MERS-CoV Spike S1 Subunit Alexa Fluor® 647-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 S1 Subunit

MERS-CoV (also known as HCoV-EMC), which causes the Middle East Respiratory Syndrome (MERS), belongs to a family of viruses known as coronaviruses that are commonly comprised of a large plus-strand RNA genome and four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1,2). Other well-known human coronaviruses include several viruses that cause relatively mild respiratory disease, plus two viruses that caused the Severe Acute Respiratory Syndrome (SARS-CoV) and the global pandemic Covid-19 (SARS-CoV2). MERS-CoV Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry, and it consists of two subunits, S1 and S2. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3). Based on amino acid (aa) sequence homology, the MERS-CoV S1 subunit shares 23% and 22% identity with SARS-CoV S1 subunit and SARS-Cov2 S1 subunit, respectively. The low aa sequence homology is consistent with the finding that MERS-CoV and SARS-CoV bind different cellular receptors (4). Unlike SARS-CoV and SARS-CoV2, which engage ACE2 as their receptors for cell entry, MERS-CoV employs Dipeptidyl Peptidase 4 (DPP4; also known as CD26) as its functional receptor (4). Based on structural biology studies, the receptor binding domain (RBD) of MERS-CoV spike protein is located in the C-terminal region of S1 subunit and consists of a core subdomain and a receptor-binding subdomain (5, 6). The S1 subunit, especially the RBD region, was commonly targeted for vaccinations or antiviral therapy against MERS (7-9).

Product Datasheets

Related Research Areas

• Infectious Diseases