Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis.

Date publication

février 2007

Auteurs

Membres identifiés du Cancéropôle Est :
Dr VAN DORSSELAER Alain

Tous les auteurs :
Chehimi S, Delalande F, Sable S, Hajlaoui MR, Van Dorsselaer A, Limam F, Pons AM

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/17496978

Résumé

We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3-10.5). The monoisotopic mass of thuricin S purified by high performance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

Référence

Can J Microbiol. 2007 Feb;53(2):284-90.