Microcins and Other Bacteriocins: Bridging the Gaps Between Killing Stategies, Ecology and Applications
Sylvie Rebuffat
from: The Bacteriocins: Current Knowledge and Future Prospects (Edited by: Robert L. Dorit, Sandra M. Roy and Margaret A. Riley). Caister Academic Press, U.K. (2016) Pages: 11-34.
Abstract
Bacteriocins are ribosomally-synthesized antimicrobial peptides or proteins produced by bacteria, which use these potent weapons to thrive in the microbial wars. To complete this arsenal, bacteriocin-producing strains are endowed with efficient strategies to evade being killed by their own toxins. Most bacteriocins are active in the pico- or nanomolar range and target bacterial species that are phylogenetically close to the producing strain, although some exhibit broader spectra of activity. Bacteriocins have been widely studied in Gram-positive- (lantibiotics, pediocin-like bacteriocins) and Gram-negative bacteria (colicins, microcins). However, it is becoming increasingly apparent that bacteriocin production is widespread in nature, including in the archaea, which produce similar defense proteins, the archaeocins. Bacteriocins can differ significantly both in in size and in chemical properties, ranging from small peptides (the Gram-positive bacteriocins and microcins are peptides below 10 kDa) to large proteins (colicins are 30-80 kDa proteins). Many are post-translationally modified using dedicated enzymes, leading to highly complex peptide-derived structures. This structural diversity is associated with complex and refined killing strategies, which contribute to the ecological roles of bacteriocins. Here we review these different aspects, bridging the gaps between biosynthesis, killing strategies, ecology and potential future applications read more ...
