title: Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria.
abstract: This review focuses on the structure and mode-of-action of non-lanthionine-containing peptide bacteriocins produced by Gram-positive bacteria. These bacteriocins may be divided into four groups: (i) the anti-listerial one-peptide pediocin-like bacteriocins that have very similar amino acid sequences, (ii) the two-peptide bacteriocins that consist of two different peptides, (iii) the cyclic bacteriocins, and (iv) the linear non-pediocin-like one-peptide bacteriocins. These bacteriocins are largely cationic, contain 20 to 70 residues, and kill cells through membrane-permeabilization. The pediocin-like bacteriocins are the ones that are best characterized. Upon contact with target membranes, their cationic N-terminal half forms a beta-sheet-like structure that binds to the target cell surface, while their more hydrophobic helical-containing C-terminal half penetrates into the hydrophobic core of target-cell membranes and apparently binds to the mannose phosphotransferase permease in a manner that results in membrane leakage. Immunity proteins that protect cells from being killed by pediocin-like bacteriocins bind to the bacteriocin-permease complex and prevent bacteriocin-induced membrane-leakage. Recent structural analyses of two-peptide bacteriocins indicate that they form a helix-helix structure that penetrates into cell membranes. Also these bacteriocins may act by binding to integrated membrane proteins. It is proposed that many membrane-active peptide bacteriocins kill target-cells through basically the same mechanism; the common theme being that a membrane-penetrating part of bacteriocins bind to a membrane embedded region of an integrated membrane protein, thereby causing conformational alterations in the protein that in turn lead to membrane-leakage and cell death.
authors.affiliation: Department of Molecular Biosciences, University of Oslo, Oslo, Norway. jon.nissen-meyer@imbv.uio.no
authors.forename: J
authors.initials: J
authors.lastname: Nissen-Meyer
authors.forename: P
authors.initials: P
authors.lastname: Rogne
authors.forename: C
authors.initials: C
authors.lastname: Oppegård
authors.forename: H S
authors.initials: HS
authors.lastname: Haugen
authors.forename: P E
authors.initials: PE
authors.lastname: Kristiansen
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry / Q000494:pharmacology; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry* / Q000145:classification* / Q000235:genetics; D006094:Gram-Positive Bacteria / Q000235:genetics / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D013329:Structure-Activity Relationship; D013440:Sulfides
chemical_list: D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D010455:Peptides; D013440:Sulfides; C001520:lanthionine; D000409:Alanine