SARS-CoV-2 Spike RBD Alexa Fluor® 532-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Spike RBD

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 glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 (2). In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into the 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 (3-5). The S1 protein of SARS-CoV-2 shares 65% and 22% amino acid (aa) sequence identity with the S1 protein of SARS-CoV-1 and MERS, respectively. The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and faster binding kinetics through the receptor binding domain (RBD) located in the C-terminal region of S1 (6). Based on structural biology studies, the RBD can be oriented either in the up/standing or down/lying state with the up/standing state associated with higher pathogenicity (7). Polyclonal antibodies to the RBD of the SARS-CoV-2 S1 protein have been shown to inhibit interaction with the ACE2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (8). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (9, 10). A SARS-CoV-2 variant (named 20A.EU2) carrying the S1 subunit amino acid (aa) change S477N and D614G emerged presumably in France and becomes the second most common variant in western Europe (11).

Product Datasheets

Related Research Areas

• Infectious Diseases