Detection and Characterization of Weissellicin 110, a Bacteriocin Produced by Weissella cibaria

Bacteriocins are natural peptides produced by bacteria that display antimicrobial activities. Much recent research has focused on the bacteriocins produced by lactic acid bacteria (LAB). These peptides have potential use as food preservatives (1-3). The classification of LAB bacteriocins has been addressed in many schemes (4-5). Generally, lantibiotics (containing post-translationally modified amino acids such as lanthionine and β-methyllanthionine) are assigned to Class I (5). ClassII bacteriocins are defined as non-lanthionine-containing bacteriocins and are further subdivided into 4 groups (classes IIa, IIb, IIc, and IId) (5). Many bacteriocins are synthesized as precursors containing leader peptides. Michiels et al. (6) demonstrated the secretion of some bacteriocins requires the activity of a dedicated ATP-binding cassette (ABC) transporter. The activity of this type of transporter typically includes cleavage of the pre-bacteriocin to release a leader peptide (the double-glycine leader sequence) and subsequent translocation of the mature bacteriocin across the cytoplasmic membrane. Bacteriocins have been frequently reported from Lactobacillus, Enterococcus, Lactococcus, and Leuconostoc (3, 7). However, relatively little information is available about bacteriocins from Weissella. A limited number of bacteriocins, such as weissellicin 110, weissellin A, weissellicin Y, weissellicin M, and weissellicin L, have been reported previously from Weissella spp. (8-12). The lengths of these bacteriocins range from 42 to 52 amino acid residues and these sequences are highly diverse, thus it is impracticable to design degenerate primers to amplify the bacteriocins of Weissella spp. Among these, weissellicin 110 is the only bacteriocin reported in Weissella cibaria. This bacteriocin represents several unique features; it is staIran J Biotech. 2015 September;13(3): e1159 DOI:10.15171/ijb.1159