Effect of enterococcin A 2000 on biological and synthetic phospholipid membranes.

Int J Food Microbiol

Department of Microbiology, Faculty of Biology, University of Sofia, 8 bul. Dragan Tzankov, 1423, Sofia, Bulgaria.

Published: January 2003

Lactic acid bacterium isolated from Bulgarian cheese and identified as Enterococcus faecium produces a small hydrophobic peptide substance (enterococcin A 2000) with broad spectrum of antimicrobial activity. The wide range of enterococcin antibacterial activity of this compound against Gram-positive, as well as against some Gram-negative bacteria, suggests a single mechanism of action. The mode of action of enterococcin A 2000 was studied in intact liver mitochondria and synthetic phospholipid liposomes used as model systems. Enterococcin A 2000 stimulated the ATPase activity in intact mitochondria. The kinetic curve of ATP hydrolysis differed from that obtained in presence of dinitrophenol (DNP) and showed a character similar to the ATP hydrolysis in the presence of classic ionophores. Enterococcin A 2000, when bound to synthetic phospholipid liposomes, permeabilized liposomes liberating the marker carboxyfluorescein (CF).

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http://dx.doi.org/10.1016/s0168-1605(02)00143-5DOI Listing

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