Titration curves for SARS-CoV-2 Spike Protein (CR3022) Human IgG1 mAb bound to recombinant SARS-CoV-2 spike proteins in ELISA. ELISA plates were coated with one of the following recombinant proteins: SARS-CoV-2 Spike (trimeric) (16-1208) Recombinant Protein (8xHis-Tag) #65444, SARS-CoV-2 Spike RBD (318-541) Recombinant Protein (8xHis-Tag) #48801, or SARS-CoV-2 Spike S1-NTD (16-316) Recombinant Protein (8xHis-Tag) #88587. Anti-Human IgG, Fc gamma Fragment Specific, HRP-Linked Antibody #32935 was added to recognize bound SARS-CoV-2 Spike Protein (CR3022) Human IgG1 mAb. Values on the y-axis indicate absorbance measured at 450 nm.
Supplied in PBS solution (pH 7.2). Store at –20°C. Avoid repeated freeze-thaw cycles.
SARS-CoV-2 Spike Protein (CR3022) Human IgG1 mAb recognizes an epitope in the receptor binding domains (RBDs) of SARS-CoV-2 and SARS-CoV spike proteins. SARS-CoV-2 Spike Protein (CR3022) Human IgG1 mAb has been reported to bind to both wild-type and P462L-mutant versions of the SARS spike protein. The epitope is only accessible in the "open" conformation of the spike protein (10,11).
Monoclonal antibody was derived from a monoclonal antibody generated semi-synthetically from a patient infected with SARS-CoV (12).
The cause of the COVID-19 pandemic is a novel and highly pathogenic coronavirus, termed SARS-CoV-2 (severe acute respiratory syndrome coronavirus-2). SARS-CoV-2 is a member of the Coronaviridae family of viruses (1). The genome of SARS-CoV-2 is similar to other coronaviruses, and is comprised of four key structural proteins: S, the spike protein, E, the envelope protein, M, the membrane protein, and N, the nucleocapsid protein (2). Coronavirus spike proteins are class I fusion proteins and harbor an ectodomain, a transmembrane domain, and an intracellular tail (3,4). The highly glycosylated ectodomain projects from the viral envelope surface and facilitates attachment and fusion with the host cell plasma membrane. The ectodomain can be further subdivided into host receptor-binding domain (RBD) (S1) and membrane-fusion (S2) subunits, which are produced upon proteolysis by host proteases at S1/S2 and S2’ sites. S1 and S2 subunits remain associated after cleavage and assemble into crown-like homotrimers (2,4). In humans, both SARS-CoV and SARS-CoV-2 spike proteins utilize the angiotensin-converting enzyme 2 (ACE2) protein as a receptor for cellular entry (5-7). Spike protein subunits represent a key antigenic feature of coronavirus virions, and therefore represent an important target of vaccines, novel therapeutic antibodies, and small-molecule inhibitors (8,9).
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