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10.15252/emmm.202114544

http://scihub22266oqcxt.onion/10.15252/emmm.202114544
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34672091!8646660!34672091
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suck abstract from ncbi


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pmid34672091      EMBO+Mol+Med 2021 ; 13 (12): e14544
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  • Uncovering a conserved vulnerability site in SARS-CoV-2 by a human antibody #MMPMID34672091
  • Li T; Cai H; Zhao Y; Li Y; Lai Y; Yao H; Liu LD; Sun Z; van Vlissingen MF; Kuiken T; GeurtsvanKessel CH; Zhang N; Zhou B; Lu L; Gong Y; Qin W; Mondal M; Duan B; Xu S; Richard AS; Raoul H; Chen J; Xu C; Wu L; Zhou H; Huang Z; Zhang X; Li J; Wang Y; Bi Y; Rockx B; Chen J; Meng FL; Lavillette D; Li D
  • EMBO Mol Med 2021[Dec]; 13 (12): e14544 PMID34672091show ga
  • An essential step for SARS-CoV-2 infection is the attachment to the host cell receptor by its Spike receptor-binding domain (RBD). Most of the existing RBD-targeting neutralizing antibodies block the receptor-binding motif (RBM), a mutable region with the potential to generate neutralization escape mutants. Here, we isolated and structurally characterized a non-RBM-targeting monoclonal antibody (FD20) from convalescent patients. FD20 engages the RBD at an epitope distal to the RBM with a K(D) of 5.6 nM, neutralizes SARS-CoV-2 including the current Variants of Concern such as B.1.1.7, B.1.351, P.1, and B.1.617.2 (Delta), displays modest cross-reactivity against SARS-CoV, and reduces viral replication in hamsters. The epitope coincides with a predicted "ideal" vulnerability site with high functional and structural constraints. Mutation of the residues of the conserved epitope variably affects FD20-binding but confers little or no resistance to neutralization. Finally, in vitro mode-of-action characterization and negative-stain electron microscopy suggest a neutralization mechanism by which FD20 destructs the Spike. Our results reveal a conserved vulnerability site in the SARS-CoV-2 Spike for the development of potential antiviral drugs.
  • |*COVID-19[MESH]
  • |*SARS-CoV-2[MESH]
  • |Antibodies, Viral[MESH]
  • |Humans[MESH]


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