Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain
Summary Nucleocapsid protein (N) is the most abundant viral protein encoded by SARS-CoV-2, the causative agent of COVID-19. N plays key roles at different steps in the replication cycle and is used as a serological marker of infection. Here we characterize the biochemical properties of SARS-CoV-2 N. We define the N domains important for oligomerization and RNA binding that are associated with spherical droplet formation and suggest that N accessibility and assembly may be regulated by phosphorylation. We also map the RNA binding interface using hydrogen-deuterium exchange mass spectrometry. Finally, we find that the N protein C-terminal domain is the most immunogenic by sensitivity, based upon antibody binding to COVID-19 patient samples from the US and Hong Kong. Together, these findings uncover domain-specific insights into the significance of SARS-CoV-2 N and highlight the diagnostic value of using N domains as highly specific and sensitive markers of COVID-19..
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Preprint| Erscheinungsjahr: |
2022 |
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| Erschienen: |
2022 |
| Enthalten in: |
bioRxiv.org - (2022) vom: 01. Dez. Zur Gesamtaufnahme - year:2022 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Wu, Chao [VerfasserIn] |
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| doi: |
10.1101/2020.11.30.404905 |
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| PPN (Katalog-ID): |
XBI019434537 |
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| 245 | 1 | 0 | |a Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain |
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| 520 | |a Summary Nucleocapsid protein (N) is the most abundant viral protein encoded by SARS-CoV-2, the causative agent of COVID-19. N plays key roles at different steps in the replication cycle and is used as a serological marker of infection. Here we characterize the biochemical properties of SARS-CoV-2 N. We define the N domains important for oligomerization and RNA binding that are associated with spherical droplet formation and suggest that N accessibility and assembly may be regulated by phosphorylation. We also map the RNA binding interface using hydrogen-deuterium exchange mass spectrometry. Finally, we find that the N protein C-terminal domain is the most immunogenic by sensitivity, based upon antibody binding to COVID-19 patient samples from the US and Hong Kong. Together, these findings uncover domain-specific insights into the significance of SARS-CoV-2 N and highlight the diagnostic value of using N domains as highly specific and sensitive markers of COVID-19. | ||
| 650 | 4 | |a Biology |7 (dpeaa)DE-84 | |
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| 700 | 1 | |a Qavi, Abraham J. |e verfasserin |4 aut | |
| 700 | 1 | |a Hachim, Asmaa |e verfasserin |4 aut | |
| 700 | 1 | |a Kavian, Niloufar |e verfasserin |4 aut | |
| 700 | 1 | |a Cole, Aidan R. |e verfasserin |4 aut | |
| 700 | 1 | |a Moyle, Austin B. |e verfasserin |4 aut | |
| 700 | 1 | |a Wagner, Nicole D. |e verfasserin |4 aut | |
| 700 | 1 | |a Sweeney-Gibbons, Joyce |e verfasserin |4 aut | |
| 700 | 1 | |a Rohrs, Henry W. |e verfasserin |4 aut | |
| 700 | 1 | |a Gross, Michael L. |e verfasserin |4 aut | |
| 700 | 1 | |a Peiris, J. S. Malik |e verfasserin |4 aut | |
| 700 | 1 | |a Basler, Christopher F. |e verfasserin |4 aut | |
| 700 | 1 | |a Farnsworth, Christopher W. |e verfasserin |4 aut | |
| 700 | 1 | |a Valkenburg, Sophie A. |e verfasserin |4 aut | |
| 700 | 1 | |a Amarasinghe, Gaya K. |e verfasserin |4 aut | |
| 700 | 1 | |a Leung, Daisy W. |e verfasserin |4 aut | |
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