The continuing story of class IIa bacteriocins.
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Journal: 2006/August - Microbiology and Molecular Biology Reviews
ISSN: 1092-2172
Abstract:
Many bacteria produce antimicrobial peptides, which are also referred to as peptide bacteriocins. The class IIa bacteriocins, often designated pediocin-like bacteriocins, constitute the most dominant group of antimicrobial peptides produced by lactic acid bacteria. The bacteriocins that belong to this class are structurally related and kill target cells by membrane permeabilization. Despite their structural similarity, class IIa bacteriocins display different target cell specificities. In the search for new antibiotic substances, the class IIa bacteriocins have been identified as promising new candidates and have thus received much attention. They kill some pathogenic bacteria (e.g., Listeria) with high efficiency, and they constitute a good model system for structure-function analyses of antimicrobial peptides in general. This review focuses on class IIa bacteriocins, especially on their structure, function, mode of action, biosynthesis, bacteriocin immunity, and current food applications. The genetics and biosynthesis of class IIa bacteriocins are well understood. The bacteriocins are ribosomally synthesized with an N-terminal leader sequence, which is cleaved off upon secretion. After externalization, the class IIa bacteriocins attach to potential target cells and, through electrostatic and hydrophobic interactions, subsequently permeabilize the cell membrane of sensitive cells. Recent observations suggest that a chiral interaction and possibly the presence of a mannose permease protein on the target cell surface are required for a bacteria to be sensitive to class IIa bacteriocins. There is also substantial evidence that the C-terminal half penetrates into the target cell membrane, and it plays an important role in determining the target cell specificity of these bacteriocins. Immunity proteins protect the bacteriocin producer from the bacteriocin it secretes. The three-dimensional structures of two class IIa immunity proteins have been determined, and it has been shown that the C-terminal halves of these cytosolic four-helix bundle proteins specify which class IIa bacteriocin they protect against.
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Microbiol Mol Biol Rev 70(2): 564-582
PMID: 16760314

The Continuing Story of Class IIa Bacteriocins

Laboratoire de Microbiologie Alimentaire et Industrielle, ENITIAA, Rue de la Géraudière, BP82225, 44322 Nantes Cedex 3, France, Program for Biochemistry and Molecular Biology, Department of Molecular Biosciences, University of Oslo, Oslo, Norway, MFA, Equipe de Microbiologie Fondamentale et Appliquée du Laboratoire de Chimie de l'Eau et de l'Environnement, UMR CNRS 6008, UFR Sciences, Université de Poitiers, 40 Avenue du Recteur Pineau, 86022 Poitiers Cedex, France, Agricultural, Food and Nutritional Science, 4-10, Agricultural Forestry Centre, Office, 2-06E Ag/For Centre, University of Alberta, Edmonton, Alberta T6G 2P5, Canada4
Corresponding author. Mailing address: Laboratoire de Microbiologie Alimentaire et Industrielle, ENITIAA, Rue de la Géraudière, BP82225, 44322 Nantes Cedex, France. Phone: 33 2 51785542. Fax: 33 2 51785520. E-mail: rf.setnan-aaitine@redird.
Copyright © 2006, American Society for Microbiology

Abstract

Many bacteria produce antimicrobial peptides, which are also referred to as peptide bacteriocins. The class IIa bacteriocins, often designated pediocin-like bacteriocins, constitute the most dominant group of antimicrobial peptides produced by lactic acid bacteria. The bacteriocins that belong to this class are structurally related and kill target cells by membrane permeabilization. Despite their structural similarity, class IIa bacteriocins display different target cell specificities. In the search for new antibiotic substances, the class IIa bacteriocins have been identified as promising new candidates and have thus received much attention. They kill some pathogenic bacteria (e.g., Listeria) with high efficiency, and they constitute a good model system for structure-function analyses of antimicrobial peptides in general. This review focuses on class IIa bacteriocins, especially on their structure, function, mode of action, biosynthesis, bacteriocin immunity, and current food applications. The genetics and biosynthesis of class IIa bacteriocins are well understood. The bacteriocins are ribosomally synthesized with an N-terminal leader sequence, which is cleaved off upon secretion. After externalization, the class IIa bacteriocins attach to potential target cells and, through electrostatic and hydrophobic interactions, subsequently permeabilize the cell membrane of sensitive cells. Recent observations suggest that a chiral interaction and possibly the presence of a mannose permease protein on the target cell surface are required for a bacteria to be sensitive to class IIa bacteriocins. There is also substantial evidence that the C-terminal half penetrates into the target cell membrane, and it plays an important role in determining the target cell specificity of these bacteriocins. Immunity proteins protect the bacteriocin producer from the bacteriocin it secretes. The three-dimensional structures of two class IIa immunity proteins have been determined, and it has been shown that the C-terminal halves of these cytosolic four-helix bundle proteins specify which class IIa bacteriocin they protect against.

Abstract

Acknowledgments

We thank Carol Robins for improvement of the English of the manuscript. We thank Pablo Hernandez (Madrid, Spain) for comments and suggestions.

D.D. and H.P. thank the French Ministry of Agriculture, La Région des Pays de la Loire, and the European Union (SEAFOODplus) for their financial support for antimicrobial peptide projects carried out at ENITIAA. Y.H. thanks Rhodia-Food Company, la Région Poitou-Charentes, and the French Ministry of Education for supporting his research projects. Research at the laboratory of L.M.M. was funded by the Natural Sciences and Engineering Research Council of Canada. G.F. was supported by the Norwegian Research Council.

Acknowledgments

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