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Other Bacterial (other + bacterial)

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Life Sciences50%

Terms modified by Other Bacterial

  • other bacterial species
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    Selected Abstracts

    Ceramide in Pseudomonas aeruginosa infections

    EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, Issue 10 2007
    Joachim Riethmüller
    Abstract Cystic fibrosis (CF), the most common autosomal recessive disorder, at least in western countries, is caused by mutations of the cystic fibrosis transmembranous conductance regulator (CFTR) molecule and affects approximately 80,000 patients in Europe and the USA. Most, if not all, CF patients develop a chronic pulmonary infection with Pseudomonas aeruginosa. At present it is unknown why CF patients are highly sensitive to P.,aeruginosa infections, and most importantly, no curative treatment for CF is available. P.,aeruginosa infection results in an activation of the enzyme acid sphingomyelinase which catalyzes the release of ceramide from sphingomyelin in the cell membrane. Ceramide forms large ceramide-enriched membrane domains that are required for internalization of bacteria, induction of cell death in infected cells and a controlled release of cytokines from infected cells. Ceramide-enriched membrane platforms seem to serve the reorganization of receptors and intracellular signaling molecules involved in the infection of mammalian cells with P.,aeruginosa. The significance of the acid sphingomyelinase and ceramide for the infection of mammalian cells with P.,aeruginosa was demonstrated on mice genetically deficient for the acid sphingomyelinase. Further studies with N.,gonorrhoeae, S.,aureus and rhinoviruses indicate that ceramide-enriched membrane domains are also important for the infection of mammalian cells with other bacterial and viral pathogens, suggesting a general role of these membrane domains in infectious biology. [source]

    Bacillus cereus is common in the environment but emetic toxin producing isolates are rare

    JOURNAL OF APPLIED MICROBIOLOGY, Issue 1 2006
    M. Altayar
    Abstract Aims:, To determine the incidence of emetic toxin producing Bacillus cereus in soil, animal faeces and selected vegetable produce to compare the results with the previously reported high incidence in rice paddy fields. To examine whether the emetic toxin has antibiotic activity. Methods and Results:, The incidence of emetic toxin producing B. cereus was evaluated by plating on selective agar 271 samples of soils, animal faeces, raw and processed vegetables. Overall, 45·8% of samples were positive for B. cereus. One hundred and seventy-seven B. cereus isolates were recovered at 30°C with the grand mean spore count being 2·6 ± 1·7 log10 CFU g,1 and 148 B. cereus isolates were recovered at 7°C with the grand mean spore count being 2·2 ± 1·2 log10 CFU g,1 of the177 B. cereus isolated at 30°C, only 3 were positive for emetic toxin production at a titre of 1/64, 1/32, 1/16, respectively. Also, 1 of 148 B. cereus isolated at 7°C was positive for emetic toxin production to a titre of 1/128. All positive isolates came from washed or unwashed potato skins, one was psychrotrophic as determined by PCR and growth at 7°C on subculture. The emetic toxin was not shown to have any antibiotic effects in growth inhibition studies. Conclusions:, While B. cereus was a common isolate, the incidence of the emetic strain was rare. This is in contrast to previous findings of the high incidence in rice paddy fields and the processing environment, which may suggest rice is a selective area for growth of the emetic strain of B. cereus. Significance and Impact of Study:, The finding that a psychrotrophic isolate of B. cereus can produce emetic toxin is the first ever such observation and suggests the possibility that psychrotrophic isolates could grow in refrigerated fresh foods and cause emesis. The incidence of emetic B. cereus strains in rice paddy fields now requires further study for comparison with the low incidence found in other soils. The emetic toxin failed to inhibit the growth of other bacterial, fungal and yeast species. Whether the toxin (which is similar in structure to the antibiotic valinomycin) plays a competitive role in the environment therefore remains unclear. [source]

    Crystallization and preliminary structural analyses of glutamate dehydrogenase from Peptoniphilus asaccharolyticus

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2010
    Tania F. Oliveira
    Glutamate dehydrogenase (EC 1.4.1.2,4) from Peptoniphilus asaccharolyticus has been expressed as a selenomethionine-derivatized recombinant protein and diffraction-quality crystals have been grown that are suitable for structure determination. Preliminary structural analyses indicate that the protein assembles as a homohexameric enzyme complex in solution, similar to other bacterial and mammalian enzymes to which its sequence identity varies between 25 and 40%. The structure will provide insight into its preference for the cofactor NADH (over NADPH) by comparisons with the known structures of mammalian and bacterial enzymes. [source]

    Structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942 complexed with NADP

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2006
    Kei Wada
    The crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH) from Synechococcus PCC 7942 (S. 7942) in complex with NADP was solved by molecular replacement and refined to an R factor of 19.1% and a free R factor of 24.0% at 2.5,Å resolution. The overall structure of NADP-GAPDH from S. 7942 was quite similar to those of other bacterial and eukaryotic GAPDHs. The nicotinamide ring of NADP, which is involved in the redox reaction, was oriented toward the catalytic site. The 2,-­phosphate O atoms of NADP exhibited hydrogen bonds to the hydroxyl groups of Ser194 belonging to the S-loop and Thr37. These residues are therefore considered to be essential in the discrimination between NADP and NAD molecules. The C-terminal region was estimated to have an extremely flexible conformation and to play an important role in the formation of the supramolecular complex phosphoribulokinase (PRK),regulatory peptide (CP12),GAPDH, which regulates enzyme activities. [source]