Journal Article Research Support, N.I.H., Extramural Epublish 9 citations
PubMed: 37726484 DOI: 10.1038/s42003-023-05332-w
SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain.
Commun Biol 6(1):953
Authors: Jiansheng Jiang, Christopher T Boughter, Javeed Ahmad, Kannan Natarajan, Lisa F Boyd, Martin Meier-Schellersheim, David H Margulies
Affiliations
- Molecular Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, 20892, USA.
- Computational Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, 20892, USA.
- Molecular Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, 20892, USA.
- Molecular Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, 20892, USA.
Abstract
The COVID-19 pandemic and SARS-CoV-2 variants have dramatically illustrated the need for a better understanding of antigen (epitope)-antibody (paratope) interactions. To gain insight into the immunogenic characteristics of epitopic sites (ES), we systematically investigated the structures of 340 Abs and 83 nanobodies (Nbs) complexed with the Receptor Binding Domain (RBD) of the SARS-CoV-2 spike protein. We identified 23 distinct ES on the RBD surface and determined the frequencies of amino acid usage in the corresponding CDR paratopes. We describe a clustering method for analysis of ES similarities that reveals binding motifs of the paratopes and that provides insights for vaccine design and therapies for SARS-CoV-2, as well as a broader understanding of the structural basis of Ab-protein antigen (Ag) interactions.
MeSH
Antibodies, Sars Virus, Binding Sites, Antibody, Covid-19, Sars-Cov-2
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