Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action
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© Springer-Verlag 1997
MINI-REVIEW
Jon Nissen-Meyer · Ingolf F. Nes
Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action
Received: 30 August 1996 / Accepted: 26 November 1996
Abstract Ribosomally synthesized peptides with antimicrobial activity are produced by prokaryotes, plants, and a wide variety of animals, both vertebrates and invertebrates. These peptides represent an important defense against micro-organisms. Although the peptides differ greatly in primary structures, they are nearly all cationic and very often amphiphilic, which reflects the fact that many of these peptides kill their target cells by permeabilizing the cell membrane. Moreover, many of these peptides may roughly be placed into one of three groups: (1) those that have a high content of one (or two) amino acid(s), often proline, (2) those that contain intramolecular disulfide bonds, often stabilizing a predominantly β-sheet structure, and (3) those with amphiphilic regions if they assume an α-helical structure. Most known ribosomally synthesized antimicrobial peptides have been identified and characterized during the past 15 years. As a result of these studies, insight has been gained into fundamental aspects of biology and biochemistry such as innate immunity, membrane-protein interactions, and protein modification and secretion. Moreover, it has become evident that these peptides may be developed into useful antimicrobial additives and drugs. This review presents a broad overview of the main types of ribosomally synthesized antimicrobial peptides produced by eukaryotes and prokaryotes. Key words Antimicrobial peptides · Defensins · Cathelicidins · Magainins · Cecropins · Bacteriocins · Lantibiotics Abbreviations CD Circular dichroism · LAP Lingual antimicrobial peptide(s) · LPS Lipopolysaccharide · TAP Tracheal antimicrobial peptide(s)
J. Nissen-Meyer (Y) Department of Biochemistry, University of Oslo, Post 1401, Blindern, 0316 Oslo, Norway Tel. +47-2285-6633, -6632, -7351; Fax +47-2285-4443 I. F. Nes Laboratory of Microbial Gene Technology, Agricultural University of Norway, Ås, Norway
Introduction Gene-encoded, ribosomally synthesized antimicrobial peptides are widely distributed in nature, being produced by mammals, birds, amphibia, insects, plants, and microorganisms (Cammue et al. 1994; Sahl 1994; Boman 1995). Although they form a diverse group of peptides as judged by their primary structures, they are often cationic and amphiphilic, and most of them kill bacteria by permeabilizing the target-cell membrane. Their positive charge presumably facilitates interactions with the negatively charged bacterial phospholipid-containing membranes and or acidic bacterial cell walls, whereas their amphiphilic character enables membrane permeabilization. In mammals, antimicrobial peptides are expressed in phagocytes and mucosal epithelial cells (Lehrer et al. 1993; Boman 1995; Martin et al. 1995). In insects, bacterial infection induces the release of antibacterial peptides into the haemo
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