Nucleic Acids Res 2008, 36:3420–3435.PubMedCrossRef Authors’ contributions CC and MFA performed the experimental design, carried out the protein fractionation and electrophoresis, performed data analysis, and drafted the manuscript. DP carried out the mass spectrometry identifications. BC participated in the design of the study. EC and LC performed animal diagnosis,
collection of animal samples, isolation, molecular identification, and cultivation of mycoplasmas. SU contributed to coordination of the study and data interpretation, and helped to draft the manuscript. AA and MP conceived I-BET151 purchase the study, participated in its design and coordination, and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background Bacteriocins are bacterial peptides or proteins inhibitory to bacteria closely related to the producer. Many of the bacteriocins produced by lactic acid bacteria (LAB) have inhibitory spectra spanning beyond the genus level and have a potential in defending unwanted microflora. Since they are produced by food grade bacteria, some are being used in food preservation. However, ZD1839 manufacturer LAB bacteriocins could have a potential in
the medical field. With the increasing spread of antibiotic resistance, the need for alternative antimicrobials is growing. Most of the bacteriocins of LAB are small, heat-stable, cationic peptides and are divided into two classes; class I, the lantibiotics containing modified amino acids and class II, the non-lantibiotics having regular amino acid residues [1]. Among the regular peptide bacteriocins, those belonging to class IIa are produced by a large number of LAB and are best studied [2]. These bacteriocins have highly conserved amino acid sequences, and have a largely common inhibitory spectrum which includes pathogens like Listeria monocytogenes and Enterococcus spp. Their mode of action is different from common
antibiotics [3, 4]. Bacterial MK0683 ic50 resistance towards these bacteriocins does not appear to be common in nature [5], while in laboratory experiments Myosin resistance to some bacteriocins appear at high frequency [6, 7]. Characterization of the resistant phenotype is important for assessment of the usefulness for application of bacteriocins. The target for class IIa bacteriocins is the mannose phosphotransferase system (mpt-PTS) [8–11], and mutants lacking a bacteriocin dedicated target are insensitive to the bacteriocin. This mannose PTS is the major uptake system for mannose and glucose in the bacteria [12]. PTS components are also involved in gene regulation of catabolic operons [13]. Hence bacteriocin resistance is likely to cause multiple effects. Among the effects seen in class IIa bacteriocin resistant strains of L. monocytogenes are changes in cell envelope, alterations in fatty acid composition [14–17], and a metabolic shift [18].