SARS-CoV-2 Spike (S) glycoprotein
Spike (S) glycoprotein corresponds to one of the leading targets for COVID-19 disease. Present on the surface of Sars-CoV-2 virus, Spike S protein is a class I fusion protein that allows the virus to enter host cells.
With a 1 273 aa length, Spike protein has 2 subunits : S1 contains the receptor-binding domain RBD and S2 induces the fusion of the viral envelop with the cellular membrane. The S1 subunit allows binding to the Angiotensin-Converting Enzyme receptor 2 (ACE2 receptor) which mediates the viral entry.
Available peptide libraries
Some proteins of Sars-CoV-2 are identified as leading targets for COVID-19 therapies. sb-PEPTIDE offers pre-made peptide libraries of Spike protein and can synthesize specific libraries upon request.
Spike (S) protein – peptide library reference #SB043
Spike (S) is a glycoprotein of 1 273 aa length. sb-PEPTIDE offers a library made of 316 peptides with a length of 15 amino acids and an overlap of 11 amino acids without post-translational modificaton.
Spike (S) protein – biotinylated peptide library reference #SB043-biotin
The above Sipke (S) protein library is also available with N-ter biotin.
Variants package of SARS CoV-2 Spike (S) protein mutation – peptide library reference #SB072
|Peptides length : 15 aa|
|Offset number : 11 aa|
|Amount : 0,5mg or 5*0,5mg (for each peptide)|
|Quality : Crude, 100% LC-MS|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Lyophilized or in solution, in 96-well plate or microtubes|
|Price : Ask for your quote|
|Peptide Solubility Guideline|
1- Ou, X., Liu, Y., Lei, X. et al. Nat Commun 11, 1620 (2020)
Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV
Since 2002, beta coronaviruses (CoV) have caused three zoonotic outbreaks, SARS-CoV in 2002–2003, MERS-CoV in 2012, and the newly emerged SARS-CoV-2 in late 2019. However, little is currently known about the biology of SARS-CoV-2. Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. Polyclonal anti-SARS S1 antibodies T62 inhibit entry of SARS-CoV S but not SARS-CoV-2 S pseudovirions. Further studies using recovered SARS and COVID-19 patients’ sera show limited cross-neutralization, suggesting that recovery from one infection might not protect against the other. Our results present potential targets for development of drugs and vaccines for SARS-CoV-2.
2- Yasunori W et al. Science (2020)
SARS-CoV-2 spike protein, elaborated
Vaccine development for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the trimeric spike protein that initiates infection. Each protomer in the trimeric spike has 22 glycosylation sites. How these sites are glycosylated may affect which cells the virus can infect and could shield some epitopes from antibody neutralization. Watanabe et al. expressed and purified recombinant glycosylated spike trimers, proteolysed them to yield glycopeptides containing a single glycan, and determined the composition of the glycan sites by mass spectrometry. The analysis provides a benchmark that can be used to measure antigen quality as vaccines and antibody tests are developed.
Science this issue p. 330
The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design.
3- Alexandra C. Walls et al. Cell (2020)
The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.