Protein is >95% pure as determined by 10% PAGE (coomassie staining).
The spike (S) protein is a key structural component of coronaviruses, including SARS-CoV (Severe Acute Respiratory Syndrome Coronavirus) and MERS-CoV (Middle East Respiratory Syndrome Coronavirus). The spike protein facilitates viral entry into host cells and is a primary target for vaccine and therapeutic development. The S1 subunit of the spike protein contains the receptor-binding domain (RBD), which is crucial for binding to host cell receptors.
The spike protein is a trimeric class I fusion protein, consisting of two subunits: S1 and S2. The S1 subunit is responsible for receptor binding, while the S2 subunit mediates membrane fusion. The S1 subunit contains the N-terminal domain (NTD) and the receptor-binding domain (RBD). The RBD is particularly important as it determines the host range and tissue tropism of the virus by binding to specific receptors on host cells.
For SARS-CoV, the RBD in the S1 subunit binds to the angiotensin-converting enzyme 2 (ACE2) receptor on human cells. Similarly, the MERS-CoV spike protein binds to the dipeptidyl peptidase 4 (DPP4) receptor. These interactions are critical for viral entry and subsequent infection.
Recombinant spike S1 proteins are produced using various expression systems, such as HEK293 cells, to study their structure, function, and immunogenicity. These recombinant proteins are used in research to understand the mechanisms of viral entry, develop vaccines, and design therapeutic interventions.
For instance, the recombinant SARS-CoV-2 spike S1 protein is expressed with a polyhistidine tag at the C-terminus, facilitating purification and detection. The recombinant protein is typically purified to high purity levels (>90% by SDS-PAGE and >95% by SEC-HPLC) and is tested for its binding ability to the ACE2 receptor .
Recombinant spike S1 proteins are invaluable tools in virology and immunology research. They are used in: