Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0519030 (Klebsiella)
21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Genetic and reversion analyses of a thermosensitive pleiotropic mutant strain of Klebsiella pneumoniae with defects in nitrogen fixation and nitrogen metabolism have shown that the pleiotropie behaviour of mutant is due to a single mutation in a gene designated nim. This gene is contransducible with trp at a frequency of about 30% (using bacteriophage P1) and with cys at a frequency of about 14%. The gene order is cys, trp, nim. The defect in the nim mutant is complemented by the E. coli F' element, F'148.
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PMID:Genetic analysis of a pleiotropic mutant of Klebsiella pneumoniae affected in nitrogen metabolism. 698 57

Cysteine-dependent (cys-) Escherichia coli and Klebsiella spp., defective in sulphate assimilation, were isolated from urine and stool samples of infected patients. These isolates reverted to prototrophy under conditions of cysteine deprivation but the revertant strains and a prototrophic wild-type E. coli strain became auxotrophic for cysteine in a cysteine-enriched medium. This suggested that excess cysteine acts as a repressor of the cys HIJ operon known to control aspects of cysteine biosynthesis. A group of mostly elderly patients infected with cys- strains suffered a disproportionate amount of renal impairment as compared with a control group. In renal impairment, sulphur compounds, including cysteine, are retained. This raises the possibility that these raised levels of cysteine and related compounds may enhance the selection of cys- strains in vivo.
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PMID:Further studies of clinical isolates of cysteine-requiring Escherichia coli and Klebsiella and possible mechanisms for their selection in vivo. 824 54

The cbl (cysB-like) gene has been identified in Escherichia coli. The analysis of the cloned cbl sequence revealed strict homology to an ORF of unknown function found initially in Klebsiella aerogenes [Schwacha and Bender, J. Bacteriol. 175 (1993) 2107-2115]. The predicted Cbl protein has structural features of the LysR family of transcriptional activators. It is also strongly similar to the CysB protein, the activator of the cys regulon. The position of cbl on the Ec physical map has been established at a 2070-kb (43.5 min) region between asnU and asnV. The gene is expressed in vivo as a 1-kb monocistronic transcript starting from one major transcription start point. Unexpectedly, the in vivo expression of cbl has shown dependence on CysB, belonging to the same family of proteins. The promoter region of cbl binds purified CysB protein in a manner similar to other CysB-responsive promoters. A cbl disruption mutant was constructed by insertion of a KmR gene cartridge into the ORF on the chromosome. Phenotypes related to cbl expression suggest the involvement of the gene in an accessory regulatory circuit within the cys regulon engaging, in the last step, the function of the cysM gene encoding O-acetylserine (thiol)-lyase B.
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PMID:A new gene, cbl, encoding a member of the LysR family of transcriptional regulators belongs to Escherichia coli cys regulon. 852 72

In the enteric bacteria Escherichia coli and Salmonella enterica, sulfate is reduced to sulfide and assimilated into the amino acid cysteine; in turn, cysteine provides the sulfur atom for other sulfur-bearing molecules in the cell, including methionine. These organisms cannot use methionine as a sole source of sulfur. Here we report that this constraint is not shared by many other enteric bacteria, which can use either cysteine or methionine as the sole source of sulfur. The enteric bacterium Klebsiella aerogenes appears to use at least two pathways to allow the reduced sulfur of methionine to be recycled into cysteine. In addition, the ability to recycle methionine on solid media, where cys mutants cannot use methionine as a sulfur source, appears to be different from that in liquid media, where they can. One pathway likely uses a cystathionine intermediate to convert homocysteine to cysteine and is induced under conditions of sulfur starvation, which is likely sensed by low levels of the sulfate reduction intermediate adenosine-5'-phosphosulfate. The CysB regulatory proteins appear to control activation of this pathway. A second pathway may use a methanesulfonate intermediate to convert methionine-derived methanethiol to sulfite. While the transsulfurylation pathway may be directed to recovery of methionine, the methanethiol pathway likely represents a general salvage mechanism for recovery of alkane sulfide and alkane sulfonates. Therefore, the relatively distinct biosyntheses of cysteine and methionine in E. coli and Salmonella appear to be more intertwined in Klebsiella.
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PMID:Methionine-to-cysteine recycling in Klebsiella aerogenes. 1111 34

It has been well-documented that leukotrienes (LTs) are released in allergic lung inflammation and that they participate in the physiopathology of asthma. A role for LTs in innate immunity has recently emerged: Cys-LTs were shown to enhance FcgammaR-mediated phagocytosis by alveolar macrophages (AMs). Thus, using a rat model of asthma, we evaluated FcgammaR-mediated phagocytosis and killing of Klebsiella pneumoniae by AMs. The effect of treatment with a cys-LT antagonist (montelukast) on macrophage function was also investigated. Male Wistar rats were immunized twice with OVA/alumen intraperitoneally and challenged with OVA aerosol. After 24 h, the animals were killed, and the AMs were obtained by bronchoalveolar lavage. Macrophages were cultured with IgG-opsonized red blood cells (50:1) or IgG-opsonized K. pneumoniae (30:1), and phagocytosis or killing was evaluated. Leukotriene C(4) and nitric oxide were quantified by the EIA and Griess methods, respectively. The results showed that AMs from sensitized and challenged rats presented a markedly increased phagocytic capacity via FcgammaR (10X compared to controls) and enhanced killing of K. pneumoniae (4X higher than controls). The increased phagocytosis was inhibited 15X and killing 3X by treatment of the rats with montelukast, as compared to the non-treated group. cys-LT addition increased phagocytosis in control AMs but had no effect on macrophages from allergic lungs. Montelukast reduced nitric oxide (39%) and LTC(4) (73%). These results suggest that LTs produced during allergic lung inflammation potentiate the capacity of AMs to phagocytose and kill K. pneumonia via FcgammaR.
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PMID:Leukotrienes produced in allergic lung inflammation activate alveolar macrophages. 2079 16

The main purpose of this work is to obtain a cotton-based textile material functionalized with L-cysteine (L-cys) to achieve an antimicrobial effect with potential application in biomedical, geriatric or pediatric textiles. The binding capacity of L-cys to cotton fibres was assessed through different functionalization strategies--surface activation and exhaustion processes. A subsequent analysis of the possible antibacterial action against Staphylococcus aureus and Klebsiella pneumoniae was performed according with the Japanese International standard (JISL, 2008). To determine the mechanism of action of L-cys on the selected strains, flow cytometry was used. The results revealed that the exhaustion process was performed with success to confer bioactivity to the treated fabric, as assessed by an effective antibacterial effect against both Gram-positive and Gram-negative bacteria, and successfully linkage of L-cys was observed via FTIR with a durable effect demonstrated after the washing tests (fastness to washing). It was also observed that L-cys exerts a bacteriostatic effect against both bacterial strains, since there were alterations in the metabolic activity of the microorganisms after the application of the bioactive textile which was shown by the CTC (cyanoditolyl tetrazolium chloride) staining used in flow cytometry. This study shows a new and successful biotechnological process to develop antibacterial textiles through the functionalization of cotton fibres with L-cys which presents a broad range of applications in healthcare, since L-cys is a natural antibacterial compound, non-toxic and affects pathogenic bacteria related to hospital infections.
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PMID:Biofunctionalization of cellulosic fibres with L-cysteine: assessment of antibacterial properties and mechanism of action against Staphylococcus aureus and Klebsiella pneumoniae. 2443 76