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 Fimland, G.
Right arrow Articles by Nissen-Meyer, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fimland, G.
Right arrow Articles by Nissen-Meyer, J.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2000, p. 2643-2648, Vol. 182, No. 9
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A C-Terminal Disulfide Bridge in Pediocin-Like Bacteriocins Renders Bacteriocin Activity Less Temperature Dependent and Is a Major Determinant of the Antimicrobial Spectrum

Gunnar Fimland,1,* Line Johnsen,1 Lars Axelsson,2 May B. Brurberg,3,4 Ingolf F. Nes,4 Vincent G. H. Eijsink,4 and Jon Nissen-Meyer1

Department of Biochemistry, University of Oslo, Oslo,1 and MATFORSK, Norwegian Food Research Institute,2 Norwegian Crop Research Institute,3 and Department of Chemistry and Biotechnology, Agricultural University of Norway,4 Ås, Norway

Received 4 November 1999/Accepted 4 February 2000

Several lactic acid bacteria produce so-called pediocin-like bacteriocins that share sequence characteristics, but differ in activity and target cell specificity. The significance of a C-terminal disulfide bridge present in only a few of these bacteriocins was studied by site-directed mutagenesis of pediocin PA-1 (which naturally contains the bridge) and sakacin P (which lacks the bridge). Introduction of the C-terminal bridge into sakacin P broadened the target cell specificity of this bacteriocin, as illustrated by the fact that the mutants were 10 to 20 times more potent than the wild-type toward certain indicator strains, whereas the potency toward other indicator strains remained essentially unchanged. Like pediocin PA-1, disulfide-containing sakacin P mutants had the same potency at 20 and 37°C, whereas wild-type sakacin P was approximately 10 times less potent at 37°C than at 20°C. Reciprocal effects on target cell specificity and the temperature dependence of potency were observed upon studying the effect of removing the C-terminal disulfide bridge from pediocin PA-1 by Cysright-arrowSer mutations. These results clearly show that a C-terminal disulfide bridge in pediocin-like bacteriocins contributes to widening of the antimicrobial spectrum as well as to higher potency at elevated temperatures. Interestingly, the differences between sakacin P and pediocin PA-1 in terms of the temperature dependency of their activities correlated well with the optimal temperatures for bacteriocin production and growth of the bacteriocin-producing strain.

* Corresponding author. Mailing address: Department of Biochemistry, University of Oslo, Post Box 1041, Blindern, 0316 Oslo, Norway. Phone: 47-22 85 66 32. Fax: 47-22 85 44 43. E-mail: gunnar.fimland{at}biokjemi.uio.no.

Journal of Bacteriology, May 2000, p. 2643-2648, Vol. 182, No. 9
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Rihakova, J., Petit, V. W., Demnerova, K., Prevost, H., Rebuffat, S., Drider, D. (2009). Insights into Structure-Activity Relationships in the C-Terminal Region of Divercin V41, a Class IIa Bacteriocin with High-Level Antilisterial Activity. Appl. Environ. Microbiol. 75: 1811-1819 [Abstract] [Full Text]  
  • Haugen, H. S., Kristiansen, P. E., Fimland, G., Nissen-Meyer, J. (2008). Mutational Analysis of the Class IIa Bacteriocin Curvacin A and Its Orientation in Target Cell Membranes. Appl. Environ. Microbiol. 74: 6766-6773 [Abstract] [Full Text]  
  • Tominaga, T., Hatakeyama, Y. (2007). Development of Innovative Pediocin PA-1 by DNA Shuffling among Class IIa Bacteriocins. Appl. Environ. Microbiol. 73: 5292-5299 [Abstract] [Full Text]  
  • Oppegard, C., Fimland, G., Thorbaek, L., Nissen-Meyer, J. (2007). Analysis of the Two-Peptide Bacteriocins Lactococcin G and Enterocin 1071 by Site-Directed Mutagenesis. Appl. Environ. Microbiol. 73: 2931-2938 [Abstract] [Full Text]  
  • Drider, D., Fimland, G., Hechard, Y., McMullen, L. M., Prevost, H. (2006). The Continuing Story of Class IIa Bacteriocins. Microbiol. Mol. Biol. Rev. 70: 564-582 [Abstract] [Full Text]  
  • Tominaga, T., Hatakeyama, Y. (2006). Determination of Essential and Variable Residues in Pediocin PA-1 by NNK Scanning. Appl. Environ. Microbiol. 72: 1141-1147 [Abstract] [Full Text]  
  • Johnsen, L., Fimland, G., Nissen-Meyer, J. (2005). The C-terminal Domain of Pediocin-like Antimicrobial Peptides (Class IIa Bacteriocins) Is Involved in Specific Recognition of the C-terminal Part of Cognate Immunity Proteins and in Determining the Antimicrobial Spectrum. J. Biol. Chem. 280: 9243-9250 [Abstract] [Full Text]  
  • Morisset, D., Berjeaud, J.-M., Marion, D., Lacombe, C., Frere, J. (2004). Mutational Analysis of Mesentericin Y105, an Anti-Listeria Bacteriocin, for Determination of Impact on Bactericidal Activity, In Vitro Secondary Structure, and Membrane Interaction. Appl. Environ. Microbiol. 70: 4672-4680 [Abstract] [Full Text]  
  • Richard, C., Drider, D., Elmorjani, K., Marion, D., Prevost, H. (2004). Heterologous Expression and Purification of Active Divercin V41, a Class IIa Bacteriocin Encoded by a Synthetic Gene in Escherichia coli. J. Bacteriol. 186: 4276-4284 [Abstract] [Full Text]  
  • Johnsen, L., Fimland, G., Mantzilas, D., Nissen-Meyer, J. (2004). Structure-Function Analysis of Immunity Proteins of Pediocin-Like Bacteriocins: C-Terminal Parts of Immunity Proteins Are Involved in Specific Recognition of Cognate Bacteriocins. Appl. Environ. Microbiol. 70: 2647-2652 [Abstract] [Full Text]  
  • Katla, T., Naterstad, K., Vancanneyt, M., Swings, J., Axelsson, L. (2003). Differences in Susceptibility of Listeria monocytogenes Strains to Sakacin P, Sakacin A, Pediocin PA-1, and Nisin. Appl. Environ. Microbiol. 69: 4431-4437 [Abstract] [Full Text]  
  • Fimland, G., Eijsink, V. G. H., Nissen-Meyer, J. (2002). Comparative studies of immunity proteins of pediocin-like bacteriocins. Microbiology 148: 3661-3670 [Abstract] [Full Text]  
  • Kazazic, M., Nissen-Meyer, J., Fimland, G. (2002). Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P. Microbiology 148: 2019-2027 [Abstract] [Full Text]  
  • Uteng, M., Hauge, H. H., Brondz, I., Nissen-Meyer, J., Fimland, G. (2002). Rapid Two-Step Procedure for Large-Scale Purification of Pediocin-Like Bacteriocins and Other Cationic Antimicrobial Peptides from Complex Culture Medium. Appl. Environ. Microbiol. 68: 952-956 [Abstract] [Full Text]  
  • Cintas, L. M., Casaus, P., Herranz, C., Håvarstein, L. S., Holo, H., Hernández, P. E., Nes, I. F. (2000). Biochemical and Genetic Evidence that Enterococcus faecium L50 Produces Enterocins L50A and L50B, the sec-Dependent Enterocin P, and a Novel Bacteriocin Secreted without an N-Terminal Extension Termed Enterocin Q. J. Bacteriol. 182: 6806-6814 [Abstract] [Full Text]  
  • Johnsen, L., Fimland, G., Eijsink, V., Nissen-Meyer, J. (2000). Engineering Increased Stability in the Antimicrobial Peptide Pediocin PA-1. Appl. Environ. Microbiol. 66: 4798-4802 [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»