Bacteriocin
Bacteriocins are proteinaceous or peptidic toxins produced by bacteria to inhibit the growth of similar or closely related bacterial strain(s).
[2][3] He was involved in the process of searching for ways to kill bacteria, which also resulted in the development of antibiotics and the discovery of bacteriophage, all within a span of a few years.
[citation needed] Bacteriocins that contain the modified amino acid lanthionine as part of their structure are called lantibiotics.
However, efforts to reorganize the nomenclature of the family of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products have led to the differentiation of lantipeptides from bacteriocins based on biosynthetic genes.
CLBs typically target same species and have species-specific names: klebicins from Klebsiella and pesticins from Yersia pestis.
[8] Some research was made to identify the pyocins and show how they are involved in the “cell-to-cell” competition of the closely related Pseudomonas bacteria.
[11][12] The C-terminal is responsible for species-specific activity, causing cell-leakage by permeabilizing the target cell wall.
The most recently proposed subclass is the Class IIe, which encompasses those bacteriocins composed of three or four non-pediocin like peptides.
The best example is aureocin A70, a four-peptide bacteriocin, highly active against Listeria monocytogenes, with potential biotechnological applications.
[16] Recent work has identified that these bacteriocins are widespread across the bacterial domain and are present in the phylum Actinomycetota.
The best studied bacteriolysin is lysostaphin, a 27 kDa peptide that hydrolyzes the cell walls of several Staphylococcus species, principally S.
Confirmation by experimental data was established with the characterisation of sublancin and glycocin F (GccF) by two independent groups.
[24] Furthermore, bacteriocins active against E. coli, Salmonella and Pseudomonas aeruginosa have been produced in plants with the aim for them to be used as food additives.
In the past, bacteriocins had to be identified by intensive culture-based screening for antimicrobial activity against suitable targets and subsequently purified using fastidious methods prior to testing.
Recently developed in silico-based methods can be applied to rapidly screen thousands of bacterial genomes in order to identify novel antimicrobial peptides.
[31] As of 2009, some bacteriocins, cytolysin, pyocin S2, colicins A and E1, and the microcin MccE492[32] had been tested on eukaryotic cell lines and in a mouse model of cancer.
