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  • 1
    Online Resource
    Online Resource
    Novel Genes of the dsr Gene Cluster and Evidence for Close Interaction of Dsr Proteins during Sulfur Oxidation in the Phototrophic Sulfur Bacterium Allochromatium vinosum
    American Society for Microbiology ; 2005
    In:  Journal of Bacteriology Vol. 187, No. 4 ( 2005-02-15), p. 1392-1404
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 187, No. 4 ( 2005-02-15), p. 1392-1404
    Abstract: Seven new genes designated dsrLJOPNSR were identified immediately downstream of dsrABEFHCMK , completing the dsr gene cluster of the phototrophic sulfur bacterium Allochromatium vinosum D (DSM 180 T ). Interposon mutagenesis proved an essential role of the encoded proteins for the oxidation of intracellular sulfur, an obligate intermediate during the oxidation of sulfide and thiosulfate. While dsrR and dsrS encode cytoplasmic proteins of unknown function, the other genes encode a predicted NADPH:acceptor oxidoreductase (DsrL), a triheme c -type cytochrome (DsrJ), a periplasmic iron-sulfur protein (DsrO), and an integral membrane protein (DsrP). DsrN resembles cobyrinic acid a,c -diamide synthases and is probably involved in the biosynthesis of siro(heme)amide, the prosthetic group of the dsrAB -encoded sulfite reductase. The presence of most predicted Dsr proteins in A. vinosum was verified by Western blot analysis. With the exception of the constitutively present DsrC, the formation of Dsr gene products was greatly enhanced by sulfide. DsrEFH were purified from the soluble fraction and constitute a soluble α 2 β 2 γ 2 -structured 75-kDa holoprotein. DsrKJO were purified from membranes pointing at the presence of a transmembrane electron-transporting complex consisting of DsrKMJOP. In accordance with the suggestion that related complexes from dissimilatory sulfate reducers transfer electrons to sulfite reductase, the A. vinosum Dsr complex is copurified with sulfite reductase, DsrEFH, and DsrC. We therefore now have an ideal and unique possibility to study the interaction of sulfite reductase with other proteins and to clarify the long-standing problem of electron transport from and to sulfite reductase, not only in phototrophic bacteria but also in sulfate-reducing prokaryotes.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/JB.187.4.1392-1404.2005
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2005
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Severity of Nonbullous Staphylococcus aureus Impetigo in Children Is Associated with Strains Harboring Genetic Markers for Exfoliative Toxin B, Panton-Valentine Leukocidin, and the Multidrug Resistance Plasmid pSK41
    American Society for Microbiology ; 2003
    In:  Journal of Clinical Microbiology Vol. 41, No. 7 ( 2003-07), p. 3017-3021
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 41, No. 7 ( 2003-07), p. 3017-3021
    Abstract: Nonbullous impetigo is a common skin infection in children and is frequently caused by Staphylococcus aureus . Staphylococcal toxins and especially exfoliative toxin A are known mediators of bullous impetigo in children. It is not known whether this is also true for nonbullous impetigo. We set out to analyze clonality among clinical isolates of S. aureus from children with nonbullous impetigo living in a restricted geographical area in The Netherlands. We investigated whether staphylococcal nasal carriage and the nature of the staphylococcal strains were associated with the severity and course of impetigo. Bacterial isolates were obtained from the noses and wounds of children suffering from impetigo. Strains were genetically characterized by pulsed-field gel electrophoresis-mediated typing and binary typing, which was also used to assess toxin gene content. In addition, a detailed clinical questionnaire was filled in by each of the participating patients. Staphylococcal nasal carriage seems to predispose the patients to the development of impetigo, and 34% of infections diagnosed in the Rotterdam area are caused by one clonal type of S. aureus . The S. aureus strains harbor the exfoliative toxin B (ETB) gene as a specific virulence factor. In particular, the numbers ( P = 0.002) and sizes ( P 〈 0.001) of the lesions were increased in patients infected with an ETB-positive strain. Additional predictors of disease severity and development could be identified. The presence of a staphylococcal plasmid encoding multiple antibiotic resistance traits, as detected by binary typing, was associated with a reduction in the cure rate. Our results recognize that a combination of staphylococcal virulence and resistance genes rather than a single gene determines the development and course of nonbullous impetigo. The identification of these microbial genetic markers, which are predictive of the severity and the course of the disease, will facilitate guided individualized antimicrobial therapy in the future.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/JCM.41.7.3017-3021.2003
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Distribution and Kinetics of Lipoprotein-Bound Lipoteichoic Acid
    American Society for Microbiology ; 2003
    In:  Infection and Immunity Vol. 71, No. 6 ( 2003-06), p. 3280-3284
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 71, No. 6 ( 2003-06), p. 3280-3284
    Abstract: Lipoteichoic acid (LTA), a major cell wall component of gram-positive bacteria, is an amphipathic anionic glycolipid with structural similarities to lipopolysaccharide (LPS) from gram-negative bacteria. LTA has been implicated as one of the primary immunostimulatory components that may trigger the systemic inflammatory response syndrome. Plasma lipoproteins have been shown to sequester LPS, which results in attenuation of the host response to infection, but little is known about the LTA binding characteristics of plasma lipid particles. In this study, we have examined the LTA binding capacities and association kinetics of the major lipoprotein classes under simulated physiological conditions in human whole blood (ex vivo) by using biologically active, fluorescently labeled LTA and high-performance gel permeation chromatography. The average distribution of an LTA preparation from Staphylococcus aureus in whole blood from 10 human volunteers revealed that 〉 95% of the LTA was associated with total plasma lipoproteins in the following proportions: high-density lipoprotein (HDL), 68% ± 10%; low-density lipoprotein (LDL), 28% ± 8%; and very low density lipoprotein (VLDL), 4% ± 5%. The saturation capacity of lipoproteins for LTA was in excess of 150 μg/ml. The LTA distribution was temperature dependent, with an optimal binding between 22 and 37°C. The binding of LTA by lipoproteins was essentially complete within 10 min and was followed by a subsequent redistribution from HDL and VLDL to LDL. We conclude that HDL has the highest binding capacity for LTA and propose that the loading and redistribution of LTA among plasma lipoproteins is a specific process that closely resembles that previously described for LPS (J. H. M. Levels, P. R. Abraham, A. van den Ende, and S. J. H. van Deventer, Infect. Immun. 68: 2821-2828, 2001).
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.71.6.3280-3284.2003
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
    detail.hit.zdb_id: 1483247-1
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  • 4
    Online Resource
    Online Resource
    Galactosyl-Lactose Sialylation Using Trypanosoma cruzi trans-Sialidase as the Biocatalyst and Bovine κ-Casein-Derived Glycomacropeptide as the Donor Substrate
    American Society for Microbiology ; 2014
    In:  Applied and Environmental Microbiology Vol. 80, No. 19 ( 2014-10), p. 5984-5991
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 80, No. 19 ( 2014-10), p. 5984-5991
    Abstract: trans -Sialidase (TS) enzymes catalyze the transfer of sialyl (Sia) residues from Sia(α2-3)Gal(β1- x )-glycans (sialo-glycans) to Gal(β1- x )-glycans (asialo-glycans). Aiming to apply this concept for the sialylation of linear and branched (Gal) n Glc oligosaccharide mixtures (GOS) using bovine κ-casein-derived glycomacropeptide (GMP) as the sialic acid donor, a kinetic study has been carried out with three components of GOS, i.e., 3′-galactosyl-lactose (β3′-GL), 4′-galactosyl-lactose (β4′-GL), and 6′-galactosyl-lactose (β6′-GL). This prebiotic GOS is prepared from lactose by incubation with suitable β-galactosidases, whereas GMP is a side-stream product of the dairy industry. The trans -sialidase from Trypanosoma cruzi (TcTS) was expressed in Escherichia coli and purified. Its temperature and pH optima were determined to be 25°C and pH 5.0, respectively. GMP [sialic acid content, 3.6% (wt/wt); N -acetylneuraminic acid (Neu5Ac), 〉 99%; (α2-3)-linked Neu5Ac, 59%] was found to be an efficient sialyl donor, and up to 95% of the (α2-3)-linked Neu5Ac could be transferred to lactose when a 10-fold excess of this acceptor substrate was used. The products of the TcTS-catalyzed sialylation of β3′-GL, β4′-GL, and β6′-GL, using GMP as the sialic acid donor, were purified, and their structures were elucidated by nuclear magnetic resonance spectroscopy. Monosialylated β3′-GL and β4′-GL contained Neu5Ac connected to the terminal Gal residue; however, in the case of β6′-GL, TcTS was shown to sialylate the 3 position of both the internal and terminal Gal moieties, yielding two different monosialylated products and a disialylated structure. Kinetic analyses showed that TcTS had higher affinity for the GL substrates than lactose, while the V max and k cat values were higher in the case of lactose.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.01465-14
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2014
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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