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Etude des relations structure/fonction d'une bactériocine anti-Listeria, la mésentéricine Y105

Abstract : Mesentericin Y105 is a sub-class IIa bacteriocin produced by Leuconostoc mesenteroides Y105. In an attempt to understand the mecanism of its anti-listerial activity, we investigated the peptides structure-function relationship. For this purpose, a bank of mesentericins Y105 peptide derivates was created with modifications at single positions of the parent peptide. Peptide derivatives were generated using, randomly primed PCR mutagenesis to create single mutations in the DNA sequences that encode the mature peptide. A method for heterologous production based on a two componant system with one vector harboring structural gene, and one other encoding the immunity protein and transport system was optimized .Thus, an universal peptide secretion tool has been established. The impact of mutations was studied for the mesentericin Y105 derivatives, by accessing there activity, secondary structure (obtained by circular dichroism in trifluoroethanol and lysophosphatidylcholin micelles), predicted tertiary structure and interaction with anisotropic environment (method of tryptophan blue shift). Finally, a nuclear magnetic resonance analysis was used to determinate the native bacteriocin structure. A general model for the mechanism of action of mesentericin Y105 and its related bacteriocins is proposed.
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Submitted on : Friday, January 21, 2011 - 12:27:30 PM
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Dany Morisset. Etude des relations structure/fonction d'une bactériocine anti-Listeria, la mésentéricine Y105. Biochimie [q-bio.BM]. Université de Poitiers, 2003. Français. ⟨tel-00558243⟩

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