9CRH

Cryo-EM structure of SARS-CoV-2 Spike Proteins on intact virions: Delta (B.1.617.2) variant 3 closed RBDs

9CRH の概要

• エントリーDOI: 10.2210/pdb9crh/pdb
• 関連するPDBエントリー: 9CRC 9CRD 9CRE 9CRF 9CRG
• EMDBエントリー: 45863 45864 45865 45866 45867 45868
• 分子名称: 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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: sars-cov-2 variant, delta (b.1.617.2) variant, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 439426.12

構造登録者

Ke, Z.,Briggs, J.A.G. (登録日: 2024-07-22, 公開日: 2024-11-27, 最終更新日: 2024-12-25)

主引用文献

Ke, Z.,Peacock, T.P.,Brown, J.C.,Sheppard, C.M.,Croll, T.I.,Kotecha, A.,Goldhill, D.H.,Barclay, W.S.,Briggs, J.A.G.
Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants.
Embo J., 43:6469-6495, 2024

PubMed Abstract: The evolution of SARS-CoV-2 variants with increased fitness has been accompanied by structural changes in the spike (S) proteins, which are the major target for the adaptive immune response. Single-particle cryo-EM analysis of soluble S protein from SARS-CoV-2 variants has revealed this structural adaptation at high resolution. The analysis of S trimers in situ on intact virions has the potential to provide more functionally relevant insights into S structure and virion morphology. Here, we characterized B.1, Alpha, Beta, Gamma, Delta, Kappa, and Mu variants by cryo-electron microscopy and tomography, assessing S cleavage, virion morphology, S incorporation, "in-situ" high-resolution S structures, and the range of S conformational states. We found no evidence for adaptive changes in virion morphology, but describe multiple different positions in the S protein where amino acid changes alter local protein structure. Taken together, our data are consistent with a model where amino acid changes at multiple positions from the top to the base of the spike cause structural changes that can modulate the conformational dynamics of the S protein.

PubMed: 39543395
DOI: 10.1038/s44318-024-00303-1

実験手法

ELECTRON MICROSCOPY (3.4 Å)