id,collection,dc.contributor.author,dc.date.accessioned,dc.date.available,dc.date.issued,dc.description.abstract[en],dc.format.extent,dc.identifier.uri,dc.language,dc.rights.uri,dc.subject.ddc,dc.subject[de],dc.subject[en],dc.title,dc.type,dcterms.accessRights.openaire,dcterms.bibliographicCitation.articlenumber,dcterms.bibliographicCitation.doi,dcterms.bibliographicCitation.journaltitle,dcterms.bibliographicCitation.number,dcterms.bibliographicCitation.url,dcterms.bibliographicCitation.volume,dcterms.isPartOf.eissn,refubium.affiliation,refubium.affiliation.other,refubium.resourceType.isindependentpub,refubium.resourceType.provider "4df333b3-be72-4771-982f-448e3dbac42d","fub188/16","Bertoglio, Federico||Fühner, Viola||Ruschig, Maximilian||Heine, Philip Alexander||Abassi, Leila||Klünemann, Thomas||Rand, Ulfert||Adler, Julia||Trimpert, Jakob||Frenzel, André","2021-09-08T07:49:28Z","2021-09-08T07:49:28Z","2021","The novel betacoronavirus severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) causes a form of severe pneumonia disease called coronavirus disease 2019 (COVID-19). To develop human neutralizing anti-SARS-CoV-2 antibodies, antibody gene libraries from convalescent COVID-19 patients were constructed and recombinant antibody fragments (scFv) against the receptor-binding domain (RBD) of the spike protein were selected by phage display. The antibody STE90-C11 shows a subnanometer IC50 in a plaque-based live SARS-CoV-2 neutralization assay. The in vivo efficacy of the antibody is demonstrated in the Syrian hamster and in the human angiotensin-converting enzyme 2 (hACE2) mice model. The crystal structure of STE90-C11 Fab in complex with SARS-CoV-2-RBD is solved at 2.0 Å resolution showing that the antibody binds at the same region as ACE2 to RBD. The binding and inhibition of STE90-C11 is not blocked by many known emerging RBD mutations. STE90-C11-derived human IgG1 with FcγR-silenced Fc (COR-101) is undergoing Phase Ib/II clinical trials for the treatment of moderate to severe COVID-19.","23 Seiten","https://refubium.fu-berlin.de/handle/fub188/31878||http://dx.doi.org/10.17169/refubium-31610","eng","https://creativecommons.org/licenses/by/4.0/","500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie","neutralizing antibody","SARS-CoV-2||RBD||spike protein||recombinant antibody||phage display||immune library||in vivo neutralization","A SARS-CoV-2 neutralizing antibody selected from COVID-19 patients binds to the ACE2-RBD interface and is tolerant to most known RBD mutations","Wissenschaftlicher Artikel","open access","109433","10.1016/j.celrep.2021.109433","Cell Reports","4","https://doi.org/10.1016/j.celrep.2021.109433","36","2211-1247","Veterinärmedizin","Institut für Virologie:::77693aa8-533b-4241-8627-e73e9ce18bc0:::600","no","WoS-Alert"