Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An inhibition factor from Streptococcus mutans strain C3603 (serotype c) was purified and isolated, and its properties indicated that it was a bacteriocin. Bacteriocin C3603 is a basic protein with a pI value of 10 and a molecular weight of 4,800. The activity of this bacteriocin was not affected by pH over a range of 1.0 to 12.0 or by storage at 100 degrees C for 10 min at pH 2.0 to 7.0 or storage at 121 degrees C for 15 min at pH 4.0. Pronase; papain, phospholipase C, trypsin, and alpha-amylase had no effect on the activity of the bacteriocin, whereas alpha-chymotrypsin and pancreatin were partially active against it. Bacteriocin activity was greater against certain S. mutans strains of serotypes b, c, e, and f than against certain S. mutans strains of serotypes a, d, and g. Bacteriocin C3603 was also effective against selected strains of S. sanguis, S. salivarius, S. bovis, S. faecium, S. lactis, Lactobacillus casei, L. plantarum, L. fermentum, Bifidobacterium bifidum, Bifidobacterium longum, Propionibacterium acnes, and Bacteroides melaninogenicus, but it was not effective against certain strains of Escherichia coli, Klebsiella pneumoniae, Corynebacterium parvum, and Candida albicans. The inhibition of S. mutans strains BHT and PS-14 by bacteriocin C3603 was found to be due to the bacteriocidal activity of the bacteriocin. When water or a diet containing bacteriocin C3603 was consumed by gnotobiotic and specific pathogen-free rats infected with S. mutans PS-14, the caries score was found to be significantly reduced.
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PMID:Purification and certain properties of a bacteriocin from Streptococcus mutans. 706 19

The effects of brodimoprim, a new trimethoprim analogue, on several virulence traits of respiratory and urinary tract pathogens exposed to sub-lethal levels of the drug was studied. Adherence to tracheal epithelial cells was inhibited by brodimoprim in Klebsiella pneumoniae (41-67% reduction), Moraxella catarrhalis (87-90%) and Haemophilus influenzae (0-53%), while in Streptococcus pneumoniae binding was unaffected. With buccal epithelial cells the comparison between treated and control bacteria indicated statistically significant reduction in adherence with both S.pneumoniae and H.influenzae, (P < 0.015). With M.catarrhalis and Streptococcus pyogenes only marginal changes were detected (P > 0.05). Exoenzyme and capsule production were assessed in at least three isolates of diverse respiratory pathogens grown in the presence of sub-lethal levels of the new agent. The drug affected protease and beta-hemolysin (alpha-toxin) production in both oxacillin-susceptible and -resistant S.aureus. On the contrary, synthesis of lipase, DNase, coagulase, and beta-lactamase (S.aureus), pneumolysin (S.pneumoniae), streptolysin S, DNase, and protease (S.pyogenes), capsule (K.pneumoniae, H.influenzae and S.pneumoniae), and beta-lactamase (K.pneumoniae, H.influenzae and M.catarrhalis) were not inhibited by subminimal inhibitory concentrations (sub-MICs) of the drug. Finally, motility was blocked in urinary pathogens E.coli, P.mirabilis and P.aeruginosa, while in this latter microorganism pigment production was also affected. High molecular weight low-copy F'lac, and low molecular weight high-copy pHSG298 plasmids were eliminated from E.coli treated with sub-MIC concentrations of brodimoprim. The incidence and cured cells ranged from 9% for F'lac to 23% for pHSG298. F'lac transfer was also inhibited by the drug. When conjugation was carried out with bacteria exposed to brodimoprim (5XMIC), a reduction (50%) in the number of recombinants was noted in comparison to the control. The fact that brodimoprim interferes with the expression of some virulence traits, in particular with adherence, at sub-MIC levels may assist the drug in eradicating respiratory pathogens from the epithelial lining, thus diminishing the probability of reinfection.
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PMID:Brodimoprim: effects of subminimal inhibitory concentrations on virulence traits of respiratory and urinary tract pathogens, and on plasmid transfer and stability. 880 12

Phospholipase C was isolated from an outbreak strain of Salmonella gallinarum with ciprofloxacin extraction, dialysis, gel filtration, ion exchange chromatography and chromatofocussing. Purified phospholipase C (mol wt. 65 KDa; isoelectric point, pI 3.5) was resistant to pasteurization, stomach enzyme (pepsin), bacterial protease and lipase but lost its activity on trypsin and chymotrypsin treatment. It was sensitive to pH > or = 8.0. It was haemolytic, embryotoxic, enterohaemorrhagic, lethal to birds, cytotoxic to Vero and MDBK cells, dermonecrotoxic in rabbit and antigenically active protein. Antisera raised against purified phospholipase C neutralized its all biological activities and agglutinated the producer Salmonella strains. Serologically it was proved similar to phospholipase C of Klebsiella pneumoniae and S. weltevreden. Fluorescent antibody technique (FAT) was standardized to detect phospholipase producer strains.
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PMID:Purification and characterization of phospholipase C of Salmonella gallinarum. 1009 8