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10.1126/sciadv.abf5632

http://scihub22266oqcxt.onion/10.1126/sciadv.abf5632
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33958322!8172134!33958322
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suck abstract from ncbi


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pmid33958322      Sci+Adv 2021 ; 7 (23): ä
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  • Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11 #MMPMID33958322
  • Fedry J; Hurdiss DL; Wang C; Li W; Obal G; Drulyte I; Du W; Howes SC; van Kuppeveld FJM; Forster F; Bosch BJ
  • Sci Adv 2021[Jun]; 7 (23): ä PMID33958322show ga
  • The emergence of SARS-CoV-2 antibody escape mutations highlights the urgent need for broadly neutralizing therapeutics. We previously identified a human monoclonal antibody, 47D11, capable of cross-neutralizing SARS-CoV-2 and SARS-CoV and protecting against the associated respiratory disease in an animal model. Here, we report cryo-EM structures of both trimeric spike ectodomains in complex with the 47D11 Fab. 47D11 binds to the closed receptor-binding domain, distal to the ACE2 binding site. The CDRL3 stabilizes the N343 glycan in an upright conformation, exposing a mutationally constrained hydrophobic pocket, into which the CDRH3 loop inserts two aromatic residues. 47D11 stabilizes a partially open conformation of the SARS-CoV-2 spike, suggesting that it could be used effectively in combination with other antibodies targeting the exposed receptor-binding motif. Together, these results reveal a cross-protective epitope on the SARS-CoV-2 spike and provide a structural roadmap for the development of 47D11 as a prophylactic or postexposure therapy for COVID-19.
  • |*Antibodies, Monoclonal/chemistry/immunology[MESH]
  • |*Antibodies, Neutralizing/chemistry/immunology[MESH]
  • |*Antibodies, Viral/chemistry/immunology[MESH]
  • |*SARS-CoV-2/chemistry/immunology[MESH]
  • |*Severe acute respiratory syndrome-related coronavirus/chemistry/immunology[MESH]
  • |Humans[MESH]


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