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Short Communication |
Biomedical Research and Study Centre, University of Latvia, 1 Ratsupites Street, LV-1067 Riga, Latvia
Correspondence
Andris Kazaks
andris{at}biomed.lu.lv
The sequence of the preS domain of the hepatitis B virus (HBV, genotype D) envelope was inserted into the major immunodominant region (MIR) of the C-terminally truncated HBV core (HBc) protein. In Escherichia coli, the HBcpreS fusion protein was partially soluble and did not produce particles. Co-expression of the wild-type HBc as a helper protein along with the fusion protein led to the formation of mosaic HBc particles that exhibited HBc, preS1 and preS2 antigenicity. Two alternative combinations of medium- and high-copy plasmids were used for co-expression of fusion and helper proteins, in an attempt to improve mosaic particle production. However, the preS fusion content of the particles remained the same in both expression combinations. In a third co-expression in which the modified HBc helper lacked aa 7685 in the MIR, the incorporation level of HBcpreS fusion into the particles was noticeably lower. Purified chimeric particles were immunogenic in mice.
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