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Journal of Bacteriology, December 1998, p. 6565-6570, Vol. 180, No. 24
Department of Microbiology and Groningen
Biomolecular Sciences and Biotechnology Institute, University of
Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
Received 13 July 1998/Accepted 15 October 1998
Nisin is a pore-forming antimicrobial peptide. The capacity of
nisin to induce transmembrane movement of a fluorescent phospholipid in
lipid vesicles was investigated. Unilamellar phospholipid vesicles that
contained a fluorescent phospholipid
(1-acyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]caproyl}-sn-glycero-3-phosphocholine) in the inner leaflet of the bilayer were used. Nisin-induced movement of the fluorescent phospholipid from the inner leaflet to the outer
leaflet of the membrane reached stable levels, which were dependent on
the concentration of nisin added. The rate constant k of
this nisin-induced transmembrane movement increased with the nisin
concentration but was not dependent on temperature within the range of
5 to 30°C. In contrast, the rate constant of movement of fluorescent
phospholipid from vesicle to vesicle strongly depended on temperature.
The data indicate that nisin transiently disturbs the phospholipid
organization of the target membrane.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Lantibiotic Nisin Induces Transmembrane
Movement of a Fluorescent Phospholipid
*
Corresponding author. Mailing address: Department of
Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. Phone: (31) (50) 3632164. Fax: (31) (50) 3632154. E-mail:
A.J.M.DRIESSEN{at}BIOL.RUG.NL.
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