Editing Bacteriocin (section)

==Research==
Bacteriocins have been proposed as a replacement for antibiotics to which pathogenic bacteria have become [[Antimicrobial resistance|resistant]]. Potentially, the bacteriocins could be produced by bacteria intentionally introduced into the patient to combat infection.<ref name="CotterRoss2012"/> There are several strategies by which new bacteriocins can be discovered. In the past, bacteriocins had to be identified by intensive [[Microbiological culture|culture-based
]] screening for antimicrobial activity against suitable targets and subsequently purified using fastidious methods prior to testing. However, since the advent of the genomic era, the availability of the bacterial genome sequences has revolutionized the approach to identifying bacteriocins. Recently developed ''[[in silico]]''-based methods can be applied to rapidly screen thousands of bacterial genomes in order to identify novel antimicrobial peptides.<ref>{{cite journal | vauthors = Rezaei Javan R, van Tonder AJ, King JP, Harrold CL, Brueggemann AB | title = Genome Sequencing Reveals a Large and Diverse Repertoire of Antimicrobial Peptides | journal = Frontiers in Microbiology | volume = 9 | issue = 9 | pages = 2012 | date = August 2018 | pmid = 30210481 | pmc = 6120550 | doi = 10.3389/fmicb.2018.02012 | doi-access = free }}</ref>

As of 2014 some bacteriocins had been studied in ''in vitro'' studies to see if they can stop viruses from replicating, namely staphylococcin 188 against [[Newcastle disease virus]], [[influenza virus]], and coliphage HSA virus; each of enterocin AAR-71 class IIa, enterocin AAR-74 class IIa, and erwiniocin NA4 against coliphage HSA virus; each of enterocin ST5Ha, enterocin NKR-5-3C, and subtilosin against HSV-1; each of enterocin ST4V and enterocin CRL35 class IIa against HSV-1 and HSV-2;  labyrinthopeptin A1 against HIV-1 and HSV-1;  and bacteriocin from ''[[Lactobacillus delbrueckii]]'' against influenza virus.<ref>{{cite journal | vauthors = Al Kassaa I, Hober D, Hamze M, Chihib NE, Drider D | title = Antiviral potential of lactic acid bacteria and their bacteriocins | journal = Probiotics and Antimicrobial Proteins | volume = 6 | issue = 3–4 | pages = 177–85 | date = December 2014 | pmid = 24880436 | doi = 10.1007/s12602-014-9162-6 | s2cid = 43785241 }}</ref>

As of 2009, some bacteriocins, [[cytolysin]], [[pyocin]] S2, [[colicin]]s A and E1, and the [[microcin]] MccE492<ref>{{cite journal | vauthors = Huang K, Zeng J, Liu X, Jiang T, Wang J | title = Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin | journal = Cell Discovery | volume = 7 | issue = 1 | pages = 20 | date = April 2021 | pmid = 33820910 | pmc = 8021565 | doi = 10.1038/s41421-021-00253-6 }}</ref> had been tested on eukaryotic cell lines and in a mouse model of cancer.<ref>{{cite journal | vauthors = Lagos R, Tello M, Mercado G, García V, Monasterio O | title = Antibacterial and antitumorigenic properties of microcin E492, a pore-forming bacteriocin | journal = Current Pharmaceutical Biotechnology | volume = 10 | issue = 1 | pages = 74–85 | date = January 2009 | pmid = 19149591 | doi = 10.2174/138920109787048643 | hdl = 10533/142500 }}</ref>