SDS-PAGE: Coomassie-stained SDS-PAGE showing purified protein.
SARS-CoV-2 Spike Glycoprotein (S2) (aa 800-1000), His-Tag (E. coli)
$563.24 – $2,113.43 excl. VAT
SARS-CoV-2 Spike Glycoprotein (S2) is a recombinant antigen manufactured in E. coli and containing the Spike subunit 2 immunodominant region (amino acids 800 to 1000). SARS-CoV-2, previously known as the 2019 Novel Coronavirus (2019-nCoV), causes the pandemic COVID-19 disease.
SARS-COV-2 SPIKE GLYCOPROTEIN (S2) (AA 800-1000)
SARS-CoV-2 Spike Glycoprotein (S2) is a recombinant antigen manufactured in E. coli and containing the Spike immunodominant region (amino acids 800 to 1000).
PRODUCT DETAILS – SARS-COV-2 SPIKE GLYCOPROTEIN (S2) (AA 800-1000)
- SARS-CoV-2 Spike Glycoprotein (S2), Wuhan-Hu-1 strain.
- Recombinant protein manufactured in E. coli cells and purified to >90% purity.
- Contains Spike protein amino acids 800-1000, with C-term 6xHis-tag.
- Presented in PBS.
In late December, 2019, a number of patients with viral pneumonia (now called 2019-nCoV acute respiratory disease) were found to be epidemiologically associated with the Huanan seafood market in Wuhan, in the Hubei province of China. A novel, human-infecting coronavirus, provisionally named 2019 Novel Coronavirus (2019-nCoV) and since named SARS-CoV-2, was identified by genomic sequencing (Lu et al., 2020). SARS-CoV-2 is closely related (88% identity) to two bat-derived severe acute respiratory syndrome (SARS)-like coronaviruses, collected in 2018 in Zhoushan, eastern China, but were more distant from SARS-CoV (~79% identity) and MERS-CoV (~50% identity). However, although bats might be the original host of this virus, an animal sold at the seafood market in Wuhan may have acted as an intermediate host (Lu et al., 2020). Relative synonymous codon usage (RSCU) analysis suggests that SARS-CoV-2 is a recombinant between the bat coronavirus and an origin-unknown coronavirus, and it has been proposed that a snake could have acted as the reservoir. The recombination event occurred within the viral spike glycoprotein (Ji et al., 2020). Homology modelling shows that SARS-CoV-2 has a similar receptor-binding domain structure to that of SARS-CoV, despite amino acid variation at some key residues. Therefore, SARS-CoV-2 may be able to bind to the angiotensin-converting enzyme 2 (ACE2) receptor in humans (Lu et al., 2020).
SARS-CoV-2 is a respiratory virus which causes coronavirus disease 2019 (COVID-19); it spreads primarily through contact with an infected person through respiratory droplets generated when a person coughs or sneezes, or through droplets of saliva or discharge from the nose. The incubation period is believed to range from 2-11 days. Infection with SARS-CoV-2 can cause mild symptoms including a runny nose, sore throat, cough, and fever. However, it can be more severe for some people and can lead to pneumonia or breathing difficulties. The elderly, and people with pre-existing medical conditions (such as, diabetes and heart disease) appear to be more vulnerable to becoming severely ill with the virus. There are currently more than 40,000 confirmed cases from 24 countries, although the vast majority are still within China, with more than 900 deaths to date (WHO, 2020).
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 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).
- Gallagher and Buchmeier (2001). Coronavirus spike proteins in viral entry and pathogenesis. Virology. 279(2):371-4.
- Ji et al. (2020). Homologous recombination within the spike glycoprotein of the newly identified coronavirus may boost cross-species transmission from snake to human. J Med Virol. 2020;10.1002/jmv.25682. doi:10.1002/jmv.25682.Li F. (2016). Structure, Function, and Evolution of Coronavirus Spike Proteins. Annu Rev Virol. 3(1):237-261.
- Lu et al. (2015). Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond. Trends Microbiol. 23(8):468–78.
- Lu R, Zhao X, Li J, et al. (2020). Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet. S0140-6736(20)30251-8. doi:10.1016/S0140-6736(20)30251-8.
- Novel coronavirus (2019-nCoV), World health Organisation (WHO), 2020.
- Schoeman D, Fielding BC. Coronavirus envelope protein: current knowledge. Virol J. 2019;16(1):69.
- Siu YL, Teoh KT, Lo J, et al. (2019). The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles. J Virol. 2008;82(22):11318–11330.
- Su et al. (2016). Epidemiology, Genetic Recombination, and Pathogenesis of Coronaviruses. Trends Microbiol. 2016 Jun; 24(6):490-502.