Identification of Three Novel  B. thuringiensis  Strains that Produce the Thuricin S Bacteriocin

Sonia Chehimi<sup>1</sup>; Ferid Limam<sup>2</sup>; Isabelle Lanneluc<sup>1</sup>; Franeois Delalande<sup>3</sup>; Alain van Dorsselaer<sup>3</sup>; Sophie Sable<sup>1</sup>

Research Report

Identification of Three Novel B. thuringiensis Strains that Produce the Thuricin S Bacteriocin

Sonia Chehimi¹

, Ferid Limam²

, Isabelle Lanneluc¹

, Franeois Delalande³

, Alain van Dorsselaer³

, Sophie Sable¹

1. Littoral environnement et societes (LIENSs), Universite de La Rochelle, 17042 La Rochelle CEDEX 1, France
2. Laboratoire des substances bioactives, Centre de Biotechnologie de Borj-Cedria, BP 901-2050 Hammam-lif, Tunisia
3. Laboratoire de spectrometrie de masse bio-organique, Universite Louis Pasteur, 67087 Strasbourg CEDEX 2, France

Author

Correspondence author
Bt Research, 2012, Vol. 3, No. 2 doi: 10.5376/bt.2012.03.0002
Received: 10 Jan., 2012 Accepted: 02 Feb., 2012 Published: 20 Feb., 2012

This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Preferred citation for this article:

Chehimi et al., 2012, Identification of Three Novel B. thuringiensis Strains that Produce the Thuricin S bacteriocin, Bt Research, Vol.3, No.2 3-10 (doi: 10.5376/bt.2012.03.0002)

Abstract

In the present work, three antibacterial substances produced by three Bacillus thuringiensis strains: Bacillus thuringiensis subsp. entomocidus HD9, Bacillus thuringiensis subsp. entomocidus HD110 and Bacillus thuringiensis subsp. tolworthy HD125 were used to study the bacteriocin diversity within Bacillus thuringiensis species. The inhibitory substances produced by these strains were purified to homogeneity by reverse phase high-performance liquid chromatography and were identified as bacteriocins. These molecules were all sensitive to proteinase K, heat-resistant and stable over a wide range of pH (3-10.5). Mass spectrometry ESI-TOF-MS analysis provided the monoisotopic masses of the three newly identified bacteriocins. The N-terminal amino acid sequences were also determined by Edman sequencing and by nanoESI-MS/MS experiments. Interestingly, the three newly identified bacteriocins shared the same molecular mass and the same N-terminal sequence with the anti-Listeria bacteriocin: thuricin S, produced by Bacillus thuringiensis subsp. entomocidus HD198 strain. Thereby, we demonstrated at the biochemical level and for the first time that four different Bacillus thuringiensis strains produce the same bacteriocin.