Expression, purification and functional validation of a cancer-associated isoform of the HBx protein from human hepatitis B virus
The human hepatitis B virus (HBV) causes hepatitis B, a liver infection that can be acute or chronic. HBV encodes four proteins, among which the X protein (HBx) plays a critical role in viral replication. During chronic HBV infection, in which the viral DNA is integrated into the host genome, the HB...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
February 2026
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| In: |
Protein expression and purification
Year: 2026, Volume: 238, Pages: 1-7 |
| ISSN: | 1096-0279 |
| DOI: | 10.1016/j.pep.2025.106842 |
| Online Access: | Verlag, kostenfrei, Volltext: https://doi.org/10.1016/j.pep.2025.106842 Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S1046592825001846 
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| Author Notes: | Alexis Clavier, Santiago Gómez-Evain, Toshinobu Shida, Rubaba R. Abanti, Franziska Hammerstein, Pavel Kielkowski, Mila Leuthold, Anne K. Schütz |
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| 520 | |a The human hepatitis B virus (HBV) causes hepatitis B, a liver infection that can be acute or chronic. HBV encodes four proteins, among which the X protein (HBx) plays a critical role in viral replication. During chronic HBV infection, in which the viral DNA is integrated into the host genome, the HBx1-120 isoform, comprising the N-terminal 120 residues, is highly expressed. Here, we describe a protocol for the recombinant overexpression and purification of untagged HBx1-120 from bacterial cells. The procedure is compatible with stable isotope labelling in minimal media. Following cell lysis, HBx1-120 was recovered from inclusion bodies (IBs), solubilized in urea, and purified by ion-exchange (IEX) and size-exclusion chromatography (SEC). The purified protein was extensively characterized, including by mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy. Functionality was confirmed by a pulldown assay with a known interacting partner, Spindlin1. This protocol provides a robust framework to obtain untagged HBx1-120 for structural and functional in vitro studies. | ||
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| 700 | 1 | |a Abanti, Rubaba R. |e VerfasserIn |4 aut | |
| 700 | 1 | |a Hammerstein, Franziska |e VerfasserIn |4 aut | |
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