Journal article
Transient RNA Interactions Leave a Covalent Imprint on a Viral Capsid Protein
ZH Taji, P Bielytskyi, M Shein, MA Sani, S Seitz, AK Schütz
Journal of the American Chemical Society | AMER CHEMICAL SOC | Published : 2022
DOI: 10.1021/JACS.1C12439
Abstract
The hepatitis B virus (HBV) is the leading cause of persistent liver infections. Its DNA-based genome is synthesized through reverse transcription of an RNA template inside the assembled capsid shell. In addition to the structured assembly domain, the capsid protein harbors a C-terminal extension that mediates both the enclosure of RNA during capsid assembly and the nuclear entry of the capsid during infection. The arginine-rich motifs within this extension, though common to many viruses, have largely escaped atomic-scale investigation. Here, we leverage solution and solid-state nuclear magnetic resonance spectroscopy at ambient and cryogenic temperatures, under dynamic nuclear polarization ..
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Awarded by Helmholtz Association
Funding Acknowledgements
This work was funded by the German Research Foundation (DFG) through the Emmy Noether program (project number 394455587 to A.K.S.), TRR179 (project number 272983813 and project 23 to A.K.S and S.S.), and SFB1035 (project number 201302640 and project B15 to A.K.S.). The work of S.S. was supported by a grant from the Helmholtz Association's Initiative and Networking Fund (Virological and immunological determinants of COVID-19 pathogenesis -lessons to get prepared for future pandemics, KA1-Co-02 `COVIPA'). M.-A.S. acknowledges the support from the Australian Research Council (ARC) via LIEF funding (LE160100120). Access to NMR spectrometers was provided by Bavarian NMR Centre of Technical University of Munich, Helmholtz Centre Munich and the Bio21 Institute at the University of Melbourne.