title: Bacteriocins: mechanism of membrane insertion and pore formation.
abstract: Lactic acid bacteria produce several types of pore forming peptides. Class I bacteriocins are lantibiotics that contain (methyl)lanthionine residues that may form intramolecular thioether rings. These peptides generally have a broad spectrum of activity and form unstable pores. Class II bacteriocins are small, heat stable peptides mostly with a narrow spectrum of activity. Most bacteriocins interact with anionic lipids that are abundantly present in the membranes of gram-positive bacteria. 'Docking molecules' may enhance the conductivity and stability of lantibiotic pores, while 'receptors' in the target membrane may determine specificity of class II bacteriocins. Insertion into the membrane of many bacteriocins is proton motive force driven. Lantibiotics may form pores according to a 'wedge-like' model, while class II bacteriocins may enhance membrane permeability either by the formation of a 'barrel stave' pore or by a 'carpet' mechanism.
authors.affiliation: Department of Microbiology and the Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.
authors.forename: G N
authors.initials: GN
authors.lastname: Moll
authors.forename: W N
authors.initials: WN
authors.lastname: Konings
authors.forename: A J
authors.initials: AJ
authors.lastname: Driessen
mesh_terms: D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology* / Q000648:ultrastructure; D006094:Gram-Positive Bacteria / Q000502:physiology* / Q000648:ultrastructure*; D019344:Lactic Acid / Q000378:metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001430:Bacteriocins; D019344:Lactic Acid