Pediocin-like bacteriocins

Class II bacteriocins can be further divided into four groups based on structural features pediocin-like bacteriocins, two-peptide bacteriocins, cyclic bacteriocins and linear non-pediocin-like one-peptide bacteriocins. NMR has been used to characterise examples from each of these subgroups. 

Pediocin PA-1 was shown to dissipate the proton motive force and inhibit the amino acid transport in sensitive cells [75]. lipoteichoic acid is essential for non-specific pediocin AcH binding, and sensitive cells present a specific receptor that potentiates contact with the membrane [17,66]. Pediocin PA-1 displays an important M-terminal -Y-G-N-G-V-X-C- consensus common with other anti-Listeria bacteriocins such as sakacin A (= curvacin A) and P, and leucocin A. This finding suggests an important role of the N-terminus in either the recognition and/or activity of the pediocin-like bacteriocins. 

Peptide bacteriocins produced by lactic acid bacteria are categorized into two different classes according to their biochemical and genetic properties (Drider et al. 2006 Nes et al. 2007). Class I peptides are the lantibiotics, which are small, post-translationally modified peptides that contain unusual amino acids such as lanthionine (TC 1.C.20). Class II includes unmodified bacteriocins that are subdivided into three subclasses, namely, class Ha (pediocin-like bacteriocins), class Ilb (two-peptide bacteriocins), and He (other (i.e., non-pediocin-like), one-peptide bacteriocins). 

Pediocin-like antimicrobial peptides, class Ha bacteriocins, cationic membrane-permeabilizing antimicrobial peptides with 37 to 48 residues produced by a group of lactic acid bacteria. Members of this dass indude, for example, leucocin A, pediodn PA-1, sakacin P, curvacin A, and mesenteridn Y105 [G. Fimland et al., J. Peptide Sci. 2005, 11, 688]. 

Devi, S.M. and Halami, P.M. (2011) Detection and characterization of pediocin PA-l/AcH like bacteriocin producing lactic acid bacteria. Curr. Microbiol, 63, 181-185. 

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