Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain,bioRxiv - Biochemistry

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Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain
bioRxiv - Biochemistry Pub Date : 2020-11-30 , DOI: 10.1101/2020.11.30.404905
Chao Wu ₁ , Abraham J Qavi ₁ , Asmaa Hachim ₂ , Niloufar Kavian _{2,

3,

4} , Aidan R Cole ₁ , Austin B Moyle ₅ , Nicole D Wagner ₅ , Joyce Sweeney-Gibbons ₆ , Henry W Rohrs ₅ , Michael L Gross ₅ , J S Malik Peiris _{2,

7} , Christopher F Basler ₆ , Christopher W Farnsworth ₁ , Sophie A Valkenburg ₂ , Gaya K Amarasinghe ₁ , Daisy W Leung _{1,

8}

Affiliation

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.

更新日期：2020-12-01

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