Journal
ISCIENCE
Volume 24, Issue 6, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.isci.2021.102681
Keywords
-
Categories
Funding
- Fast Grant [2161, 2158]
- NIH [P01AI120943, R01AI123926, R01AI107056, P41GM103422, R24GM136766, R01AI143292, R01AI148663]
- Health and Medical Research Fund, Food and Health Bureau, Hong Kong [COVID190115, COVID190126]
- NIH/NIAID CEIRS contract [HHSN272201400006C]
- NIH T32 training grant [T32CA009547]
Ask authors/readers for more resources
The study characterizes the biochemical properties of the nucleocapsid protein N encoded by SARS-CoV-2 and highlights the value of using N domains as highly specific and sensitive diagnostic markers. The research provides insights into N oligomerization, RNA binding, phosphorylation regulation, and immunogenicity of different N domains.
Nucleocapsid (N) encoded by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) plays key roles in the replication cycle and is a critical serological marker. Here, we characterize essential biochemical properties of N and describe the utility of these insights in serological studies. We define N domains important for oligomerization and RNA binding and show that N oligomerization provides a high-affinity RNA-binding platform. We also map the RNA-binding interface, showing protection in the N-terminal domain and linker region. In addition, phosphorylation causes reduction of RNA binding and redistribution of N from liquid droplets to loose coils, showing how N-RNA accessibility and assembly may be regulated by phosphorylation. Finally, we find that the C-terminal domain of N is the most immunogenic, based on antibody binding to patient samples. Together, we provide a biochemical description of SARS-CoV-2 N and highlight the value of using N domains as highly specific and sensitive diagnostic markers.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available