Effect of enterococcin A 2000 on biological and synthetic phospholipid membranes.
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).
Pantev
A
A
Department of Microbiology, Faculty of Biology, University of Sofia, 8 bul. Dragan Tzankov, 1423, Sofia, Bulgaria. chobert@nantes.inra.fr
Valcheva
R
R
Danova
S
S
Ivanova
I
I
Minkov
I
I
Haertlé
T
T
Chobert
J-M
JM
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins; D001430:Bacteriocins / Q000302:isolation & purification / Q000494:pharmacology*; D002611:Cheese / Q000382:microbiology*; D016984:Enterococcus faecium / Q000378:metabolism*; D005516:Food Microbiology; D006868:Hydrolysis; D007700:Kinetics; D008081:Liposomes / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats
D001426:Bacterial Proteins; D001430:Bacteriocins; D008081:Liposomes; D000251:Adenosine Triphosphatases