Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Normal rat serum shows antibacterial activity because of the presence of endogenous substances. The aim of this research was to study some aspects of the interaction between this biological fluid and some antibiotics, in order to demonstrate possible synergistic activity. Serum is able to lower the minimum inhibitory concentration of gentamicin and ofloxacin against some Gram-negative microorganisms. This can be explained by the presence of lysozyme, antibodies, beta-lysin and other complementary factors that are able to cooperate with these antibiotics.
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PMID:Enhancement of in-vitro activity of ofloxacin and gentamicin by rat serum. 209 7

Numerous studies have demonstrated that patients with dry eyes have a compromised ocular surface. Furthermore, these patients suffer deficiencies of various surface defense mechanisms, such as tear volume, tear components (lysozyme, lactoferrin, and beta-lysin), the mucin network, cellular exfoliation, and subsurface immune secretions. When such individuals wear contact lenses (CLs), a special set of circumstances arises that increases the risk of ocular infection. The risk is greatest if the lenses are soft and, therefore, provide for little tear exchange beneath their surface. Under such circumstances, limited tear flow allows for a greater buildup of lens deposits and metabolic wastes, while permitting increased tear evaporation from the lens surface. The pathogenesis of infection is attributed to various mechanisms, including decreased tear flow beneath the lens, decreased tear components, stagnation of the mucin network, changes in surface cell exfoliation, and putative changes in the subsurface immune secretory system. Dry eye patients who wear soft CLs also run a greater risk of bacterial conjunctivitis, blepharitis, and sterile corneal infiltrates.
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PMID:Is the dry eye contact lens wearer at risk? Yes. 218 82

The lysA gene specifying an endolysin of Lactobacillus delbrueckii subsp. bulgaricus bacteriophage mv1, was cloned and expressed in Escherichia coli. The 4.05-kb restriction fragment containing this gene was analysed by restriction and deletion mapping, and by subcloning. The nucleotide sequence of a 1150-bp fragment coding for an active lysin was determined. The lysA gene consists of 585 bp and codes for a protein of a deduced Mr of 21,120, which agrees with the size based on in vivo transcription/translation studies. The deduced amino acid sequence of the mv1 lysin (LysA) was compared to that of other known lytic enzymes. Significant homology was observed with the N-terminal portion of the muramidase of the fungus Chalaropsis and that of the muramidase of the Streptococcus pneumoniae phage Cp-1, suggesting that LysA might be a muramidase. In E. coli, the cloned lysA gene was able to complement the muramidase-defective bacteriophage lambda Ram5, proving that the products of these two genes are interchangeable. The lysA gene is preceded by an open reading frame with unknown function and no characteristic prokaryotic promoter sequences could be detected upstream from lysA, suggesting that this gene is part of an operon.
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PMID:Cloning, expression and sequence analysis of an endolysin-encoding gene of Lactobacillus bulgaricus bacteriophage mv1. 222 53

The course of beta + lysin level and lysozyme activity in the gingival capillary blood serum was investigated in periodontitis patients immediately after treatment with indomethacin ointment with prolonged effect. Additional investigation confirmed that inflammation stabilized after the treatment. X-ray showed that the cortical plate increased in density, as did the partially resorbed margins of interalveolar septa. Osteoporosis focuses faded. The data evidence the high efficiency of the prolonged effect ointment in the combined treatment of generalized periodontitis.
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PMID:[The use of a prolonged-action indomethacin ointment in the combined treatment of periodontitis]. 274 10

The state of pregnancy changes the immune system by allowing the trophoblast to go on developing without letting the mother's body be invaded by it, and by keeping intact immune defences against the usual assaults. The non specific immune system is the first bulwark against invaders. The elements of this system, which do not depend on immunological memory, are: the macrophage-monocyte system, Natural Killer cells (NK), the complement component and other bactericidal substances such as lysozyme, fibronectin and interferon. Pregnancy improves the working of the monocyte-macrophage system. In fact, the macrophages of th reticulo-endothelial system, which can be found in different strategic places in the body, phagocytose abnormal particles more intensely. The monocytes in the circulation are more aggressive in pregnancy. They are drawn to the feto-placental interface where they are activated by different lymphokines and cytokines which can be found in quantity at this site. The role of these local active monocytes is not limited only to phagocytosis because among the hundred substances that they can elaborate are some that will regulate trophoblastic proliferation. The activity of the Natural Killer cells that are circulating and which can control tumour cell growth and cells infected by viruses is lowered in pregnancy. The serum taken from pregnant women seems to have a substance that counters the maturation of the Natural Killer cell lines. The complement system of protein synthesis, which normally acts to lyse bacteria in the chemotaxis during opsonisation, is raised in pregnancy. At the feto-placental interface it does seem to activate this system but not elsewhere in the general circulation. Interferon, which is a molecule that normally activates NK cells, has been found at the feto-placental site, without seeming to have a particular role. Pregnancy changes the quantity and the distribution of other elements in the non specific immune system such as transferrin , fibronectin and beta-lysin.
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PMID:[Non-specific immune defenses present in pregnancy]. 306 97

Ampicillin, fusidic acid, gentamicin, imipenem, mezlocillin, ofloxacin, penicillin G, piperacillin, and vancomycin were examined for inhibitory and bactericidal activity in various broth media against 7 clinical isolates of Streptococcus faecalis. On a weight-for-weight basis, ampicillin, imipenem, mezlocillin, and ofloxacin proved to be more efficacious. All enterococcal isolates were resistant against gentamicin; fusidic acid and vancomycin lacked bactericidal activity. The combinations of either ampicillin, imipenem, mezlocillin, ofloxacin, piperacillin, or vancomycin with a subinhibitory concentration (4 micrograms/ml) of gentamicin, with or without added 65% (v/v) fresh defibrinated human blood, respectively, yielded additive effects against all enterococcal isolates. The addition of fresh human blood failed to enhance the antienterococcal activity of 4 micrograms/ml of gentamicin; in contrast, addition of 65% (v/v) fresh or heat-inactivated (56 degrees C, 30 min) normal rabbit, bovine, and human sera augmented the activity of gentamicin, an effect that was ablated through the addition of either 0.005 M DTT or 0.01 M MgCl2 + 0.01 M EGTA + 0.01 M CaCl2, supplements known to antagonize human serum beta-lysin, but not lysozyme activity.
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PMID:Streptococcus faecalis: in vitro susceptibility to antimicrobial drugs, single and combined, with and without defibrinated human blood. 308 51

Streptococci and streptococcal cell wall fragments induce arthritis in rats, with the severity and duration depending on the capacity of the cells or cell fragments to resist degradation by tissue enzymes. Their phlogogenic effects are apparently related to their ability to activate the alternate complement pathway (ACP). The in vitro activation of the ACP by lysozyme-treated cells and cell walls of group A, B, and D streptococci suggests that both rat and human lysozyme can modulate this activity, i.e., increasing it, decreasing it, or doing both in that order. The effects of the lysozymes also correlated with the degree to which they can unmask the aminosugar-reducing groups detectable in a given amount of cell wall, which suggests that partial depolymerization of the cell wall is critical for ACP activation. The effects of mutanolysin and C phage lysin on ACP activation were found to be correlated with their action on streptococcal cell walls. Neuraminidase had relatively little effect on ACP activation by most streptococcal strains tested. We conclude that the participation of tissue enzymes, including but not necessarily limited to lysozyme, is an important determinant for the clinical arthritis induced by group A, B, or D streptococci. Experimental arthritis induced in rats with whole (or disrupted) streptococci may depend both on the capacities of the cell walls to activate the ACP and on the capacities of the host tissue enzymes to modulate this activation. Great severity and long durations of the disease were determined by the capacity of the enzymes to degrade cell wall antigens to a degree sufficient to ensure efficient activation of the ACP without completely degrading the material so that it no longer activates complement. In this model, the limited resistance of group B peptidoglycan to lysozyme was a critical pathogenic factor.
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PMID:Modulation of complement fixation and the phlogistic capacity of group A, B, and D streptococci by human lysozyme acting on their cell walls. 308 32

The effects of different serum components alone and in conjunction with each other on Escherichia coli B were investigated. In general, the viability, turbidity, and electron microscope results were compatible with the following conclusions. The most efficient killing and destruction of E. coli B occurred when beta-lysin, lysozyme, and the antibody-complement system functioned in cooperation with each other at the serum concentration in isotonic solutions. The addition of sucrose protected the bacteria from the lethal and lytic action of these agents. Elimination of lysozyme from serum had the least effect on bactericidal activity, even though lysozyme treatment caused the cell wall to separate from the cytoplasmic membrane and caused clear areas to appear in the inner granular layer of the cell wall. Beta-lysin removal had an intermediate effect on the serum bactericidal activity. Beta-lysin treatment caused cell walls to collapse, allowed cytoplasmic contents to leak out of the cells, and stopped the separation of cell wall and cytoplasmic membrane, which normally takes place in 0.5 M sucrose solution. Inactivation of the complement eliminated the serum bactericidal activity against E. coli B. After treatment with antibody and complement, the cell walls became thick and indistinct, a portion of the cytoplasmic contents escaped, and patches of the middle layer of the cell wall appeared in freeze-etch preparations. Beta-lysin damaged the cytoplasmic membrane, lysozyme damaged the inner peptidoglycan layer of the cell wall, and the antibody-complement system damaged both the middle lipopolysaccharide layer of the cell wall and the cytoplasmic membrane.
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PMID:Interrelationship between serum beta-lysin, lysozyme, and the antibody-complement system in killing Escherichia coli. 460 6

A cationic protein of rabbit serum bactericidal for Staphylococcus aureus was purified. The specific activity per unit of protein of the purified staphylocidal preparation was approximately 37,000 times greater than that of the serum from which it was isolated. Similar techniques were used to purify serum beta-lysin active against Bacillus subtilis approximately 24,000 times. The staphylocidal activity cannot be attributed to the same beta-lysin active against B. subtilis, lysozyme, or antibody-complement systems. The concentrations of staphylocidal beta-lysin in the sera of the five mammalian species studied did not correlate with their beta-lysin activities against B. subtilis. The two beta-lysins are similar in that both were heat-stable, sensitive to trypsin digestion, had molecular weights near 6,000, and were found in higher concentrations in serum than in plasma. Furthermore, similar techniques can be used to absorb and elute both substances in highly purified forms using cellulose asbestos filter pads and ion exchange chromatography on carboxymethyl cellulose. In contrast to the beta-lysin against B. subtilis, the staphylocidal beta-lysin was not released from blood platelets, and it was inactive in the presence of heparin, sodium citrate, sodium oxalate, ethylenediaminetetraacetic acid, acidic phospholipids, and acid pH values. A variety of proteins, including those of normal serum, preferentially inhibited the bactericidal activity of staphylocidal beta-lysin but not the beta-lysin against B. subtilis.
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PMID:Purification of staphylocidal beta-lysin from rabbit serum. 497 97

A lytic enzyme induced in Micrococcus lysodeikticus strain 1 by infection with N1 bacteriophage was purified 45- to 50-fold by ammonium sulfate precipitation, acid precipitation, and selective adsorption of contaminating proteins with calcium phosphate gel. The optimal pH for activity of the enzyme was 6.5 to 7.0. Maximal activity occurred at 45 to 50 C and at an ionic strength of 0.06. The enzyme had a limited specificity and lysed cell walls of M. lysodeikticus with the release of dinitrofluorobenzene reactive groups. Living cells were lysed in the absence of phage; however, the rate of lysis increased when phage was present in excess of 10 particles per bacterial cell. Young cells were most sensitive, and the sensitivity decreased to a minimum with stationary-phase cells. Acting synergistically, lysozyme and the N1-induced lysin caused lysis of cells which were resistant to either enzyme acting independently. The N1 lysin did not exhibit proteolytic activity.
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PMID:Characteristics of a lytic enzyme induced by bacteriophage infection of Micrococcus lysodeikticus. 562 71


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