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Publication : The antigenic anatomy of SARS-CoV-2 receptor binding domain.

First Author	Dejnirattisai W	Year	2021
Journal	Cell	Volume	184
Issue	8	Pages	2183-2200.e22
PubMed ID	33756110	Mgi Jnum	J:335893
Mgi Id	MGI:6706295	Doi	10.1016/j.cell.2021.02.032
Citation	Dejnirattisai W, et al. (2021) The antigenic anatomy of SARS-CoV-2 receptor binding domain. Cell 184(8):2183-2200.e22

abstractText

Antibodies are crucial to immune protection against SARS-CoV-2, with some in emergency use as therapeutics. Here, we identify 377 human monoclonal antibodies (mAbs) recognizing the virus spike and focus mainly on 80 that bind the receptor binding domain (RBD). We devise a competition data-driven method to map RBD binding sites. We find that although antibody binding sites are widely dispersed, neutralizing antibody binding is focused, with nearly all highly inhibitory mAbs (IC50 < 0.1 mug/mL) blocking receptor interaction, except for one that binds a unique epitope in the N-terminal domain. Many of these neutralizing mAbs use public V-genes and are close to germline. We dissect the structural basis of recognition for this large panel of antibodies through X-ray crystallography and cryoelectron microscopy of 19 Fab-antigen structures. We find novel binding modes for some potently inhibitory antibodies and demonstrate that strongly neutralizing mAbs protect, prophylactically or therapeutically, in animal models.

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Publication : The antigenic anatomy of SARS-CoV-2 receptor binding domain.

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