8GNH

Complex structure of BD-218 and Spike protein

Summary for 8GNH

• Entry DOI: 10.2210/pdb8gnh/pdb
• EMDB information: 34164
• Descriptor: Spike glycoprotein, Heavy chain of BD-218, Light chain of BD-218, ... (5 entities in total)
• Functional Keywords: sars-cov-2, neutralizing monoclonal antibody, antiviral protein, viral protein-antiviral protein complex, viral protein/antiviral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2; More
• Total number of polymer chains: 5
• Total formula weight: 469326.87

Authors

Wang, B.,Xu, H.,Su, X.D. (deposition date: 2022-08-23, release date: 2023-08-30, Last modification date: 2024-10-23)

Primary citation

Wang, B.,Xu, H.,Liang, Z.T.,Zhao, T.N.,Zhang, X.,Peng, T.B.,Wang, Y.C.,Su, X.D.
Human antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2.
Int.J.Biol.Macromol., 227:896-902, 2023

PubMed Abstract: As SARS-CoV-2 variants of concern (VOC) reduce the effectiveness of existing anti-COVID therapeutics, it is increasingly critical to identify highly potent neutralizing antibodies (nAbs) that bind to conserved regions across multiple variants, especially beta, delta, and omicron variants. Using single-cell sequencing with biochemical methods and pseudo-typed virus neutralization experiments, here we report the characterization of a potent nAb BD-218, identified from an early screen of patients recovering from the original virus. We have determined the cryo-EM structure of the BD-218/spike protein complex to define its epitope in detail, which revealed that BD-218 interacts with a novel epitope on the receptor-binding domain (RBD) of the spike protein. We concluded that BD-218 is a highly effective and broadly active nAb against SARS-CoV-2 variants with promising potential for therapeutic development.

PubMed: 36528147
DOI: 10.1016/j.ijbiomac.2022.12.120

Experimental method

ELECTRON MICROSCOPY (3.74 Å)