The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Copyright © 2020 Elsevier Inc. All rights reserved..
The spike protein of SARS-CoV-2 has been undergoing mutations and is highly glycosylated. It is critically important to investigate the biological significance of these mutations. Here, we investigated 80 variants and 26 glycosylation site modifications for the infectivity and reactivity to a panel of neutralizing antibodies and sera from convalescent patients. D614G, along with several variants containing both D614G and another amino acid change, were significantly more infectious. Most variants with amino acid change at receptor binding domain were less infectious, but variants including A475V, L452R, V483A, and F490L became resistant to some neutralizing antibodies. Moreover, the majority of glycosylation deletions were less infectious, whereas deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of glycosylation for viral infectivity. Interestingly, N234Q was markedly resistant to neutralizing antibodies, whereas N165Q became more sensitive. These findings could be of value in the development of vaccine and therapeutic antibodies.
| Errataetall: |
CommentIn: Signal Transduct Target Ther. 2020 Sep 3;5(1):185. - PMID 32883949 |
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:182 |
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| Enthalten in: |
Cell - 182(2020), 5 vom: 03. Sept., Seite 1284-1294.e9 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Li, Qianqian [VerfasserIn] |
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| Links: |
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| Themen: |
Antigens, Viral |
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| Anmerkungen: |
Date Completed 17.09.2020 Date Revised 31.03.2024 published: Print-Electronic CommentIn: Signal Transduct Target Ther. 2020 Sep 3;5(1):185. - PMID 32883949 Citation Status MEDLINE |
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| doi: |
10.1016/j.cell.2020.07.012 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM313063605 |
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| 520 | |a Copyright © 2020 Elsevier Inc. All rights reserved. | ||
| 520 | |a The spike protein of SARS-CoV-2 has been undergoing mutations and is highly glycosylated. It is critically important to investigate the biological significance of these mutations. Here, we investigated 80 variants and 26 glycosylation site modifications for the infectivity and reactivity to a panel of neutralizing antibodies and sera from convalescent patients. D614G, along with several variants containing both D614G and another amino acid change, were significantly more infectious. Most variants with amino acid change at receptor binding domain were less infectious, but variants including A475V, L452R, V483A, and F490L became resistant to some neutralizing antibodies. Moreover, the majority of glycosylation deletions were less infectious, whereas deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of glycosylation for viral infectivity. Interestingly, N234Q was markedly resistant to neutralizing antibodies, whereas N165Q became more sensitive. These findings could be of value in the development of vaccine and therapeutic antibodies | ||
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| 700 | 1 | |a Zhao, Chenyan |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Qi |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Huan |e verfasserin |4 aut | |
| 700 | 1 | |a Nie, Lingling |e verfasserin |4 aut | |
| 700 | 1 | |a Qin, Haiyang |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Meng |e verfasserin |4 aut | |
| 700 | 1 | |a Lu, Qiong |e verfasserin |4 aut | |
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| 700 | 1 | |a Huang, Weijin |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Youchun |e verfasserin |4 aut | |
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