N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry
© 2021. The Author(s)..
N-glycosylation plays an important role in the structure and function of membrane and secreted proteins. The spike protein on the surface of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is heavily glycosylated and the major target for developing vaccines, therapeutic drugs and diagnostic tests. The first major SARS-CoV-2 variant carries a D614G substitution in the spike (S-D614G) that has been associated with altered conformation, enhanced ACE2 binding, and increased infectivity and transmission. In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. The data showed that half of the N-glycosylation sequons changed their distribution of glycans in the S-614G variant. The S-614G variant showed a decrease in the relative abundance of complex-type glycans (up to 45%) and an increase in oligomannose glycans (up to 33%) on all altered sequons. These changes led to a reduction in the overall complexity of the total N-glycosylation profile. All the glycosylation sites with altered patterns were in the spike head while the glycosylation of three sites in the stalk remained unchanged between S-614G and S-614D proteins.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:11 |
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| Enthalten in: |
Scientific reports - 11(2021), 1 vom: 07. Dez., Seite 23561 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Wang, Dongxia [VerfasserIn] |
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| Links: |
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| Themen: |
Angiotensin-Converting Enzyme 2 |
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| Anmerkungen: |
Date Completed 15.12.2021 Date Revised 13.09.2022 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1038/s41598-021-02904-w |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 100 | 1 | |a Wang, Dongxia |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry |
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| 520 | |a © 2021. The Author(s). | ||
| 520 | |a N-glycosylation plays an important role in the structure and function of membrane and secreted proteins. The spike protein on the surface of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is heavily glycosylated and the major target for developing vaccines, therapeutic drugs and diagnostic tests. The first major SARS-CoV-2 variant carries a D614G substitution in the spike (S-D614G) that has been associated with altered conformation, enhanced ACE2 binding, and increased infectivity and transmission. In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. The data showed that half of the N-glycosylation sequons changed their distribution of glycans in the S-614G variant. The S-614G variant showed a decrease in the relative abundance of complex-type glycans (up to 45%) and an increase in oligomannose glycans (up to 33%) on all altered sequons. These changes led to a reduction in the overall complexity of the total N-glycosylation profile. All the glycosylation sites with altered patterns were in the spike head while the glycosylation of three sites in the stalk remained unchanged between S-614G and S-614D proteins | ||
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| 700 | 1 | |a Keppel, Theodore R |e verfasserin |4 aut | |
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| 700 | 1 | |a Baudys, Jakub |e verfasserin |4 aut | |
| 700 | 1 | |a Goldstein, Jason |e verfasserin |4 aut | |
| 700 | 1 | |a Finn, M G |e verfasserin |4 aut | |
| 700 | 1 | |a Fan, Xiaoyu |e verfasserin |4 aut | |
| 700 | 1 | |a Chapman, Asheley P |e verfasserin |4 aut | |
| 700 | 1 | |a Bundy, Jonathan L |e verfasserin |4 aut | |
| 700 | 1 | |a Woolfitt, Adrian R |e verfasserin |4 aut | |
| 700 | 1 | |a Osman, Sarah H |e verfasserin |4 aut | |
| 700 | 1 | |a Pirkle, James L |e verfasserin |4 aut | |
| 700 | 1 | |a Wentworth, David E |e verfasserin |4 aut | |
| 700 | 1 | |a Barr, John R |e verfasserin |4 aut | |
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