An ‘Upp'‐turn in bacteriocin receptor identification

• Published in: Molecular microbiology 2014-06, Vol.92 (6), p.1159-1163
• Main Author: Cotter, Paul D.
• Format: Article
• Language: English
• Subjects: Anti-Bacterial Agents - pharmacology; Bacteria; Bacteriocins - pharmacology; Cell Wall - metabolism; Lactococcus lactis - drug effects; Lactococcus lactis - enzymology; Microbiology; Molecular biology; Peptides; Peptidoglycan - metabolism; Pyrophosphatases - metabolism
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/mmi.12645

Summary Bacteriocins are gene encoded, bacterially produced antimicrobial peptides that have been the focus of considerable scientific interest but which are relatively underutilized by the food, veterinary and medical industries. One means via which the latter issue can be overcome is through a better understanding of how these peptides work or, more specifically, the identification of bacteriocin receptors and the subsequent application of such information to enhance the potency, and commercial value, of bacteriocins. For a time since the identification of lipid II and subunits of the mannose phosphotransferase system as receptors for several class I (modified) and class II (unmodified) bacteriocins, respectively, there were relatively few developments in this area. However, a number of recent studies have addressed this issue, resulting in the identification of a maltose ABC transporter and metallopeptidase as the targets for the garvicin ML (class IIc) and LsbB (class IId) bacteriocins, respectively, and, most recently, the identification of UppP as the receptor for lactococcin G and enterocin 1071 (both class IIb). In addition to these exciting discoveries, the development, and further application, of new strategies to facilitate receptor identification has the potential to lead to even further breakthroughs in bacteriocin research.