EMD-22301

Single-particle
3.7 Å
EMD-22301 Deposition: 15/07/2020
Map released: 22/07/2020
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-22301

SARS-CoV-2 Spike D614G variant, minus RBD

EMD-22301

Single-particle
3.7 Å
EMD-22301 Deposition: 15/07/2020
Map released: 22/07/2020
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Severe acute respiratory syndrome coronavirus 2
Sample: SARS2 Spike D614G
Fitted models: 6xs6 (Avg. Q-score: 0.468)

Deposition Authors: Wang X, Egri SB
Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.
PUBMED: 32991842
DOI: doi:10.1016/j.cell.2020.09.032
ISSN: 1097-4172
Abstract:
The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated.