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TitleCharacterization of SARS-CoV-2 nucleocapsid protein oligomers.
Journal, issue, pagesJ Struct Biol, Vol. 217, Issue 1, Page 108162, Year 2025
Publish dateDec 13, 2024
AuthorsDomenica Farci / André T Graça / Michael Hall / Patrycja Haniewicz / Sami Kereïche / Peter Faull / Joanna Kirkpatrick / Enzo Tramontano / Wolfgang P Schröder / Dario Piano /
PubMed AbstractOligomers 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 ...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.
External linksJ Struct Biol / PubMed:39675446
MethodsEM (single particle)
Resolution4.5 - 6.8 Å
Structure data

EMDB-16868: Nucleocapsid protein Sars-Cov2, refined map
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-17430: Nucleocapsid protein Sars-Cov2
Method: EM (single particle) / Resolution: 6.8 Å

Source
  • Severe acute respiratory syndrome coronavirus 2

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