FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein.

ABSTRACT: A phage library displaying 10¹⁰ 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

SUBMITTER: Miller CJ 

PROVIDER: S-EPMC7863792 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature