{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Miller CJ"],"funding":["NIAID NIH HHS","Small Business Technology Transfer","National Institutes of Health","NIGMS NIH HHS"],"pagination":["79-85"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7863792"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62"],"pubmed_abstract":["A phage library displaying 10<sup>10</sup> variants of the fibronectin type III (FN3) domain was affinity selected with the biotinylated form of the receptor binding domain (RBD, residues 319-541) of the SARS-CoV-2 virus spike protein. Nine binding FN3 variants (i.e. monobodies) were recovered, representing four different primary structures. Soluble forms of the monobodies bound to several different preparations of the RBD and the S1 spike subunit, with affinities ranging from 3 to 14 nM as measured by bio-layer interferometry. Three of the four monobodies bound selectively to the RBD of SARS-CoV-2, with the fourth monobody showing slight cross-reactivity to the RBD of SARS-CoV-1 virus. Examination of binding to the spike fragments and its trimeric form revealed that the monobodies recogni"],"journal":["New biotechnology"],"pubmed_title":["FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein."],"pmcid":["PMC7863792"],"funding_grant_id":["HHSN272201400008C","R41 GM134782","GM134782-01"],"pubmed_authors":["Simmons E","Abdeen SJ","Amet T","Van Huysse JW","Martinez MJ","Wang G","Bowsher RR","McGinnis JE","Miller CJ","Zhou J","Kay BK"],"additional_accession":[]},"is_claimable":false,"name":"FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein.","description":"A phage library displaying 10<sup>10</sup> variants of the fibronectin type III (FN3) domain was affinity selected with the biotinylated form of the receptor binding domain (RBD, residues 319-541) of the SARS-CoV-2 virus spike protein. Nine binding FN3 variants (i.e. monobodies) were recovered, representing four different primary structures. Soluble forms of the monobodies bound to several different preparations of the RBD and the S1 spike subunit, with affinities ranging from 3 to 14 nM as measured by bio-layer interferometry. Three of the four monobodies bound selectively to the RBD of SARS-CoV-2, with the fourth monobody showing slight cross-reactivity to the RBD of SARS-CoV-1 virus. Examination of binding to the spike fragments and its trimeric form revealed that the monobodies recogni","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2026-04-30T17:01:58.19Z","creation":"2021-02-21T10:04:53Z"},"accession":"S-EPMC7863792","cross_references":{"pubmed":["33556628"],"doi":["10.1016/j.nbt.2021.01.010"]}}