PropertyValue
?:abstract
  • SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.
is ?:annotates of
?:creator
?:doi
?:doi
  • 10.1038/s41467-020-19231-9
?:journal
  • Nat_Commun
?:license
  • cc-by
?:pdf_json_files
  • document_parses/pdf_json/0ade70faad3f2013170784909b30715714378c93.json
?:pmc_json_files
  • document_parses/pmc_json/PMC7591918.xml.json
?:pmcid
?:pmid
?:pmid
  • 33110068.0
?:publication_isRelatedTo_Disease
?:sha_id
?:source
  • Medline; PMC
?:title
  • Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
?:type
?:year
  • 2020-10-27

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