Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action
- Cite this article as:
- Nissen-Meyer, J. & Nes, I. Arch Microbiol (1997) 167: 67. doi:10.1007/s002030050418
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.