About: Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy

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About: Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy
Creator	Liu, Bin Zhang, Tao Zeng, Xin Lin, Jing Du, Jianhua Kong, Yang Li, Lingfang Li, Xinlei Liu, Jianghai Xiao, Huahong Zeng, Shunze Zhang, Shelin
Source	BioRxiv
abstract	The infection of the novel coronavirus SARS-CoV-2 have caused more than 150,000 deaths, but no vaccine or specific therapeutic antibody is currently available. SARS-CoV-2 relies on its spike protein, in particular the receptor binding domain (RBD), to bind human cell receptor angiotensin-converting enzyme 2 (ACE2) for viral entry, and thus targeting RBD holds the promise for preventing SARS-CoV-2 infection. In this work, a competitive biopanning strategy of a phage display antibody library was applied to screen blocking antibodies against RBD. High-affinity antibodies were enriched after the first round using a standard panning process in which RBD-His recombinant protein was immobilized as a bait. At the next two rounds, immobilized ACE2-Fc and free RBD-His proteins were mixed with the enriched phage antibodies. Antibodies binding to RBD at epitopes different from ACE2-binding site were captured by the immobilized ACE2-Fc, forming a “sandwich” complex. Only antibodies competed with ACE2 for recognizing RBD at the same or similar epitopes can bind to the free RBD-His in the supernatant and be subsequently separated by the Ni-NTA magnetic beads. Top 1 lead from the competitive biopanning of a synthetic antibody library, Lib AB1, was produced as the full-length IgG1 format. It was proved to competitively block the binding of RBD to ACE2 protein, and potently inhibit SARS-CoV-2 pseudovirus infection of ACE2-overexpressing Hela cells with IC50 values of 12nM. Nevertheless, top 1 lead from the standard biopanning of Lib AB1, can only bind to RBD in vitro but not have the blocking or neutralization activity. Our strategy can efficiently isolate the blocking antibodies of RBD, and it would speed up the discovery of neutralizing antibodies against SARS-CoV-2.
has issue date	2020-04-20(xsd:dateTime)
bibo:doi	10.1101/2020.04.19.049643
has license	biorxiv
sha1sum (hex)	b84047a5731db3ab96287fffef86b04ddda65825
schema:url	https://doi.org/10.1101/2020.04.19.049643
resource representing a document's title	Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy
schema:publication	bioRxiv
resource representing a document's body	covid:b84047a5731db3ab96287fffef86b04ddda65825#body_text
is schema:about of	named entity 'beads' named entity 'bind' named entity 'antibodies' named entity 'captured' named entity 'library' named entity 'RBD' named entity 'competitive' named entity 'recognizing' named entity 'holds' named entity 'library' named entity 'CAUSED' named entity 'binding site' named entity 'antibodies' named entity 'immobilized' named entity 'therapeutic' named entity 'mixed' named entity 'block' named entity 'bind' named entity 'infection' named entity 'ACE2' named entity 'host cells' named entity 'SARS-CoV-2' named entity 'lysis buffer' named entity 'infection' named entity 'receptor' named entity 'public health emergency of international concern' named entity 'antibody' named entity 'phage' named entity 'SARS-CoV-2' named entity 'efficiently' named entity 'coronavirus' named entity 'ACE2' named entity 'ACE2' named entity 'receptor' named entity 'blocking antibodies' named entity 'Hela cells' named entity 'Ni-NTA' named entity 'neutralizing antibodies' named entity 'RBD' named entity 'biopanning' named entity 'vaccine' named entity 'phage' named entity 'RBD' named entity 'binding site' named entity 'phage display' named entity 'Antibodies' named entity 'antibody' named entity 'supernatant' named entity 'RBD' named entity 'IC50' named entity 'ACE2' named entity 'coronavirus' named entity 'ACE2' named entity 'recombinant protein' named entity 'SARS-CoV-2' named entity 'biopanning' named entity 'SARS-CoV-2' named entity 'antibodies' named entity 'SARS-CoV-2' named entity 'homology' named entity 'high-affinity' named entity 'ACE2' named entity 'phages' named entity 'IC50' named entity 'competitive binding' named entity 'proteolysis' named entity 'human monoclonal antibodies' named entity 'coronavirus' named entity 'RBD' named entity 'recombinant' named entity 'RBD' named entity 'SARS-CoV-2' named entity 'ACE2'

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