Characterization of SARS-CoV-2 nucleocapsid protein oligomers. Farci, D., Graça, A. T., Hall, M., Haniewicz, P., Kereïche, S., Faull, P., Kirkpatrick, J., Tramontano, E., Schröder, W. P., & Piano, D. Journal of Structural Biology, 217(1):108162, March, 2025. ![Characterization of SARS-CoV-2 nucleocapsid protein oligomers [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Oligomers of the SARS-CoV-2 nucleocapsid (N) protein are characterized by pronounced instability resulting in fast degradation. This property likely relates to two contrasting behaviors of the N protein: genome stabilization through a compact nucleocapsid during cell evasion and genome release by nucleocapsid disassembling during infection. In vivo, the N protein forms rounded complexes of high molecular mass from its interaction with the viral genome. To study the N protein and understand its instability, we analyzed degradation profiles under different conditions by size-exclusion chromatography and characterized samples by mass spectrometry and cryo-electron microscopy. We identified self-cleavage properties of the N protein based on specific Proprotein convertases activities, with Cl- playing a key role in modulating stability and degradation. These findings allowed isolation of a stable oligomeric complex of N, for which we report the 3D structure at ∼6.8 Å resolution. Findings are discussed considering available knowledge about the coronaviruses’ infection cycle.
@article{farci_characterization_2025,
title = {Characterization of {SARS}-{CoV}-2 nucleocapsid protein oligomers},
volume = {217},
issn = {1047-8477},
url = {https://www.sciencedirect.com/science/article/pii/S1047847724001023},
doi = {10.1016/j.jsb.2024.108162},
abstract = {Oligomers of the SARS-CoV-2 nucleocapsid (N) protein are characterized by pronounced instability resulting in fast degradation. This property likely relates to two contrasting behaviors of the N protein: genome stabilization through a compact nucleocapsid during cell evasion and genome release by nucleocapsid disassembling during infection. In vivo, the N protein forms rounded complexes of high molecular mass from its interaction with the viral genome. To study the N protein and understand its instability, we analyzed degradation profiles under different conditions by size-exclusion chromatography and characterized samples by mass spectrometry and cryo-electron microscopy. We identified self-cleavage properties of the N protein based on specific Proprotein convertases activities, with Cl- playing a key role in modulating stability and degradation. These findings allowed isolation of a stable oligomeric complex of N, for which we report the 3D structure at ∼6.8 Å resolution. Findings are discussed considering available knowledge about the coronaviruses’ infection cycle.},
number = {1},
urldate = {2025-01-10},
journal = {Journal of Structural Biology},
author = {Farci, Domenica and Graça, André T. and Hall, Michael and Haniewicz, Patrycja and Kereïche, Sami and Faull, Peter and Kirkpatrick, Joanna and Tramontano, Enzo and Schröder, Wolfgang P. and Piano, Dario},
month = mar,
year = {2025},
keywords = {Covid-19, Cryo-electron microscopy, Furin, Nucleocapsid protein, Proprotein convertases, SARS-CoV-2, Self-cleavage},
pages = {108162},
}
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In vivo, the N protein forms rounded complexes of high molecular mass from its interaction with the viral genome. To study the N protein and understand its instability, we analyzed degradation profiles under different conditions by size-exclusion chromatography and characterized samples by mass spectrometry and cryo-electron microscopy. We identified self-cleavage properties of the N protein based on specific Proprotein convertases activities, with Cl- playing a key role in modulating stability and degradation. These findings allowed isolation of a stable oligomeric complex of N, for which we report the 3D structure at ∼6.8 Å resolution. 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