Characterization and biological activity against Naegleria fowleri of amoebicins produced by Bacillus licheniformis D-13

Abstract

The strain Bacillus licheniformis D-13 produces three hydrophobic peptides (amoebicins d13-A, d13-B, and d13-C) that elicit antiamoebic activity against human-pathogenic and nonpathogenic species of Naegleria and have a broad spectrum of antibacterial activity. The three amoebicins have the same amino acid composition (three Asp, two Glu, two Val, and nine Leu residues) and molecular weight (1,870). Amoebicin d13-B causes lysis of amoebae through disorganization of the cell membrane. It also induces permeability to 86Rb and membrane disruption in asolectin vesicles.