EMD-11497

Single-particle
3.5 Å
EMD-11497 Deposition: 28/07/2020
Map released: 05/08/2020
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-11497

Cryo-EM structure of SARS-CoV-2 Spike Proteins on intact virions: 3 Closed RBDs

EMD-11497

Single-particle
3.5 Å
EMD-11497 Deposition: 28/07/2020
Map released: 05/08/2020
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Severe acute respiratory syndrome coronavirus 2
Sample: Severe acute respiratory syndrome coronavirus 2
Fitted models: 6zwv (Avg. Q-score: 0.402)
Raw data: EMPIAR-10492

Deposition Authors: Ke Z , Qu K , Nakane T , Xiong X , Cortese M , Zila V , Scheres SHW , Briggs JAG
Structures and distributions of SARS-CoV-2 spike proteins on intact virions.
PUBMED: 32805734
DOI: doi:10.1038/s41586-020-2665-2
ISSN: 1476-4687
ASTM: NATUAS
Abstract:
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2-6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9-12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.