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TitleAntibody-mediated disruption of the SARS-CoV-2 spike glycoprotein.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5337, Year 2020
Publish dateOct 21, 2020
AuthorsAntoni G Wrobel / Donald J Benton / Saira Hussain / Ruth Harvey / Stephen R Martin / Chloë Roustan / Peter B Rosenthal / John J Skehel / Steven J Gamblin /
PubMed AbstractThe 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- ...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.
External linksNat Commun / PubMed:33087721 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 3.9 Å
Structure data

11647

7a5s

EMDB-11647, PDB-7a5s:
Complex of SARS-CoV-2 spike and CR3022 Fab (Homogeneous Refinement)
Method: EM (single particle) / Resolution: 3.9 Å

11648

7a5r

EMDB-11648, PDB-7a5r:
Complex of SARS-CoV-2 spike and CR3022 Fab (Non-Uniform Refinement)
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
  • Homo heidelbergensis (Heidelberg man)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Antibody

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