ArticleBiotechnology and applied biochemistry2009
High-level expression and large-scale preparation of soluble HBx antigen from Escherichia coli.
Article in Biotechnology and applied biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Purification and Evaluation of the Biological Activity of Recombinant Mouse Prolactin.Journal of microbiology and biotechnology · 2025Article
- Fusion proteins towards fungi and bacteria in plant protection.Microbiology (Reading, England) · 2018Article
- Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Antigenicity of recombinant maltose binding protein-Mycobacterium avium subsp. paratuberculosis fusion proteins with and without factor Xa cleaving.Clinical and vaccine immunology : CVI · 2013Article
- Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus.Molecules and cells · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The HBx (hepatitis B virus X protein) is a multifunctional regulator of cellular signal transduction and transcription pathways in host-infected cells. Evidence suggests that HBx has a critical role in the pathogenesis of hepatocellular carcinoma. However, the lack of efficient large-scale preparation methods for soluble HBx has hindered studies on the structure and function of HBx. Here, a new pMAL-c2x protein fusion and purification system was used for high-level expression of soluble HBx fusion protein. The high-purity fusion protein was obtained via amylose resin chromatography and Q-Sepharose chromatography. The untagged HBx was efficiently and rapidly purified by Sephadex G-75 chromatography after cleavage by Factor Xa at 23 degrees C. The purity of active HBx protein was >99% with a very stable secondary structure dominated by alpha-helix, beta-sheet and random structure. The purified HBx protein can be analysed to determine its crystal structure and function and its capabilities as an effective immunogen.
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