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Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain.
Wu, Chao; Qavi, Abraham J; Hachim, Asmaa; Kavian, Niloufar; Cole, Aidan R; Moyle, Austin B; Wagner, Nicole D; Sweeney-Gibbons, Joyce; Rohrs, Henry W; Gross, Michael L; Peiris, J S Malik; Basler, Christopher F; Farnsworth, Christopher W; Valkenburg, Sophie A; Amarasinghe, Gaya K; Leung, Daisy W.
  • Wu C; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Qavi AJ; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Hachim A; HKU-Pasteur Research Pole, School of Public Health, The University of Hong Kong, Hong Kong, China.
  • Kavian N; HKU-Pasteur Research Pole, School of Public Health, The University of Hong Kong, Hong Kong, China.
  • Cole AR; Université Paris Descartes, Sorbonne Paris Cité, Faculté de Médecine, Assistance Publique-Hôpitaux de Paris, Hôpital Universitaire Paris Centre, Centre Hospitalier Universitaire Cochin, Service d'Immunologie Biologique, Paris, France.
  • Moyle AB; Institut Cochin, INSERM U1016, Université Paris Descartes, Sorbonne Paris Cité, Paris.
  • Wagner ND; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Sweeney-Gibbons J; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Rohrs HW; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Gross ML; Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA, USA.
  • Peiris JSM; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Basler CF; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Farnsworth CW; HKU-Pasteur Research Pole, School of Public Health, The University of Hong Kong, Hong Kong, China.
  • Valkenburg SA; Division of Public Health Laboratory Sciences, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong, China.
  • Amarasinghe GK; Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA, USA.
  • Leung DW; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
bioRxiv ; 2020 Nov 30.
Article in English | MEDLINE | ID: covidwho-955697
Preprint
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ABSTRACT
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.

Full text: Available Collection: International databases Database: MEDLINE Language: English Year: 2020 Document Type: Article Affiliation country: 2020.11.30.404905

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Full text: Available Collection: International databases Database: MEDLINE Language: English Year: 2020 Document Type: Article Affiliation country: 2020.11.30.404905