by SARS-CoV-2 Omicron spike mutations.
Cell Rep, 39:110729-110729, 2022

PubMed Abstract: The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutralizing antibodies. These results suggest that Omicron S has acquired an extraordinary ability to evade host immunity by excessive mutations, which also compromise its fusogenic capability.

PubMed: 35452593
DOI: 10.1016/j.celrep.2022.110729

Experimental method

ELECTRON MICROSCOPY (3.1 Å)