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To explore the feasibility of using fusion protein of interleukin-6 (IL6) and interferon-¦Á (IFN¦Á) as an immunoadjuvant, the mature peptide genes of IL6 and IFN¦Á were cloned and linked via a hydrophilic and low charge linker sequence£¬and subcloned to pET32¦Á for prokaryotic expression. The recombinant plasmid was transformed into E.coli DH5¦Á and Rosetta (DE3), then induced with different concentrations' IPTG. SDS-PAGE results showed that recombinant proteins were expressed in inclusion bodies with molecular weight of 44.96 KDa. The results show that the expression plasmid is successfully constructed and IL6-IFN¦Á protein is expressed in E.coli. This study will be a foundation for further study and application of IL6-IFN¦Á as a novel efficient immunoadjuvant.

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To explore the capability of interleukin-6/interferon-¦Á (IL6/IFN¦Á) fusion protein as/being as an immunoadjuvant, the coding sequences of IL6 and IFN were cloned. Considering the characteristics of these coding sequences and the sequence of prokaryotic expression vector pET32a, the mature peptide sequences were amplified using the specific primer(s) designed with restriction enzyme sites, Linker sequence and His tag, and then transfected into E.coli DH5¦Áafter linked with pMD18-T, respectively. The plasmids were extracted and restricted, and then linked via a hydrophilic and low-charge Linker sequence, which was then restricted simultaneously to construct the recombinant plasmid of pMD18-IL6-IFN¦Á. This recombinant plasmid and expression vector pET32a were restricted and linked to construct the pET32-IL6-IFN¦Á plasmid. The plasmid was transformed into E.coli DH5¦Á and Rosetta (DE3), and then expressed under different concentrations' IPTG and times. The results showed that the pET32-IL6-IFN¦Áwas constructed successfully. ¡­. The results show that the expression plasmid is successfully constructed and IL6-IFN¦Á protein is expressed in E.coli. This study will be a foundation for further study and application of IL6-IFN¦Á as a novel efficient immunoadjuvant.
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