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10.1038/s41598-020-71748-7

http://scihub22266oqcxt.onion/10.1038/s41598-020-71748-7
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suck abstract from ncbi


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pmid32929138      Sci+Rep 2020 ; 10 (1): 14991
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  • Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition #MMPMID32929138
  • Grant OC; Montgomery D; Ito K; Woods RJ
  • Sci Rep 2020[Sep]; 10 (1): 14991 PMID32929138show ga
  • Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identified peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the innate and adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight of the S trimer (17% for the HEK293 glycoform) they shield approximately 40% of the protein surface.
  • |Adaptive Immunity[MESH]
  • |Amino Acid Sequence[MESH]
  • |Angiotensin-Converting Enzyme 2[MESH]
  • |Antibodies, Neutralizing/immunology[MESH]
  • |Antigen-Antibody Complex[MESH]
  • |Betacoronavirus/immunology/isolation & purification/*metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/immunology/*pathology/virology[MESH]
  • |Glycosylation[MESH]
  • |HEK293 Cells[MESH]
  • |HLA Antigens/metabolism[MESH]
  • |Humans[MESH]
  • |Immunity, Innate[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Pandemics[MESH]
  • |Peptidyl-Dipeptidase A/chemistry/metabolism[MESH]
  • |Pneumonia, Viral/immunology/*pathology/virology[MESH]
  • |Polysaccharides/*chemistry[MESH]
  • |Protein Binding[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |SARS-CoV-2[MESH]
  • |Sequence Alignment[MESH]


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