Design of a fusion gene construct for production of recombinant laterosporulin bacteriocin and bioinformatic analysis for assessing the role of the amino-terminal SH2 domain

Bacteriocins are peptides produced by bacteria that are known for their antimicrobial activity against bacteria and fungi. Some chaperone peptides can be probably applied to neutralize the toxic effect of the peptide and produce a soluble form of the protein, as well as to provide high amounts of bacteriocin using recombinant DNA technology. Laterosporulin is described as a 49 amino acid bacteriocin that is naturally secreted from Brevibacillus laterosporus GI-9. In the present study, for the first time, the amine region of the SH2 protein was used to construct a fusion protein for the production of recombinant laterosporulin. In the current study, a fusion gene construct was designed containing the histidine sequence, the SH2 domain, the enterokinase cleavage site, and the laterosporulin peptide. The findings demonstrated that N-SH2 with suitable hydrophobic surfaces can be capable of preventing the aggregation and irreversible structural disruption of bacteriocin laterosporulin as a suitable chaperone. Furthermore, our analysis raised the possibility that target peptide can be expressed with appropriate folding in vitro. The present study revealed that the N-SH2 peptide region could be considered as a suitable alternative for the production of recombinant bacteriocins in Escherichia coli.