Hepatitis Delta Antigen Retains the Assembly Domain as the Only Rigid Entity
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2024-10-30
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Journal Article
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Abstract
The hepatitis delta virus (HDV) S-HDAg and L-HDAg antigens are the two isoforms of the single protein encoded by the viral genome. Together with the double-stranded RNA genome they form the HDV ribonucleoprotein (RNP) complex. In the context of a divide-and-conquer approach, we used a combination of cell-free protein synthesis and proton (H-1)-detected fast magic angle spinning solid-state NMR at highest magnetic field to characterize S-HDAg. We sequentially assigned denovo its isolated N-terminal assembly domain using less than 1 mg of fully protonated protein. Our results show that the assembly domain is the sole rigid component in S-HDAg, with its structure remaining fully conserved within the full-length protein. In contrast, the rest of the protein remains dynamic. This work provides the necessary foundation for future studies of the viral RNP.
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published
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146 (43)
Pages / Article No.
29531 - 29539
Publisher
American Chemical Society
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09681 - Barnes, Alexander / Barnes, Alexander
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201070 - Dynamic Nuclear Polarization at Room Temperature for High Sensitivity Nuclear Magnetic Resonance (SNF)