Selected article for: "affinity receptor and SARS cov"
Author: Asif Shajahan; Nitin T. Supekar; Anne S. Gleinich; Parastoo Azadi
Title: Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2
  • Document date: 2020_4_3
    • ID: f0xsisdg_25
    Snippet: Although it is unclear what function these predicted O-linked glycans perform, they have been suggested to create a 'mucin-like domain' which could shield SARS-CoV-2 spike protein epitopes or key residues (Bagdonaite, I. and Wandall, H.H. 2018) . Since some viruses can utilize mucin- The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.01.020966 doi: bioRxiv preprint extensive polar residue.....
    Document: Although it is unclear what function these predicted O-linked glycans perform, they have been suggested to create a 'mucin-like domain' which could shield SARS-CoV-2 spike protein epitopes or key residues (Bagdonaite, I. and Wandall, H.H. 2018) . Since some viruses can utilize mucin- The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.01.020966 doi: bioRxiv preprint extensive polar residue interactions between RBD and the peptidase domain of hACE2 (Hoffmann, M., Kleine-Weber, H., et al. 2020 , Walls, A.C., Park, Y.J., et al. 2020 ). The S protein RBD located in the S1 subunit of SARS-CoV-2 undergoes a hinge-like dynamic movement to enhance the capture of the receptor RBD with hACE2, displaying 10-20-fold higher affinity for the human ACE2 receptor than SARS-CoV-1, which partially explains the higher transmissibility of the new virus (Wrapp, D., Wang, N., et al. 2020 , Yan, R., Zhang, Y., et al. 2020 ). The residues Thr323 and Ser325 are located at the RBD of the S1 subunit of SARS-Cov-2, and thus the Oglycosylation at this location could play a critical role in viral binding with hACE2 receptors The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.01.020966 doi: bioRxiv preprint therapeutic possibilities, as well as in the design of suitable immunogens for vaccine development.

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