Lisää artikkeleita ja viitteitä SARS-2 Spike glykosylaatioista

https://www.acrobiosystems.com/A1117-The-Art-of-glycosylation-of-SARS-CoV-2-S-Protein.html

3.  Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2^[3]

Azadi’s team from the University of Georgia published their work on bioRxiv. They digested the recombinant SARS-CoV-2 subunit S1 and S2 expressed in HEK293 cells into the glycopeptides. After that, high resolution LC-MS/MS was used to analyze these glycopeptides. In this way, they identified partial N-glycan occupancy on 17 out of 22 N-glycosylation sites with a combination of high mannose and complex type, but no hybrid-type glycans (Figure 5). Interestingly, they observed two unexpected O-glycosylation modifications on the receptor binding domain (RBD) of spike protein subunit S1. Even though O-glycosylation has been predicted on the spike protein of SARS-Cov-2, this is the first report of the site of O-glycosylation and identity of the O-glycans attached on the subunit S1. 

https://www.acrobiosystems.com/images/upload/20200414/1586865449960750.png

Reference: 

1. Yasunori Watanabe et al. Site-specific analysis of the SARS-CoV-2 glycan shield. bioRxiv preprint doi: https://doi.org/10.1101/2020.03.26.010322
2. Yong Zhang et al. Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins using High-Resolution Mass Spectrometry. bioRxiv preprint doi: https://doi.org/10.1101/2020.03.28.013276.  
3. Asif Shajahan et al. Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2. bioRxiv preprint doi: https://doi.org/10.1101/2020.04.01.020966.
4. Dora Pinto et al. Structural and functional analysis of a potent sarbecovirus neutralizing antibody. bioRxiv preprint doi: https://doi.org/10.1101/2020.04.07.023903.
5. Oliver C. Grant et al. 3D Models of glycosylated SARS-CoV-2 spike protein suggest challenges and opportunities for vaccine development. bioRxiv preprint doi: http://biorxiv.org/cgi/content/short/2020.04.07.030445.

6. https://www.who.int/emergencies/diseases/novel-coronavirus-2019/situation-reports/

7. Walls et al., Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein, Cell (2020).

8. Walls, A.C. et al. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nat. Struct. Mol. Biol. 23, 899–905. (2016).

9. Walls, A.C. et al. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc. Natl. Acad. Sci. USA 114, 11157–11162. (2017).

ACROBiosystems has developed various SARS-CoV-2 proteins based on their HEK293 protein expression platform. The state of their mammalian cell expressed recombinant proteins is closer to that of the protein in human including the glycosylation level.