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Comprehensive Analysis of the Glycan Complement of SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry
[Image: see text] Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to a global pandemic of coronavirus disease 2019 (COVID-19). The spike protein expressed on the surface of this virus is highly glycosylated and plays an essential role during the process of infection. We conducte...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7586457/ https://www.ncbi.nlm.nih.gov/pubmed/33064451 http://dx.doi.org/10.1021/acs.analchem.0c03301 |
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author | Wang, Dongxia Baudys, Jakub Bundy, Jonathan L. Solano, Maria Keppel, Theodore Barr, John R. |
author_facet | Wang, Dongxia Baudys, Jakub Bundy, Jonathan L. Solano, Maria Keppel, Theodore Barr, John R. |
author_sort | Wang, Dongxia |
collection | PubMed |
description | [Image: see text] Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to a global pandemic of coronavirus disease 2019 (COVID-19). The spike protein expressed on the surface of this virus is highly glycosylated and plays an essential role during the process of infection. We conducted a comprehensive mass spectrometric analysis of the N-glycosylation profiles of the SARS-CoV-2 spike proteins using signature ions-triggered electron-transfer/higher-energy collision dissociation (EThcD) mass spectrometry. The patterns of N-glycosylation within the recombinant ectodomain and S1 subunit of the SARS-CoV-2 spike protein were characterized using this approach. Significant variations were observed in the distribution of glycan types as well as the specific individual glycans on the modification sites of the ectodomain and subunit proteins. The relative abundance of sialylated glycans in the S1 subunit compared to the full-length protein could indicate differences in the global structure and function of these two species. In addition, we compared N-glycan profiles of the recombinant spike proteins produced from different expression systems, including human embryonic kidney (HEK 293) cells and Spodoptera frugiperda (SF9) insect cells. These results provide useful information for the study of the interactions of SARS-CoV-2 viral proteins and for the development of effective vaccines and therapeutics. |
format | Online Article Text |
id | pubmed-7586457 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-75864572020-10-29 Comprehensive Analysis of the Glycan Complement of SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry Wang, Dongxia Baudys, Jakub Bundy, Jonathan L. Solano, Maria Keppel, Theodore Barr, John R. Anal Chem [Image: see text] Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to a global pandemic of coronavirus disease 2019 (COVID-19). The spike protein expressed on the surface of this virus is highly glycosylated and plays an essential role during the process of infection. We conducted a comprehensive mass spectrometric analysis of the N-glycosylation profiles of the SARS-CoV-2 spike proteins using signature ions-triggered electron-transfer/higher-energy collision dissociation (EThcD) mass spectrometry. The patterns of N-glycosylation within the recombinant ectodomain and S1 subunit of the SARS-CoV-2 spike protein were characterized using this approach. Significant variations were observed in the distribution of glycan types as well as the specific individual glycans on the modification sites of the ectodomain and subunit proteins. The relative abundance of sialylated glycans in the S1 subunit compared to the full-length protein could indicate differences in the global structure and function of these two species. In addition, we compared N-glycan profiles of the recombinant spike proteins produced from different expression systems, including human embryonic kidney (HEK 293) cells and Spodoptera frugiperda (SF9) insect cells. These results provide useful information for the study of the interactions of SARS-CoV-2 viral proteins and for the development of effective vaccines and therapeutics. American Chemical Society 2020-10-16 2020-11-03 /pmc/articles/PMC7586457/ /pubmed/33064451 http://dx.doi.org/10.1021/acs.analchem.0c03301 Text en © 2020 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Wang, Dongxia Baudys, Jakub Bundy, Jonathan L. Solano, Maria Keppel, Theodore Barr, John R. Comprehensive Analysis of the Glycan Complement of SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry |
title | Comprehensive Analysis of the Glycan Complement of
SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy
Collisional Dissociation (EThcD) Mass Spectrometry |
title_full | Comprehensive Analysis of the Glycan Complement of
SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy
Collisional Dissociation (EThcD) Mass Spectrometry |
title_fullStr | Comprehensive Analysis of the Glycan Complement of
SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy
Collisional Dissociation (EThcD) Mass Spectrometry |
title_full_unstemmed | Comprehensive Analysis of the Glycan Complement of
SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy
Collisional Dissociation (EThcD) Mass Spectrometry |
title_short | Comprehensive Analysis of the Glycan Complement of
SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy
Collisional Dissociation (EThcD) Mass Spectrometry |
title_sort | comprehensive analysis of the glycan complement of
sars-cov-2 spike proteins using signature ions-triggered electron-transfer/higher-energy
collisional dissociation (ethcd) mass spectrometry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7586457/ https://www.ncbi.nlm.nih.gov/pubmed/33064451 http://dx.doi.org/10.1021/acs.analchem.0c03301 |
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