A Review on the Use of the Signal Peptide in Recombinant Interferon beta Secretion in Escherichia coli

Eukaryotic and prokaryotic expression systems are used with similar processes for the production of rIFN-β1a and rIFN-β1b which are from the recombinant interferon beta (rIFN-β) protein varieties. The difficulties in purification of the produced rIFN-β1a by eukaryotic expression systems and the influence of its biological activity make recombinant protein production difficult with these processes. In the production of rIFN-β1b, where prokaryotic expression systems were used, purification and activity problems were found to be less frequent. Better use of product secretion capability in Escherichia coli from prokaryotic bacteria indicates that this system will be preferred in the production of rIfN-β1b. If the construct is designed to secrete recombinant proteins out of the host cell from which the recombinant proteins are produced, it is envisaged that the host cells will not fragment during purification, thereby facilitating product purification processes. The use of E. coli with type I and type II secretion in the production of rIFN-β1b proteins will reduce the purification and activity problems in the secretion of rIFN-β1b produced in this host, as well as the toxic effect of rIFN-β1b to the host cell is expected to diminish. To this end, various approaches are contemplated to overcome the disadvantages of the E. coli production system, such as transferring the DmsA signal peptide, the Tat-type signal peptide, to the expression vector pET22b, in addition to the PelB signal peptide, the Sec signal peptide. In this review, information about the properties of IFNs, the clinical applications of rIFN-β and the researches based on the investigations of rIFN-β1b production methods, and information about the use of signal peptides in the process of producing rIFN-β1b in E. coli host cells were highlighted