AAC
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 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 Herranz, C.
Right arrow Articles by Driessen, A. J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Herranz, C.
Right arrow Articles by Driessen, A. J. M.

Antimicrobial Agents and Chemotherapy, March 2001, p. 901-904, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.901-904.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Enterocin P Causes Potassium Ion Efflux from Enterococcus faecium T136 Cells

Carmen Herranz,1,* Luis M. Cintas,1 Pablo E. Hernández,1 Gert N. Moll,2 and Arnold J. M. Driessen2

Departamento de Nutrición y Bromatología III, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain,1 and Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands2

Received 24 April 2000/Returned for modification 15 August 2000/Accepted 21 December 2000

Enterocin P is a bacteriocin produced by Enterococcus faecium P13. We studied the mechanism of its bactericidal action using enterocin-P-sensitive E. faecium T136 cells. The bacteriocin is incapable of dissipating the transmembrane pH gradient. On the other hand, depending on the buffer used, enterocin P dissipates the transmembrane potential. Enterocin P efficiently elicits efflux of potassium ions, but not of intracellularly accumulated anions like phosphate and glutamate. Taken together, these data demonstrate that enterocin P forms specific, potassium ion-conducting pores in the cytoplasmic membrane of target cells.


* Corresponding author. Mailing address: Departamento de Nutrición y Bromatología III, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain. Phone: 34913943750. Fax: 34913943743. E-mail: cburgy{at}eucmax.sim.ucm.es.


Antimicrobial Agents and Chemotherapy, March 2001, p. 901-904, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.901-904.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Clin. Vaccine Immunol. Clin. Microbiol. Rev.
J. Clin. Microbiol. ALL ASM JOURNALS

Copyright © 2001 by the American Society for Microbiology. All rights reserved.