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Description

Spike glycoprotein (UniProt: P0DTC2, also known as S glycoprotein, E2, Peplomer protein) is encoded by the S (also known as 2) gene (Gene ID: 43740568) in Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The SARS-CoV-2 is a positive-strand RNA virus that causes severe respiratory syndrome in human. The mature SARS-CoV-2 contains 4 structural proteins: Envelope (E), Membrane (M), Nucleocapsid (N), and the Spike protein (S). E and M proteins help in viral assembly and N protein is needed for RNA synthesis. The S protein is a single-pass type I, homotrimeric, membrane glycoprotein that is responsible for virus binding and entry into host cell. It is synthesized with a signal peptide (aa 1-12), which is subsequently cleaved off to generate the mature protein that contains an extracellular domain (aa 13-1213), a transmembrane domain (aa 1214-1234), and a cytoplasmic domain 1235-1273). The S protein is further processed into S1 (aa 13-685) and S2 (aa 686-1273) subunits by host cell furin. The presence of a furin polybasic cleavage site in S protein from SARS-CoV-2 sets it apart from S protein in SARS-CoV that possesses a monobasic S1/S2 cleavage site. The S1 subunit has the receptor binding domain (RBD, aa 319-541) that mediates entry of SARS-CoV-2 into sensitive cells through the peptidase domain of host Angiotensin-converting enzyme 2 (ACE2) with high affinity (KD = 15 nM). The S2 domain (aa 686-1213), which is reported to be well conserved, is responsible for membrane fusion. Clone R52 can detect both native spike protein expressed in HEK293T cells and the artificial spike glycoprotein carrying T4 foldon. It recognizes a continuous epitope in amino acids 549-568 of spike protein receptor binding domain. (Ref.: Guo, Y., et al. (2021). J. Biol. Chem. 296, 100346).