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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 °C. The purity of active HBx protein was >99% with a very stable secondary structure dominated by α‐helix, β‐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.

High‐level expression and large‐scale preparation of soluble HBx antigen from Escherichia coli