Evaluation of antibacterial activity of enterocin A-colicin E1 fusion peptide.

OBJECTIVES

Bacterial resistance to most common antibiotics is a harbinger of the requirement to find novel anti-infective, antimicrobials agents, and increase innovative strategies to struggle them. Numerous bacteria produce small peptides with antimicrobial activities called bacteriocin. This study aimed to investigate the antibacterial properties of the fusion protein of Enterocin A and Colicin E1 modified against pathogens.

MATERIALS AND METHODS

Analysis of recombinant bacteriocin Enterocin A and Colicin E1 (ent A-col E1) was performed to assay the stability and antibacterial activity of this fusion protein. The pET-22b vector was employed to express the coding sequence of the ent A-col E1 peptide in BL21 (DE3). Minimum inhibitory concentration (MIC), disk diffusion, and time-kill tests were performed to evaluate the antibacterial activity of the ent A-col E1 against (ATCC 9027), (ATCC 10536), (ATCC 29212), and (ATCC 33591).

RESULTS

The suggested recombinant peptide had good antibacterial activity against both Gram-negative and Gram-positive pathogens. It has also good stability at various temperatures, pH levels, and salt concentrations.

CONCLUSION

Because bacteriocins are harmless compounds, they can be recommended as therapeutic or preventive supplements to control pathogens. According to the obtained results, the ent A-col E1 peptide can serve as an efficient antibacterial compound to treat or prevent bacterial infections.