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 Kramer, N. E.
Right arrow Articles by Kuipers, O. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kramer, N. E.
Right arrow Articles by Kuipers, O. P.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, May 2006, p. 1753-1761, Vol. 50, No. 5
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.5.1753-1761.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Transcriptome Analysis Reveals Mechanisms by Which Lactococcus lactis Acquires Nisin Resistance

Naomi E. Kramer,{dagger} Sacha A. F. T. van Hijum, Jan Knol, Jan Kok, and Oscar P. Kuipers*

Molecular Genetics Group, Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands

Received 19 October 2005/ Returned for modification 18 January 2006/ Accepted 7 February 2006

Nisin, a posttranslationally modified antimicrobial peptide produced by Lactococcus lactis, is widely used as a food preservative. Yet, the mechanisms leading to the development of nisin resistance in bacteria are poorly understood. We used whole-genome DNA microarrays of L. lactis IL1403 to identify the factors underlying acquired nisin resistance mechanisms. The transcriptomes of L. lactis IL1403 and L. lactis IL1403 Nisr, which reached a 75-fold higher nisin resistance level, were compared. Differential expression was observed in genes encoding proteins that are involved in cell wall biosynthesis, energy metabolism, fatty acid and phospholipid metabolism, regulatory functions, and metal and/or peptide transport and binding. These results were further substantiated by showing that several knockout and overexpression mutants of these genes had strongly altered nisin resistance levels and that some knockout strains could no longer become resistant to the same level of nisin as that of the wild-type strain. The acquired nisin resistance mechanism in L. lactis is complex, involving various different mechanisms. The four major mechanisms are (i) preventing nisin from reaching the cytoplasmic membrane, (ii) reducing the acidity of the extracellular medium, thereby stimulating the binding of nisin to the cell wall, (iii) preventing the insertion of nisin into the membrane, and (iv) possibly transporting nisin across the membrane or extruding nisin out of the membrane.

* Corresponding author. Mailing address: Molecular Genetics Group, Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands. Phone: 31 50 3632093. Fax: 31 50 3632348. E-mail: o.p.kuipers{at}rug.nl.

{dagger} Present address: Public Health Research Institute, 225 Warren Street, Newark, NJ 07103.

Antimicrobial Agents and Chemotherapy, May 2006, p. 1753-1761, Vol. 50, No. 5
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.5.1753-1761.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sun, Z., Zhong, J., Liang, X., Liu, J., Chen, X., Huan, L. (2009). Novel Mechanism for Nisin Resistance via Proteolytic Degradation of Nisin by the Nisin Resistance Protein NSR. Antimicrob. Agents Chemother. 53: 1964-1973 [Abstract] [Full Text]  
  • Schneider, T., Gries, K., Josten, M., Wiedemann, I., Pelzer, S., Labischinski, H., Sahl, H.-G. (2009). The Lipopeptide Antibiotic Friulimicin B Inhibits Cell Wall Biosynthesis through Complex Formation with Bactoprenol Phosphate. Antimicrob. Agents Chemother. 53: 1610-1618 [Abstract] [Full Text]  
  • Giaouris, E., Briandet, R., Meyrand, M., Courtin, P., Chapot-Chartier, M.-P. (2008). Variations in the Degree of D-Alanylation of Teichoic Acids in Lactococcus lactis Alter Resistance to Cationic Antimicrobials but Have No Effect on Bacterial Surface Hydrophobicity and Charge. Appl. Environ. Microbiol. 74: 4764-4767 [Abstract] [Full Text]  
  • Kramer, N. E., Hasper, H. E., van den Bogaard, P. T. C., Morath, S., de Kruijff, B., Hartung, T., Smid, E. J., Breukink, E., Kok, J., Kuipers, O. P. (2008). Increased D-alanylation of lipoteichoic acid and a thickened septum are main determinants in the nisin resistance mechanism of Lactococcus lactis. Microbiology 154: 1755-1762 [Abstract] [Full Text]  
  • Guinane, C. M., Cotter, P. D., Lawton, E. M., Hill, C., Ross, R. P. (2007). Insertional Mutagenesis To Generate Lantibiotic Resistance in Lactococcus lactis. Appl. Environ. Microbiol. 73: 4677-4680 [Abstract] [Full Text]  
  • Veiga, P., Bulbarela-Sampieri, C., Furlan, S., Maisons, A., Chapot-Chartier, M.-P., Erkelenz, M., Mervelet, P., Noirot, P., Frees, D., Kuipers, O. P., Kok, J., Gruss, A., Buist, G., Kulakauskas, S. (2007). SpxB Regulates O-Acetylation-dependent Resistance of Lactococcus lactis Peptidoglycan to Hydrolysis. J. Biol. Chem. 282: 19342-19354 [Abstract] [Full Text]  
  • Neves, A. R., Pool, W. A., Castro, R., Mingote, A., Santos, F., Kok, J., Kuipers, O. P., Santos, H. (2006). The {alpha}-Phosphoglucomutase of Lactococcus lactis Is Unrelated to the {alpha}-D-Phosphohexomutase Superfamily and Is Encoded by the Essential Gene pgmH. J. Biol. Chem. 281: 36864-36873 [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»