The continuing problem of the emergence of multidrug resistance in pathogens has resulted in renewed efforts
to identify novel antimicrobials that could be used in clinical settings. Lantibiotics are bacterially produced gene encoded
antimicrobial peptides which have been the focus of extensive investigation in recent years because of their broad spectrum
of activity. Lantibiotics (lanthionine-containing antibiotics), which have traditionally been regarded as antimicrobials
for use in food or veterinary medicine, may provide at least part of the solution to these problems. Lacticin 3147 is a two
peptide lantibiotic (consisting of the peptides Ltnα and Ltnβ) which is active at low concentrations against many pathogens.
It has been the subject of extensive research, which has generated significant insights into the mechanisms of lacticin
3147 biosynthesis, immunity, structure function relationships and the consequences of molecular bioengineering. The
merits of employing lacticin 3147 to control spoilage microbes as well as its potential in the elimination of food, human
and veterinary pathogens have also been highlighted. Here we review the knowledge which has been gained with respect
to lacticin 3147 since its discovery in 1995.
Keywords: Antimicrobial peptides, bacteriocins, bioengineering, lacticin 3147, lantibiotics, lantibiotic applications, mutagenesis, genera, bioavailability, biostability
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