EMD-34687

Single-particle
3.5 Å
EMD-34687 Deposition: 08/11/2022
Map released: 26/04/2023
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-34687

SARS-CoV-2 Spike trimer in complex with RmAb 9H1 Fab in the class 2 conformation

EMD-34687

Single-particle
3.5 Å
EMD-34687 Deposition: 08/11/2022
Map released: 26/04/2023
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Severe acute respiratory syndrome coronavirus 2, Oryctolagus cuniculus
Sample: SARS-CoV-2 WT spike glycoprotein complex with RmAb 9H1 Fabs
Fitted models: 8hec (Avg. Q-score: 0.358)

Deposition Authors: Guo H , Gao Y, Lu Y , Yang H, Ji X
Mechanism of an RBM-targeted rabbit monoclonal antibody 9H1 neutralizing SARS-CoV-2.
Chu X, Ding X, Yang Y, Lu Y , Li T, Gao Y, Zheng L, Xiao H, Yang T, Cheng H, Huang H, Liu Y, Lou Y, Wu C, Chen Y , Yang H, Ji X, Guo H
(2023) Biochem Biophys Res Commun , 660 , 43 - 49
PUBMED: 37062240
DOI: doi:10.1016/j.bbrc.2023.04.002
ISSN: 1090-2104
ASTM: BBRCA9
Abstract:
The COVID-19 pandemic, caused by SARS-CoV-2, has led to over 750 million infections and 6.8 million deaths worldwide since late 2019. Due to the continuous evolution of SARS-CoV-2, many significant variants have emerged, creating ongoing challenges to the prevention and treatment of the pandemic. Therefore, the study of antibody responses against SARS-CoV-2 is essential for the development of vaccines and therapeutics. Here we perform single particle cryo-electron microscopy (cryo-EM) structure determination of a rabbit monoclonal antibody (RmAb) 9H1 in complex with the SARS-CoV-2 wild-type (WT) spike trimer. Our structural analysis shows that 9H1 interacts with the receptor-binding motif (RBM) region of the receptor-binding domain (RBD) on the spike protein and by directly competing with angiotensin-converting enzyme 2 (ACE2), it blocks the binding of the virus to the receptor and achieves neutralization. Our findings suggest that utilizing rabbit-derived mAbs provides valuable insights into the molecular interactions between neutralizing antibodies and spike proteins and may also facilitate the development of therapeutic antibodies and expand the antibody library.