Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis.
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.
Chehimi
Sonia
S
Laboratoire de biotechnologies et de chimie bio-organique, Pôle Sciences, Université de La Rochelle, 17042 La Rochelle CEDEX 01, France. chehimisonia@yahoo.fr
Delalande
François
F
Sablé
Sophie
S
Hajlaoui
Mohamed-Rabeh
MR
Van Dorsselaer
Alain
A
Limam
Férid
F
Pons
Anne-Marie
AM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001413:Bacillus thuringiensis / Q000737:chemistry*; D001430:Bacteriocins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D008087:Listeria / Q000187:drug effects*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight
D000596:Amino Acids; D001430:Bacteriocins; C059740:thuricin