Abstract
Each year, nearly 900,000 deaths are due to serious liver diseases caused by chronic hepatitis B virus infection. The viral particle is composed of an outer envelope and an inner icosahedral nucleocapsid formed by multiple dimers of a ~ 20 kDa self-assembling core protein (Cp). Here we report the solid-state 13C and 15N resonance assignments of the assembly domain, Cp149, of the core protein in its capsid form. A secondary chemical shift analysis of the 140 visible residues suggests an overall alpha-helical three-dimensional fold matching that derived for Cp149 from the X-ray crystallography of the capsid, and from solution-state NMR of the Cp149 dimer. Interestingly, however, at three distinct regions the chemical shifts in solution differ significantly between core proteins in the capsid state versus in the dimer state, strongly suggesting the respective residues to be involved in capsid assembly.
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Acknowledgements
This work was supported by the French ANR (ANR-14-CE09-0024B), the LABEX ECOFECT (ANR-11-LABX-0048) within the Université de Lyon program Investissements d’Avenir (ANR-11-IDEX-0007) (AB), the Swiss National Science Foundation (Grant 200020_159707) (BHM), the DFG Grant NA154/9-4 (MN), a doctoral stipend from the Chinese Scientific Council (SW) and by the Marie Skłodowska-Curie program (H2020-MSCA-IF-2016 748516) (LL). We thank the Centre d’Imagerie Quantitative Lyon-Est (CIQLE) for the access and training on the electron microscopy platform.
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Lauriane Lecoq and Shishan Wang have contributed equally to this work.
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Lecoq, L., Wang, S., Wiegand, T. et al. Solid-state [13C–15N] NMR resonance assignment of hepatitis B virus core protein. Biomol NMR Assign 12, 205–214 (2018). https://doi.org/10.1007/s12104-018-9810-y
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DOI: https://doi.org/10.1007/s12104-018-9810-y