Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain
| Autor: | Joyce Sweeney-Gibbons, Abraham J. Qavi, Michael L. Gross, Niloufar Kavian, Christopher W Farnsworth, Christopher F. Basler, Asamaa Hachim, Gaya K. Amarasinghe, Daisy W. Leung, Austin B. Moyle, Aidan R. Cole, Nicole D. Wagner, Chao Wu, Henry W. Rohrs, J. S. Malik Peiris, Sophie A. Valkenburg |
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| Rok vydání: | 2020 |
| Předmět: |
Coronavirus disease 2019 (COVID-19)
Chemistry Viral protein SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) C-terminus RNA COVID-19 serology RNA binding Antigen binding medicine.disease_cause Replication cycle Article oligomerization Cell biology medicine Phosphorylation LLPS phase separation nucleoprotein |
| Zdroj: | iScience bioRxiv article-version (status) pre article-version (number) 1 |
| Popis: | Nucleocapsid (N) encoded by 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 upon 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. Graphical Abstract |
| Databáze: | OpenAIRE |
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