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10.1038/s41467-020-19146-5

http://scihub22266oqcxt.onion/10.1038/s41467-020-19146-5
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33087721!7577971!33087721
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suck abstract from ncbi


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pmid33087721      Nat+Commun 2020 ; 11 (1): 5337
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  • Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein #MMPMID33087721
  • Wrobel AG; Benton DJ; Hussain S; Harvey R; Martin SR; Roustan C; Rosenthal PB; Skehel JJ; Gamblin SJ
  • Nat Commun 2020[Oct]; 11 (1): 5337 PMID33087721show ga
  • The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.
  • |Animals[MESH]
  • |Antibodies, Monoclonal/*immunology[MESH]
  • |Antibodies, Viral/*immunology[MESH]
  • |Betacoronavirus/*immunology[MESH]
  • |Binding Sites, Antibody/*immunology[MESH]
  • |COVID-19[MESH]
  • |Cell Line[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Coronavirus Infections/virology[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Humans[MESH]
  • |Neutralization Tests[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/virology[MESH]
  • |Protein Domains/immunology[MESH]
  • |SARS-CoV-2[MESH]
  • |Spike Glycoprotein, Coronavirus/*immunology[MESH]


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