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Volume 272, Number 22, Issue of May 30, 1997 pp. 14277-14284
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Thermophilin 13, a Nontypical Antilisterial Poration Complex Bacteriocin, That Functions without a Receptor

(Received for publication, September 19, 1996, and in revised form, February 18, 1997)

Olivier Marciset ^§ , Margot C. Jeronimus-Stratingh ^¶ , Beat Mollet ^§ and Bert Poolman

From the  Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, the ^§ Nestlé Research Center, Nestec Ltd., Vers-Chez-Les-Blanc, P.O. Box 44, CH-1000 Lausanne 26, Switzerland, and the ^¶ Centre for Pharmacy, University of Groningen, A. Deusinglaan 2, 9713 AW Groningen, The Netherlands

A novel broad host range antimicrobial substance, Thermophilin 13, has been isolated and purified from the growth medium of Streptococcus thermophilus. Thermophilin 13 is composed of the antibacterial peptide ThmA (M_r of 5776) and the enhancing factor ThmB (M_r of 3910); the latter peptide increased the activity of ThmA ~40 ×. Both peptides are encoded by a single operon, and an equimolar ratio was optimal for Thermophilin 13 activity. Despite the antilisterial activity of Thermophilin 13, neither ThmA nor ThmB contain the YGNGV-C consensus sequence of Listeria-active peptides, and post-translational modifications comparable to that in the lantibiotics are also absent. Mass spectrometry did reveal the apparent oxidation of methionines in ThmA, which resulted in a peptide that could not be enhanced any longer by ThmB, whereas the intrinsic bactericidal activity was normal. Thermophilin 13 dissipated the membrane potential and the pH gradient in liposomes, and this activity was independent of membrane components from a sensitive strain (e.g. lipid or proteinaceous receptor). Models of possible poration complexes formed are proposed on the basis of sequence comparisons, structure predictions, and the functional analysis of Thermophilin 13.

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