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TitleHuman antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2.
Journal, issue, pagesInt J Biol Macromol, Vol. 227, Page 896-902, Year 2023
Publish dateFeb 1, 2023
AuthorsBo Wang / Hua Xu / Zi-Teng Liang / Tian-Ning Zhao / Xin Zhang / Tian-Bo Peng / You-Chun Wang / Xiao-Dong Su /
PubMed AbstractAs 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 ...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.
External linksInt J Biol Macromol / PubMed:36528147 / PubMed Central
MethodsEM (single particle)
Resolution3.74 Å
Structure data

34164

8gnh

EMDB-34164, PDB-8gnh:
Complex structure of BD-218 and Spike protein
Method: EM (single particle) / Resolution: 3.74 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/ANTIVIRAL PROTEIN / SARS-CoV-2 / Neutralizing monoclonal antibody / ANTIVIRAL PROTEIN / VIRAL PROTEIN-ANTIVIRAL PROTEIN complex

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