Abstract
Bacteriocins produced by lactic acid bacteria (LAB-bacteriocins) may serve as alternatives for aging antibiotics. LAB-bacteriocins can be used alone, or in some cases as potentiating agents to treat bacterial infections. This approach could meet the different calls and politics, which aim to reduce the use of traditional antibiotics and develop novel therapeutic options. Considering the clinical applications of LAB-bacteriocins as a reasonable and desirable therapeutic approach, it is therefore important to assess the advances achieved in understanding their modes of action, and the resistance mechanisms developed by the producing bacteria to their own bacteriocins. Most LAB-bacteriocins act by disturbing the cytoplasmic membrane through forming pores, or by cell wall degradation. Nevertheless, some of these peptides still have unknown modes of action, especially those that are active against Gram-negative bacteria. Regarding immunity, most bacteriocin-producing strains have an immunity mechanism involving an immunity protein and a dedicated ABC transporter system. However, these immunity mechanisms vary from one bacteriocin to another.
Highlights
Production of bacteriocins can give a bacterium a competitive advantage in its natural environment
OR-7 [5], bacteriocin SMXD51 [6], and E20 fraction [7] are even active against Gramnegative bacteria such as Campylobacter jejuni and Escherichia coli, including E. coli strains carrying mcr-1 gene, which is responsible for colistin resistance [8]
The first studies on Pediocin PA-1 showed the ability of this bacteriocin to permeabilize lipidic vesicles, but the authors thought this effect occurred with higher concentrations of bacteriocin than necessary [118,119,120]
Summary
Production of bacteriocins can give a bacterium a competitive advantage in its natural environment. Different classifications of bacteriocins have been proposed and include LAB-bacteriocins as well as those produced by other Gram-positive or Gram-negative bacteria [11,12,13,14,15,16]. RiPPs belong to a group of antimicrobial peptides (AMP) known for their ability to undergo post-translational enzymatic modifications during their biosynthesis As mentioned above, these AMP contain unusual amino acids and structures which play a major role in their antimicrobial activity (e.g., lanthionine, heterocycle, head-to-tail cyclization, glycosylation). These AMP contain unusual amino acids and structures which play a major role in their antimicrobial activity (e.g., lanthionine, heterocycle, head-to-tail cyclization, glycosylation) They are produced by Archaea, as well as by bacteria and eukaryotic cells, and their classification is based on the post-translational modifications [46]
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