Mechanism of bactericidal activity of microcin L in Escherichia coli and Salmonella enterica.

For the first time, the mechanism of action of microcin L (MccL) was investigated in live bacteria. MccL is a gene-encoded peptide produced by Escherichia coli LR05 that exhibits a strong antibacterial activity against related Enterobacteriaceae, including Salmonella enterica serovars Typhimurium and Enteritidis. We first subcloned the MccL genetic system to remove the sequences not involved in MccL production.

Mode of action of thuricin S, a new class IId bacteriocin from Bacillus thuringiensis.

Different methods were used to elucidate the mode of action of thuricin S, a new class IId bacteriocin produced by Bacillus thuringiensis subsp. entomocidus HD198. According to cell viability tests, thuricin S was shown to exert a bactericidal effect on the sensitive cells of Bacillus thuringiensis subsp.

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.

Two vibrio splendidus related strains collaborate to kill Crassostrea gigas: taxonomy and host alterations.

For several years, strains phenotypically related to Vibrio splendidus have been associated with mortality outbreaks of molluscs. A former study on Crassostrea gigas demonstrated the genetic diversity of V. splendidus strains associated with diseased animals.

Genetic analysis and complete primary structure of microcin L.

Escherichia coli LR05, in addition to producing MccB17, J25, and D93, secretes microcin L, a newly discovered microcin that exhibits strong antibacterial activity against related Enterobacteriaceae, including Salmonella enterica serovars Typhimurium and Enteritidis. Microcin L was purified using a two-step procedure including solid-phase extraction and reverse-phase C(18) high-performance liquid chromatography. A 4,901-bp region of the DNA plasmid of E.

Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.

The mechanism of action of microcin E492 (MccE492) was investigated for the first time in live bacteria. MccE492 was expressed and purified to homogeneity through an optimized large-scale procedure. Highly purified MccE492 showed potent antibacterial activity at minimal inhibitory concentrations in the range of 0.

New developments in non-post translationally modified microcins.

Microcins are a family of low molecular weight antibiotic peptides produced by Enterobacteriaceae strains and active against related bacteria. According to some features we propose to classify these antibiotic substances into two distinct groups. The class I microcins contain Mcc B17, C7, J25 and D93 that are small molecules (molecular mass inferior to 5 kDa), largely post-translationally modified and with specific intracellular targets.

Antibacterial, antifungal and cytotoxic activities of extracts from fish epidermis and epidermal mucus.

Annual discards from the world fisheries are estimated to be approximately 20 million metric tonnes (25%) per year. The main objective of this work is to increase the utilisation of by-products (notably skin) from fish species in order to isolate new biologically active compounds. This study presents the results of a screening program for antifungal, antibacterial and cytotoxic activities in epidermal mucus and epidermis extracts of thirteen fish species that are commonly caught in North Atlantic waters and generate an important amount of fish waste.

Microcin E492 is an unmodified peptide related in structure to colicin V.

The pore-forming microcin E492 was purified by solid-phase extraction and reversed-phase high-pressure liquid chromatography. Its molecular mass was 7,886 Da. The entire 84-amino-acid sequence was determined.