EMD-27067

Single-particle
2.3 Å
EMD-27067 Deposition: 22/05/2022
Map released: 06/07/2022
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-27067

SARS-CoV-2 Spike protein in complex with a pan-sarbecovirus nanobody 1-22

EMD-27067

Single-particle
2.3 Å
EMD-27067 Deposition: 22/05/2022
Map released: 06/07/2022
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Lama glama, Severe acute respiratory syndrome coronavirus 2
Sample: SARS-CoV-2 spike protein with psNb 1-22 bound
Fitted models: 8cxq (Avg. Q-score: 0.38)
Raw data: EMPIAR-11105

Deposition Authors: Huang W, Taylor D
Superimmunity by pan-sarbecovirus nanobodies.
PUBMED: 35738279
DOI: doi:10.1016/j.celrep.2022.111004
ISSN: 2211-1247
Abstract:
Vaccine boosters and infection can facilitate the development of SARS-CoV-2 antibodies with improved potency and breadth. Here, we observe superimmunity in a camelid extensively immunized with the SARS-CoV-2 receptor-binding domain (RBD). We rapidly isolate a large repertoire of specific ultra-high-affinity nanobodies that bind strongly to all known sarbecovirus clades using integrative proteomics. These pan-sarbecovirus nanobodies (psNbs) are highly effective against SARS-CoV and SARS-CoV-2 variants, including Omicron, with the best median neutralization potency at single-digit nanograms per milliliter. A highly potent, inhalable, and bispecific psNb (PiN-31) is also developed. Structural determinations of 13 psNbs with the SARS-CoV-2 spike or RBD reveal five epitope classes, providing insights into the mechanisms and evolution of their broad activities. The highly evolved psNbs target small, flat, and flexible epitopes that contain over 75% of conserved RBD surface residues. Their potencies are strongly and negatively correlated with the distance of the epitopes from the receptor binding sites.