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Related Experiment Video

Updated: Jan 23, 2026

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods
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Hepatitis B Virus X Protein Function Requires Zinc Binding.

Dhivya Ramakrishnan1, Weimei Xing1, Rudolf K Beran1

  • 1Gilead Sciences, Inc., Foster City, California, USA.

Journal of Virology
|June 7, 2019
PubMed
Summary
This summary is machine-generated.

Hepatitis B virus X protein (HBx) uses a zinc-binding CCCH motif to degrade the host Smc5/6 complex, enabling viral transcription. This study identifies key residues essential for HBx function in HBV replication.

Keywords:
DDB1HBxSmc5/6 complexhepatitis B virus

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • The host Smc5/6 complex restricts hepatitis B virus (HBV) transcription.
  • HBV X protein (HBx) antagonizes Smc5/6 by recruiting a ubiquitin ligase for its degradation.
  • The precise mechanism by which HBx interacts with DDB1 and Smc5/6 remains unclear.

Purpose of the Study:

  • To identify key regions and residues of HBx essential for Smc5/6 degradation and HBV transcription.
  • To elucidate the structural and functional role of HBx in modulating host-pathogen interactions.

Main Methods:

  • Biophysical analyses of recombinant HBx, including zinc binding assays.
  • Mass spectrometry-based hydrogen-deuterium exchange and chemical footprinting of the HBx:DDB1 complex.
  • Functional analysis of HBx mutants in HBV-infected primary human hepatocytes (PHH).

Main Results:

  • Recombinant HBx is soluble and binds zinc stoichiometrically with DDB1.
  • A conserved CCCH motif (amino acids 61-137) in HBx is critical for zinc binding and HBx function.
  • Mutagenesis of C61, C69, C137, and H139 abolishes HBx-mediated Smc6 degradation and HBV transcription.

Conclusions:

  • The identified CCCH motif is essential for HBx function, likely by coordinating zinc.
  • HBx utilizes this zinc-binding motif to counteract the host Smc5/6 restriction factor.
  • This study provides insights into the HBx structure-function relationship and suggests methods for further structural studies.