7WG9

Delta Spike Trimer(1 RBD Up)

Summary for 7WG9

• Entry DOI: 10.2210/pdb7wg9/pdb
• EMDB information: 32481
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: sars-cov-2, delta, spike, neutral, structural protein
• Biological source: Severe acute respiratory syndrome coronavirus 2
• Total number of polymer chains: 3
• Total formula weight: 436308.06

Authors

Cui, Z. (deposition date: 2021-12-28, release date: 2022-06-22, Last modification date: 2024-10-23)

Primary citation

Cui, Z.,Liu, P.,Wang, N.,Wang, L.,Fan, K.,Zhu, Q.,Wang, K.,Chen, R.,Feng, R.,Jia, Z.,Yang, M.,Xu, G.,Zhu, B.,Fu, W.,Chu, T.,Feng, L.,Wang, Y.,Pei, X.,Yang, P.,Xie, X.S.,Cao, L.,Cao, Y.,Wang, X.
Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron.
Cell, 185:860-871.e13, 2022

PubMed Abstract: The SARS-CoV-2 Omicron variant with increased fitness is spreading rapidly worldwide. Analysis of cryo-EM structures of the spike (S) from Omicron reveals amino acid substitutions forging interactions that stably maintain an active conformation for receptor recognition. The relatively more compact domain organization confers improved stability and enhances attachment but compromises the efficiency of the viral fusion step. Alterations in local conformation, charge, and hydrophobic microenvironments underpin the modulation of the epitopes such that they are not recognized by most NTD- and RBD-antibodies, facilitating viral immune escape. Structure of the Omicron S bound with human ACE2, together with the analysis of sequence conservation in ACE2 binding region of 25 sarbecovirus members, as well as heatmaps of the immunogenic sites and their corresponding mutational frequencies, sheds light on conserved and structurally restrained regions that can be used for the development of broad-spectrum vaccines and therapeutics.

PubMed: 35120603
DOI: 10.1016/j.cell.2022.01.019

Experimental method

ELECTRON MICROSCOPY (3.5 Å)