Author: Maffei, Mariano; Montemiglio, Linda Celeste; Vitagliano, Grazia; Fedele, Luigi; Sellathurai, Shaila; Bucci, Federica; Compagnone, Mirco; Chiarini, Valerio; Exertier, Cécile; Muzi, Alessia; Roscilli, Giuseppe; Vallone, Beatrice; Marra, Emanuele
Title: The nuts and bolts of SARS-CoV-2 Spike Receptor Binding Domain heterologous expression Cord-id: 6qqq64l2 Document date: 2021_9_17
ID: 6qqq64l2
Snippet: COVID-19 is a highly infectious disease caused by a newly emerged coronavirus (SARS-CoV-2) that has rapidly progressed into a pandemic. This unprecedent emergency has stressed the significance of developing effective therapeutics to fight current and future outbreaks. The receptor-binding domain (RBD) of the SARS-CoV-2 surface Spike protein is the main target for vaccines and represents a helpful “tool†to produce neutralizing antibodies or diagnostic kits. In this work, we provide a detaile
Document: COVID-19 is a highly infectious disease caused by a newly emerged coronavirus (SARS-CoV-2) that has rapidly progressed into a pandemic. This unprecedent emergency has stressed the significance of developing effective therapeutics to fight current and future outbreaks. The receptor-binding domain (RBD) of the SARS-CoV-2 surface Spike protein is the main target for vaccines and represents a helpful “tool†to produce neutralizing antibodies or diagnostic kits. In this work, we provide a detailed characterization of the native RBD produced in three major model systems: Escherichia coli, insect and HEK-293 cells. Circular dichroism, gel filtration chromatography and thermal denaturation experiments indicated that recombinant SARS-CoV-2 RBD proteins are stable and correctly folded. In addition, their functionality and receptor-binding ability were further evaluated through ELISA, flow cytometry assays and bio-layer interferometry.
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