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About:
Antibodies that potently inhibit or enhance SARS-CoV-2 spike protein-ACE2 interaction isolated from synthetic single-chain antibody libraries
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Antibodies that potently inhibit or enhance SARS-CoV-2 spike protein-ACE2 interaction isolated from synthetic single-chain antibody libraries
Creator
Le, Thien-Kim
Aracic, Sanja
Beasley, Matthew
Church, Nicole
Gracey, Fiona
Jabar, Shereen
Kannan, Ruban
Kiefel, Ben
Makris, Dahna
Masarati, Avisa
Mccoll, Bradley
Premaratne, S
Udawela, Madhara
Wood, Rebecca
Source
BioRxiv
abstract
Antibodies with high affinity against the receptor binding domain (RBD) of the SARS-CoV-2 S1 ectodomain were identified from screens using the Retained Display™ (ReD) platform employing a 1 × 1011 clone single-chain antibody (scFv) library. Numerous unique scFv clones capable of inhibiting binding of the viral S1 ectodomain to the ACE2 receptor in vitro were characterized. To maximize avidity, selected clones were reformatted as bivalent diabodies and monoclonal antibodies (mAb). The highest affinity mAb completely neutralized live SARS-CoV-2 virus in cell culture for four days at a concentration of 6.7 nM, suggesting potential therapeutic and/or prophylactic use. Furthermore, scFvs were identified that greatly increased the interaction of the viral S1 trimer with the ACE2 receptor, with potential implications for vaccine development.
has issue date
2020-07-28
(
xsd:dateTime
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bibo:doi
10.1101/2020.07.27.224089
has license
biorxiv
sha1sum (hex)
cddbdb9568bcba791ab5f45096257cba44feb364
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https://doi.org/10.1101/2020.07.27.224089
resource representing a document's title
Antibodies that potently inhibit or enhance SARS-CoV-2 spike protein-ACE2 interaction isolated from synthetic single-chain antibody libraries
schema:publication
bioRxiv
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covid:cddbdb9568bcba791ab5f45096257cba44feb364#body_text
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schema:about
of
named entity 'ACE2'
named entity 'UNIQUE'
named entity 'SARS-CoV-2 virus'
named entity 'scFv'
named entity 'avidity'
named entity 'ectodomain'
named entity '7 nM'
named entity 'monoclonal antibodies'
named entity 'spike protein'
named entity 'BLI'
named entity 'neutralizing antibodies'
named entity 'protein'
named entity 'ectodomain'
named entity 'antibody'
named entity 'biotin'
named entity 'molar concentration'
named entity 'ACE2'
named entity 'SARS'
named entity 'SARS-CoV-2'
named entity 'RBD'
named entity 'BLI'
named entity 'cytoplasm'
named entity 'BLI'
named entity 'ACE2'
named entity 'COVID'
named entity 'scFv'
named entity 'developing world'
named entity '0.9'
named entity 'ACE2'
named entity 'antibody-dependent enhancement'
named entity 'nM 22'
named entity 'recombinant'
named entity 'diabodies'
named entity 'SARS-CoV-2'
named entity 'infectivity'
named entity 'fluorescence'
named entity 'ACE2'
named entity 'vaccine'
named entity 'ACE2'
named entity 'protein'
named entity 'MERS-CoV'
named entity 'high affinity'
named entity '14 nM'
named entity 'SARS-CoV-2'
named entity 'FACS'
named entity 'scFv'
named entity 'antibody'
named entity 'molar'
named entity 'infection'
named entity 'ACE2'
named entity 'virus'
named entity 'Antibody'
named entity 'SARS-CoV-2'
named entity 'long-term'
named entity 'fluorescence'
named entity 'bio-layer interferometry'
named entity 'protein'
named entity 'infection'
named entity 'scFvs'
named entity 'ACE2'
named entity 'scFvs'
named entity 'ACE2'
named entity 'health care workers'
named entity 'viruses'
named entity 'mAb'
named entity 'variable domain'
named entity 'antibody'
named entity 'clone'
named entity 'Antibody-mediated'
named entity 'FACS'
named entity 'BLI'
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