Cloning, expression and antimicrobial activity of a recombinant (CBD)2-DrsB1 peptide against human microbial pathogens

New and effective antimicrobial agents are inevitable because of the increased use of antibiotics and spread of microbial resistance. The expression of antimicrobial peptides that are part of the inherent immune system of all organisms, is a novel approach of confronting a wide range of pathogens. Among the wide range of antimicrobial peptides, Dermaseptin B1 is a potent cationic peptide with strong antimicrobial activity. In this study, Dermaseptin B1 (DrsB1) coding sequence from Phyllomedusa bicolor frogs was fused to a tandem repeat of a chitin-binding domain (CBD) from Cladosporium fulvum Avr4 effector protein and expressed in tobacco Hairy Roots (HRs). The expression of recombinant (CBD)2-DrsB1 peptide was confirmed, using molecular methods and its antimicrobial activity was evaluated against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Enterococcus faecalis and Bacillus subtilis bacteria. The results of antimicrobial activity analysis demonstrated that the recombinant protein had a significant (P