This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moll, G. N.
Right arrow Articles by Driessen, A. J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moll, G. N.
Right arrow Articles by Driessen, A. J. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 1998, p. 6565-6570, Vol. 180, No. 24
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

Gert N. Moll, Wil N. Konings, and Arnold J. M. Driessen*

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.

* 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.

Journal of Bacteriology, December 1998, p. 6565-6570, Vol. 180, No. 24
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Kuipers, A., de Boef, E., Rink, R., Fekken, S., Kluskens, L. D., Driessen, A. J. M., Leenhouts, K., Kuipers, O. P., Moll, G. N. (2004). NisT, the Transporter of the Lantibiotic Nisin, Can Transport Fully Modified, Dehydrated, and Unmodified Prenisin and Fusions of the Leader Peptide with Non-lantibiotic Peptides. J. Biol. Chem. 279: 22176-22182 [Abstract] [Full Text]  
  • Makino, A., Baba, T., Fujimoto, K., Iwamoto, K., Yano, Y., Terada, N., Ohno, S., Sato, S. B., Ohta, A., Umeda, M., Matsuzaki, K., Kobayashi, T. (2003). Cinnamycin (Ro 09-0198) Promotes Cell Binding and Toxicity by Inducing Transbilayer Lipid Movement. J. Biol. Chem. 278: 3204-3209 [Abstract] [Full Text]  
  • Benech, R.-O., Kheadr, E. E., Lacroix, C., Fliss, I. (2002). Antibacterial Activities of Nisin Z Encapsulated in Liposomes or Produced In Situ by Mixed Culture during Cheddar Cheese Ripening. Appl. Environ. Microbiol. 68: 5607-5619 [Abstract] [Full Text]  
  • Hrafnsdóttir, S., Menon, A. K. (2000). Reconstitution and Partial Characterization of Phospholipid Flippase Activity from Detergent Extracts of the Bacillus subtilis Cell Membrane. J. Bacteriol. 182: 4198-4206 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»