LiaRS reporter assay: A simple tool to identify lipid II binding moieties in lantibiotic nukacin ISK-1

• Published in: Journal of bioscience and bioengineering Vol. 123; no. 3; pp. 398 - 401
• Main Authors: Elsayed, Khaled M., Islam, Mohammad R., Abdullah-Al-Mahin, Nagao, Jun-ichi, Zendo, Takeshi, Sonomoto, Kenji
• Format: Journal Article
• Language: English
• Published: Japan Elsevier B.V 01.03.2017
• Subjects: Alanine - analogs & derivatives; Alanine - metabolism; Amino Acid Sequence; Bacillus subtilis - metabolism; Bacteriocin; Bacteriocins - chemistry; Bacteriocins - metabolism; Cell Wall - metabolism; Genes, Reporter; Lantibiotic; Lipid II; Nukacin ISK-1; Structure-activity relationship; Sulfides - metabolism; Two-component system; Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid - metabolism; Lipid II; Two-component system; Lantibiotic; Nukacin ISK-1; Structure-activity relationship; Bacteriocin
• ISSN: 1389-1723; 1347-4421
• DOI: 10.1016/j.jbiosc.2016.10.002

Binding to lipid II is an important step in the mode of action of most lantibiotics targeting the bacterial cell wall. We applied the Bacillus subtilis two-component system, LiaRS, that is known to respond to antibiotics interfering with lipid II cycle, in order to evaluate lipid II binding activity of known bacteriocins and also to identify lipid II binding moieties in lantibiotic nukacin ISK-1. Using this method, we confirmed that the methyllanthionine ring in nukacin ISK-1 is crucial for lipid II binding as previously indicated. In this study, we further identified that the three N-terminal lysine residues (K1, K2, and K3) and the glycine (G5) residue in nukacin ISK-1 are also important in lipid II binding.