SARS CORONAVIRUS SPIKE GLYCOPROTEIN MOSAIC (S1)
SARS Coronavirus Spike Glycoprotein Mosaic (S1) is a recombinant antigen which contains the N-terminal section of the Spike protein 12-53, 90-115, 171-203 amino acids immunodominant regions. It is manufactured in E. coli with greater than 95% purity.
- SARS Coronavirus Spike Glycoprotein Mosaic (S1).
- Recombinant protein manufactured in E. coli.
- Contains N-terminus of the Spike protein 12-53, 90-115, 171-203 amino acid immunodominant regions.
- Purity >95% as determined by 10% PAGE (Coomassie staining).
- For use in ELISA and other immunoassays.
Coronaviruses are a family of large, enveloped, positive-stranded RNA viruses that cause upper respiratory, gastrointestinal and central nervous system diseases in humans and other animals (Gallagher and Buchmeier, 2001). Human coronaviruses (HCoV-OC43, HCoV-229E, HCoV-NL63 and HCoV-HKU1) circulate in humans and cause mild respiratory diseases (Su et al., 2016). However, the outbreak of SARS-CoV in 2002 and MERS-CoV in 2012 showed that coronaviruses can cross the species barrier and emerge as highly pathogenic viruses (Lu et al., 2015). The high fatality rate and wide spread of SARS-CoV and MERS-CoV confirmed that they are a severe threat to global health.
The coronavirus spike (S) glycoprotein is a class I viral fusion protein on the outer envelope of the virion that plays a critical role in viral infection by recognizing host cell receptors and mediating fusion of the viral and cellular membranes (Li, 2016). The coronavirus S glycoprotein is synthesized as a precursor protein consisting of ~1,300 amino acids that is then cleaved into an amino (N)-terminal S1 subunit (~700 amino acids) and a carboxyl (C)-terminal S2 subunit (~600 amino acids). Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. Triggered by receptor binding, proteolytic processing and/or acidic pH in the cellular compartments, the class I viral fusion protein undergoes a transition from a metastable prefusion state to a stable postfusion state during infection, in which the receptor-binding subunit is cleaved, and the fusion subunit undergoes large-scale conformational rearrangements to expose the hydrophobic fusion peptide, induce the formation of a six-helix bundle, and bring the viral and cellular membranes close for fusion (Belouzard et al., 2012). The trimeric SARS coronavirus (SARS-CoV) S glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition (Song et al., 2018).
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