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. 1994 Jun;38(6):1314–1319. doi: 10.1128/aac.38.6.1314

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

A Gálvez 1, M Maqueda 1, P Cordovilla 1, M Martínez-Bueno 1, M Lebbadi 1, E Valdivia 1
PMCID: PMC188204  PMID: 8092831

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.

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Selected References

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