title: Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.
abstract: Microorganisms synthesize several compounds with antimicrobial activity in order to compete or defend themselves against others and ensure their survival. In this line, the cell wall is a major protective barrier whose integrity is essential for many vital bacterial processes. Probably for this reason, it represents a 'hot spot' as a target for many antibiotics and antimicrobial peptides such as bacteriocins. Bacteriocins have largely been recognized by their pore-forming ability that collapses the selective permeability of the cytoplasmic membrane. However, in the last few years, many bacteriocins have been shown to inhibit cell wall biosyntheis alone, or in a concerted action with pore formation like nisin. Examples of cell wall-active bacteriocins are found in both Gram-negative and Gram-positive bacteria and include a wide diversity of structures such as nisin-like and mersacidin-like lipid II-binding bacteriocins, two-peptide lantibiotics, and non-modified bacteriocins. In this review, we summarize the current knowledge on these antimicrobial peptides as well as the role, composition, and biosynthesis of the bacterial cell wall as their target. Moreover, even though bacteriocins have been a matter of interest as natural food antimicrobials, we propose them as suitable tools to provide new means to improve biotechnologically relevant microorganisms.
authors.affiliation: DairySafe Group, Department of Technology and Biotechnology of Dairy Products, Instituto de Productos Lácteos de Asturias (IPLA-CSIC), Paseo Río Linares s/n., 33300, Villaviciosa, Asturias, Spain.
authors.forename: Clara
authors.initials: C
authors.lastname: Roces
authors.affiliation: DairySafe Group, Department of Technology and Biotechnology of Dairy Products, Instituto de Productos Lácteos de Asturias (IPLA-CSIC), Paseo Río Linares s/n., 33300, Villaviciosa, Asturias, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Rodríguez
authors.affiliation: DairySafe Group, Department of Technology and Biotechnology of Dairy Products, Instituto de Productos Lácteos de Asturias (IPLA-CSIC), Paseo Río Linares s/n., 33300, Villaviciosa, Asturias, Spain. bmf1@ipla.csic.es.
authors.forename: Beatriz
authors.initials: B
authors.lastname: Martínez
keywords: Bacteriocins; Cell envelope stress; Lipid II; Mode of action; Peptidoglycan