Recombinant SARS-CoV Spike RBD protein

Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV), Middle Eastern Respiratory Syndrome Coronavirus (MERS-CoV), and the recently identified novel Coronavirus (SARS-CoV-2) belong to the Coronaviridae family, genus Betacoronavirus, that has been related to important epidemiological outbreaks. SARS-CoV emerged in 2003 as a significant threat to human health. SARS-CoV has four structural proteins, known as the S (spike), E (envelope), M (membrane), and N (nucleocapsid) proteins. The spike protein, responsible for allowing the virus to attach to and fuse with the membrane of a host cell and is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. It attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. A metallopeptidase, angiotensin-converting enzyme 2 (ACE-2), has been identified as a functional receptor for SARS-CoV through interaction with a receptor binding domain (RBD) located at the C-terminus of S1 subunit. Recombinant SARS-CoV spike RBD protein fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.