HCoV-NL63 Human Coronavirus Spike RBD 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 RBD

HCoV-NL63, a virus first isolated from a child suffering from respiratory disease in 2003, 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 three viruses that cause relatively mild respiratory disease: HCoV-229E, HCoV-HKU1 and HCov-OC43, plus three viruses that cause the Severe Acute Respiratory Syndrome (SARS-CoV), the Middle East Respirator Syndrome (MERS-CoV), and the global pandemic Covid-19 (SARS-CoV2). HCov-NL63 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. As with most coronaviruses, proteolytic cleavage of the S protein generates two distinct peptides, S1 and S2 subunits. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion.  Although HCoV-NL63 S protein shares high homology (56%) with HCoV-229E, it does not employ CD13 (aminopeptidase N) as the receptor like HCoV-229E. Instead, HCoV-NL63 engages Angiotensin-Converting Enzyme 2 (ACE-2), the same receptor as SARS-CoV and SARS-CoV2, for cellular entry and replication (3). The receptor binding domain (RBD) of HCoV-NL63 is located at C-terminal region of S1 subunit (4, 5). Although NL63-CoV and SARS-CoV do not share structural homology in RBD region, they bind an overlapping region of ACE-2 (6, 7).

Product Datasheets

Related Research Areas

• Infectious Diseases