Disease relevance of STM1028

• Salmonella typhimurium galE mutants in which O-antigen synthesis is dependent on addition of exogenous galactose were employed, and the distribution and fate of pulse-synthesized O antigen was examined by indirect ferritin labeling with anti-O-antigen IgG of spheroplasts prepared by treatment with lysozyme/EDTA [1].
• Sheep anti-human lysozyme antibody did not affect the bactericidal activity of C9DHS or NHS even when added at more than twice the concentration required to block the serum lysozyme activity on Micrococcus luteus [2].
• Low Brucella LPS-mediated superoxide and lysozyme production might contribute to the survival of these facultative intracellular bacteria in phagocytic cells [3].
• We also found that the food spoilage thermophile Clostridium thermosaccharolyticum was highly susceptible to lysozyme and confirmed that the spoilage organisms Bacillus stearothermophilus and Clostridium tyrobutyricum were also extremely sensitive [4].
• The results of this study suggest that lysozyme may have selected applications in food preservation, especially when thermophilic sporeformers are problems, and as a safeguard against food poisoning caused by C. botulinum and L. monocytogenes [4].

High impact information on STM1028

• Here we examined which of the layers of the cell wall limited the size of the penetrating molecules, by studying the penetration of saccharides into (a) cells whose peptidoglycan layer had been destroyed by lysozyme treatment or growth in the presence of penicillin and (b) isolated outer membrane vesicles [5].
• The comparison between Brucella LPS and lipid A versus Salmonella LPS revealed that at least 100 times more LPS and 1,000 times more lipid A of the former genus were required to induce significant nitroblue tetrazolium reduction and a corresponding lysozyme release in neutrophils [3].
• Effect of Brucella abortus lipopolysaccharide on oxidative metabolism and lysozyme release by human neutrophils [3].
• Larger lysine polymers and the protamine salmine were bactericidal but, at sublethal concentrations, sensitized the strains to the antibiotics mentioned above, whereas lysine4, streptomycin, cytochrome c, lysozyme, and the polyamines cadaverine, spermidine, and spermine had neither bactericidal nor sensitizing activity [6].
• Lysozyme was undetected throughout the course of the experiment, but was present in oil-induced peritoneal macrophages and peripheral mononuclear cells [7].

Chemical compound and disease context of STM1028

• Both Brucella abortus lipopolysaccharide (LPS) and lipid A were low activators of nitroblue tetrazolium reduction and lysozyme release in human neutrophils [3].
• The phosphoglycerate transport system was employed to supply energy-depleted, lysozyme-treated Salmonella typhimurium cells with a continuous intracellular source of phosphoenolpyruvate [8].
• Phage specific lysozyme is induced when the cultures are supplemented with elaidic, palmitelaidic, linoleic and linolelaidic acids but not with oleic and plamitoleic acids [9].
• Destruction of Salmonella on poultry meat with lysozyme, EDTA, x-ray, microwave and chlorine [10].

Biological context of STM1028

• The kinetics of increase in surface hydrophobicity was similar to the kinetics of the conversion of the substrate cell peptidoglycan to a lysozyme-resistant form (M. Thomashow and S. Rittenberg, J. Bacteriol. 135:1008-1014, 1978), and hydrophobicity reached a maximum at about 60 min in a synchronous culture [11].
• Human neutrophil defensins 1-3 (HNP 1-3) and lysozyme are components of the systemic innate immunity [12].
• Cell wall substrate specificity of six different lysozymes and lysozyme inhibitory activity of bacterial extracts [13].
• Binding was inhibited when the cell walls were subjected to treatment with metaperiodate or trichloroacetic acid but not when they were subjected to treatment with lysozyme, trypsin, or proteinase K, reflecting the role of the carbohydrate component as a binding site [14].
• Recombinant human tumor necrosis factor alpha, known for its ability to stimulate lysozyme in human macrophages and to elevate respiratory burst activity of rainbow trout macrophages, failed to stimulate lysozyme production of Atlantic salmon macrophages [15].

Anatomical context of STM1028

• Cell walls or outer membranes from which the mucopeptide had been removed by lysozyme digestion at 0 degrees C carried the label on the outer face of the membrane [16].
• Macrophages isolated from fish suffering from a non-lethal Ichthyobodo necator infection displayed a highly increased ability to produce lysozyme in response to both beta-glucan and LPS [15].
• METHODS: Mucosal tissue sections were studied by immunohistochemistry using antibodies to neutrophil defensins 1-3 and lysozyme [12].
• Effect of leukocyte hydrolases on bacteria. XV. Inhibition by antibiotics, metabolic inhibitors, and ultraviolet irradiation of the release by leukocyte extracts, trypsin, and lysozyme of lipopolysaccharide from gram-negative bacteria [17].
• RESULTS: Surface epithelial cells strongly immunoreactive for neutrophil defensins and lysozyme were seen in active ulcerative colitis and Crohn's disease (but not normal or inactive IBD) mucosal samples [12].

Associations of STM1028 with chemical compounds

• P. aeruginosa was effectively sensitized to lysozyme by lactic acid and by HCl [18].
• 2. When the murein layer was removed by either lysozyme or trypsin at physiological temperature (25-37 degrees C) subsequent labelling showed the lipopolysaccharide to be present on both membrane faces [16].
• The methods used were assays for lysozyme release and for nitroblue tetrazolium (NBT) reduction which measures the level of oxidative metabolism of neutrophils [19].
• Enhanced lysozyme production in Atlantic salmon (Salmo salar L.) macrophages treated with yeast beta-glucan and bacterial lipopolysaccharide [15].
• CONCLUSION: HNP 1-3 and lysozyme are expressed in surface enterocytes of mucosa with active IBD and they may play an important role in intestinal host defence against luminal microorganisms [12].

Analytical, diagnostic and therapeutic context of STM1028

• In this protocol, fixed cells are permeabilized with lysozyme and subjected to a seminested reverse transcriptase PCR using reporter molecule-labeled primers, and subsequently, intracellular reporter molecules are detected microscopically at the individual-cell level by use of a horseradish peroxidase-conjugated antifluorescein antibody assay [20].

References