EMD-26647

Single-particle
3.74 Å
EMD-26647 Deposition: 12/04/2022
Map released: 20/04/2022
Last modified: 17/01/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-26647

SARS-CoV-2 Omicron-BA.2 1-RBD-up Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-Omicron-BA.2)

EMD-26647

Single-particle
3.74 Å
EMD-26647 Deposition: 12/04/2022
Map released: 20/04/2022
Last modified: 17/01/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: SARS-CoV-2 S-GSAS-Omicron-BA.2 Spike Ectodomain

Deposition Authors: Stalls V , Acharya P
Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike.
PUBMED: 35732171
DOI: doi:10.1016/j.celrep.2022.111009
ISSN: 2211-1247
Abstract:
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron BA.2 sub-lineage has gained in proportion relative to BA.1. Because spike (S) protein variations may underlie differences in their pathobiology, here we determine cryoelectron microscopy (cryo-EM) structures of the BA.2 S ectodomain and compare these with previously determined BA.1 S structures. BA.2 receptor-binding domain (RBD) mutations induce remodeling of the RBD structure, resulting in tighter packing and improved thermostability. Interprotomer RBD interactions are enhanced in the closed (or 3-RBD-down) BA.2 S, while the fusion peptide is less accessible to antibodies than in BA.1. Binding and pseudovirus neutralization assays reveal extensive immune evasion while defining epitopes of two outer RBD face-binding antibodies, DH1044 and DH1193, that neutralize both BA.1 and BA.2. Taken together, our results indicate that stabilization of the closed state through interprotomer RBD-RBD packing is a hallmark of the Omicron variant and show differences in key functional regions in the BA.1 and BA.2 S proteins.