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?:abstract
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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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?:doi
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10.1101/2020.11.30.404905
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?:doi
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?:journal
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?:pdf_json_files
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document_parses/pdf_json/8823df56ffee2c6aeff0c0bf2c24f85f216ef455.json; document_parses/pdf_json/e50f46387be14295d057cf924e664eebe1250e5c.json
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document_parses/pmc_json/PMC7709165.xml.json
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?:pmid
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?:source
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BioRxiv; Medline; PMC; WHO
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?:title
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Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain
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