Chao Wu, Abraham J. Qavi, A. Hachim, N. Kavian, Aidan R. Cole, Austin B. Moyle, N. Wagner, Joyce Sweeney-Gibbons, H. Rohrs, M. Gross, J. Peiris, C. Basler, C. Farnsworth, S. Valkenburg, G. Amarasinghe, D. Leung
bioRxiv : the preprint server for biology, 2020
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.
Cited by 7 publications.
Field of study: Chemistry