Recombinant SARS-CoV-2 20A.EU1 S1 Subunit His Protein, CF

Recombinant SARS-CoV-2 20A.EU1 S1 Subunit His Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Spike S1 Subunit

SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein(S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1). SARS-CoV-2 Spike Protein (S Protein) is a homotrimeric glycoprotein that mediates membrane fusion and viral entry. As with most coronaviruses, proteolytic cleavage of the SARS-CoV-2 S protein into two distinct peptides, S1 and S2 subunits, is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (2-5). A SARS-CoV-2 variant (named 20A.EU1) carrying the S1 subunit amino acid (aa) change A222V and D614G emerged presumably in Spain and subsequently spread to multiple locations in Europe (6,7). Based on structural biology studies, the receptor binding domain (RBD), located in the C-terminal region of S1, can be oriented either in the up/standing or down/lying state (8). The standing state is associated with higher pathogenicity and both SARS-CoV-1 and MERS can access this state due to the flexibility in their respective RBDs. A similar two-state structure and flexibility is found in the SARS-CoV-2 RBD (9). Based on amino acid (aa) sequence homology, the SARS-CoV-2 S1 subunit has 65% identity with SARS-CoV-1 S1 subunit, but only 22% homology with the MERS S1 subunit. The low aa sequence homology is consistent with the finding that SARS and MERS bind different cellular receptors (10). The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds Angiotensin-Converting Enzyme 2 (ACE-2), but with much higher affinity and faster binding kinetics (11). Before binding to the ACE-2 receptor, structural analysis of the S1 trimer shows that only one of the three RBD domains in the trimeric structure is in the "up" conformation. This is an unstable and transient state that passes between trimeric subunits but is nevertheless an exposed state to be targeted for neutralizing antibody therapy (12). Polyclonal antibodies to the RBD of the SARS-CoV-2 S1 subunit have been shown to inhibit interaction with the ACE-2 receptor, confirming S1 subunit especially the RBD as an attractive target for vaccinations or antiviral therapy (13). There is also promising work showing that the RBD may be used to detect presence of neutralizing antibodies present in a patient's bloodstream, consistent with developed immunity after exposure to the SARS-CoV-2 virus (14). Lastly, it has been demonstrated the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (15, 16).

Related Research Areas

• Infectious Diseases