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Current Protein & Peptide Science


ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Lacticin 3147 - Biosynthesis, Molecular Analysis, Immunity, Bioengineering and Applications

Author(s): Srinivas Suda, Paul D. Cotter, Colin Hill and R. Paul Ross

Volume 13, Issue 3, 2012

Page: [193 - 204] Pages: 12

DOI: 10.2174/138920312800785021

Price: $65


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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