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At least 55 records · Page 3Linked to original sources
PubMed1977

Bacteriolysis by immobilized enzymes.

Bacteriolytic enzymes produced by Achromobacter lunatus were immobilized in collagen membrane. Intact bacteria such as Pseudomonas solanacearum, Xanthomonas oryzae, Staphylococcus aureus, and Pseudomonas aeruginosa were lyzed with the bacteriolytic enzyme-collagen membrane. Relative activity of the bacteriolytic enzyme-collagen membrane against Pseu. solanacearum was about 2% of that of native bacteriolytic enzymes. No difference in the optimum pH was observed between immobilized enzymes and native enzymes. The bacteriolytic enzymes in the collagen membrane were stable against sodium chloride which was an inhibitor of the native bacteriolytic enzymes. Xanthomonas oryzae and Pseu. aeruginosa were continuously lyzed by a reactor containing the rolled bacteriolytic enzyme-collagen membrane.

Alcaligenes↗
PubMed1989

Bacteriolysis is inhibited by hydrogen peroxide and by proteases.

Treatment of Staphylococcus aureus in vitro with cationic agents results in the activation of their autolytic wall enzymes and in the degradation of their cell walls. Exposure of staphylococci either to hydrogen peroxide or the proteinases abolished the autolytic process. This effect was totally reversed by catalase and by proteinase inhibitors, respectively. It is suggested that the failure of neutrophils and macrophages to effectively degrade microbial cell wall components in inflammatory sites might be due to the inactivation of the autolytic wall enzymes of bacteria by hydrogen peroxide and by proteinases generated by the activated leukocytes. This might explain the prolonged chronic inflammatory sequelae seen following infections.

Bacteriolysis↗
PubMed1983

Synergism of lysozyme, proteases and inorganic monovalent anions in the bacteriolysis of oral Streptococcus mutans GS5.

Streptococcus mutans GS5 was grown in synthetic medium containing radioactive thymidine to monitor deoxyribonucleic acid release. At neutral pH, cell lysis of hen egg-white lysozyme- or lysozyme-protease-treated cells was dependent upon the nature and concentration of the additive inorganic anions, HCO-3, SCN-, Cl- or F-. At acidic pH, NaHCO3, but not NaSCN, NaCl or NaF, was effective in promoting cell lysis which was due not only to the change in pH but also to the new HCO-3 anion concentration at the new pH. In both pH 4 and 5.2 reaction mixtures, the lysozyme and trypsin acted synergistically with NaHCO3 and the amount of lysis produced was markedly greater than in reaction mixtures containing lysozyme and bicarbonate but no protease. At apparent sub-lytic concentrations of NaHCO3, lysis was achieved by adding an appropriate concentration of one of NaSCN, NaCl or NaF to the lysozyme-protease-damaged cells. Thiocyanate proved to be most effective among the anions requiring lower concentrations to elicit lysis compared to chloride or fluoride for a fixed sub-lytic concentration of bicarbonate. As the NaHCO3 concentration increased, the lysis in the presence of these other anions increased until maximum levels of released deoxyribonucleic acid (DNA) were attained. In addition, the higher the NaHCO3 concentration, the more marked was the change in the degree of cell lysis. At a selected concentration at which NaHCO3 was not effective with any one salt, lysis could be achieved by combining all four inorganic anions at this concentration. The results suggest that the various anions present in oral fluids may together be sufficient to trigger lysis of oral microorganisms.

Anions↗
PubMed1986

Modulation of bacteriolysis by cooperative effects of penicillin-binding proteins 1a and 3 in Escherichia coli.

Escherichia coli characteristically lyses upon treatment with most beta-lactam antimicrobial agents. In contrast, an investigational aminothiazole cephem, CGP 31523A, produced a new combination of antibacterial effects: it was highly bactericidal without causing cell wall degradation or lysis. Killing was associated with the formation of vacuolated filaments. Because the compound bound to penicillin-binding proteins (PBPs) 1a and 3, we investigated the role of PBP 3 in modulation of lysis caused by inhibition of PBP 1a. A temperature-sensitive mutant with a nonfunctional PBP 3 lysed when treated with CGP 31523A. The combination of a PBP 1 inhibitor (cefsulodin) and a PBP 3 inhibitor (aztreonam) also caused filamentation and death without lysis of wild-type cells over a narrow concentration range. We conclude that cooperative effects between PBPs in E. coli can lead to a dissociation of bacterial killing and lysis.

Acyltransferases↗
PubMed1971

Bacteriolysis and inhibition of gram-positive bacteria by components of Streptococcus zymogenes lysin.

The ability of the A and L components of Streptococcus zymogenes lysin to cause lysis or to inhibit growth of a variety of gram-positive bacteria has been examined. Frank lysis of some, but not all, strains of S. faecalis, S. faecium, and S. liquefaciens by L component alone was demonstrated. None of the strains of these species was lysed by A component alone. S. durans was not lysed by either component. Inhibition of growth of all enterococcal strains by both A substance-producing and L substance-producing mutants of S. zymogenes was also demonstrated. However, inhibition by the A substance producer was markedly less than by the L substance producer. Inhibition of the growth of a number of other gram-positive genera by both A and L mutants was also noted.

Bacteriological Techniques↗
PubMed1995

Beta-lactam-induced bacteriolysis of amino acid-deprived Escherichia coli is dependent on phospholipid synthesis.

The penicillin tolerance of amino acid-deprived relA+ Escherichia coli is attributed to the stringent response; i.e., relaxation of the stringent response suppresses penicillin tolerance. The beta-lactam-induced lysis of amino acid-deprived bacteria resulting from relaxation of the stringent response was inhibited by cerulenin, or by glycerol deprivation in the case of a gpsA mutant (defective in the biosynthetic sn-glycerol 3-phosphate dehydrogenase). Therefore, beta-lactam-induced lysis of amino acid-deprived cells was dependent on phospholipid synthesis. The lysis process during amino acid deprivation can be experimentally dissociated into two stages designated the priming stage (during which the interaction between the beta-lactam and the penicillin-binding proteins occurs) and the beta-lactam-independent lysis induction stage. Both stages were shown to require phospholipid synthesis. It has been known for some time that the inhibition of phospholipid synthesis is among the plethora of physiological changes resulting from the stringent response. These results indicate that the inhibition of peptidoglycan synthesis and the penicillin tolerance associated with the stringent response are both secondary consequences of the inhibition of phospholipid synthesis.

Ampicillin↗