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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.


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