Journal
BIOMOLECULES
Volume 11, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/biom11121812
Keywords
SARS-CoV-2; receptor-binding domain; COVID-19; spike protein; heterologous expression; protein production
Categories
Funding
- Regione Lazio (POR FESR 2014-2020, Avviso Pubblico EMERGENZA CORONAVIRUS E OLTRE [CUP F84E21000030006]
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This study provides a detailed characterization of the native RBD produced in three major model systems, confirming their stability and correct folding. Their functionality and receptor-binding ability were further evaluated through various assays, highlighting their potential for vaccine development and diagnostic applications.
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 the 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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