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        Cationic hydrous thorium dioxide colloids – a useful tool for staining negatively charged surface matrices of bacteria for use in energy-filtered transmission electron microscopy

        Lünsdorf, Heinrich; Kristen, Ingeborg; Barth, Elke (BioMed Central, 2006-06-27)
        Background Synthesis of cationic hydrous thorium dioxide colloids (ca. 1.0 to 1.7 nm) has been originally described by Müller [22] and Groot [11] and these have been used by Groot to stain acidic glucosaminoglycans for ultrastructure research of different tissues by conventional transmission electron microscopy. Results Synthesis of colloidal thorium dioxide has been modified and its use as a suitable stain of acidic mucopolysaccharides and other anionic biopolymers from bacteria, either as whole mount preparations or as preembedment labels, is described. The differences in stain behavior relative to commonly used rutheniumred-lysine and Alcian Blue™ electron dense acidic stains has been investigated and its use is exemplified for Pseudomonas aeruginosa adjacent cell wall biopolymers. For the first time thorificated biopolymers, i.e. bacterial outer cell wall layers, have been analysed at the ultrastructural level with electron energy loss spectroscopy (EELS) and electron spectroscopic imaging (ESI), leading to excellent contrast and signal strength for these extracellular biopolymers. Conclusion Application of cationic hydrous ThO2 colloids for tracing acidic groups of the bacterial surface and/or EPS has been shown to be rather effective by transmission electron microscopy. Because of its high electron density and its good diffusibility it stains and outlines electro-negative charges within these biopolymers. In combination with ESI, based on integrated energy-filtered electron microscopy (EFTEM) Th-densities and thus negative charge densities can be discriminated from other elemental densities, especially in environmental samples, such as biofilms.
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        7-O-malonyl macrolactin A, a new macrolactin antibiotic from Bacillus subtilis active against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and a small-colony variant of Burkholderia cepacia.

        Romero-Tabarez, Magally; Jansen, Rolf; Sylla, Marita; Lünsdorf, Heinrich; Häussler, Susanne; Santosa, Dwi A; Timmis, Kenneth N; Molinari, Gabriella (2006-05-01)
        We report here the discovery, isolation, and chemical and preliminary biological characterization of a new antibiotic compound, 7-O-malonyl macrolactin A (MMA), produced by a Bacillus subtilis soil isolate. MMA is a bacteriostatic antibiotic that inhibits a number of multidrug-resistant gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and a small-colony variant of Burkholderia cepacia. MMA-treated staphylococci and enterococci were pseudomulticellular and exhibited multiple asymmetric initiation points of septum formation, indicating that MMA may inhibit a cell division function.
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        Identification of new acceptor specificities of glycosyltransferase R with the aid of substrate microarrays.

        Seibel, Jürgen; Hellmuth, Hendrik; Hofer, Bernd; Kicinska, Anna-Maria; Schmalbruch, Bodo (2006-02-01)
        Finding opportunities to construct sugar motifs and to transfer them to targets of biological relevance and rapid identification of glycosylation events are important goals for glycobiology and a field of increasing interest. Here we have applied an enzyme microarray screening system for the identification of new acceptor specificities of the glycosyltransferase R (GTFR) from Streptococcus oralis (E.C. 2.4.1.5), which was able to effect the synthesis of sugar motifs in short times and with low amounts of substrate. These observations resulted in the development of a convenient alpha-glycosylation by the non-Leloir glycosyltransferase GTFR, with sucrose as substrate and with different alcohols and amino acid derivatives as acceptors, for the synthesis of glycoethers and glycosylated amino acids not observed with the use of familiar GTFs with high sequence homology.
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        Growth of Polychlorinated-Biphenyl-Degrading Bacteria in the Presence of Biphenyl and Chlorobiphenyls Generates Oxidative Stress and Massive Accumulation of Inorganic Polyphosphate

        Chávez, Francisco P.; Lünsdorf, Heinrich; Jerez, Carlos A. (American Society for Microbiology, 2004-05)
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        Identification of B- and T-Cell Epitopes within the Fibronectin-Binding Domain of the SfbI Protein of Streptococcus pyogenes

        Schulze, Kai; Medina, Eva; Chhatwal, Gursharan S.; Guzmán, Carlos A. (American Society for Microbiology, 2003-12)
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        Intracellular Survival of Streptococcus pyogenes in Polymorphonuclear Cells Results in Increased Bacterial Virulence

        Medina, Eva; Rohde, Manfred; Chhatwal, Gursharan S. (American Society for Microbiology, 2003-09)
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        Influence of different rol gene products on the chain length of Shigella dysenteriae type 1 lipopolysaccharide O antigen expressed by Shigella flexneri carrier strains.

        Klee, S R; Tzschaschel, B D; Timmis, K N; Guzman, C A (1997-04)
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        Localization of the stress protein SP21 in indole-induced spores, fruiting bodies, and heat-shocked cells of Stigmatella aurantiaca.

        Lünsdorf, H; Schairer, H U; Heidelbach, M (1995-12)
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        Interaction of Listeria monocytogenes with mouse dendritic cells.

        Guzman, C A; Rohde, M; Chakraborty, T; Domann, E; Hudel, M; Wehland, J; Timmis, K N (1995-09)
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        Conversion of chlorobiphenyls into phenylhexadienoates and benzoates by the enzymes of the upper pathway for polychlorobiphenyl degradation encoded by the bph locus of Pseudomonas sp. strain LB400.

        Seeger, M; Timmis, K N; Hofer, B; Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany. (1995-07)
        Metabolism of 21 chlorobiphenyls by the enzymes of the upper biphenyl catabolic pathway encoded by the bph locus of Pseudomonas sp. strain LB400 was investigated by using recombinant strains harboring gene cassettes containing bphABC or bphABCD. The enzymes of the upper pathway were generally able to metabolize mono- and dichlorinated biphenyls but only partially transform most trichlorinated congeners investigated: 14 of 15 mono- and dichlorinated and 2 of 6 trichlorinated congeners were converted into benzoates. All mono- and at least 8 of 12 dichlorinated congeners were attacked by the bphA-encoded biphenyl dioxygenase virtually exclusively at ortho and meta carbons. This enzyme exhibited a high degree of selectivity for the aromatic ring to be attacked, with the order of ring preference being non- > ortho- > meta- > para-substituted for mono- and dichlorinated congeners. The influence of the chlorine substitution pattern of the metabolized ring on benzoate formation resembled its influence on the reactivity of initial dioxygenation, suggesting that the rate of benzoate formation may frequently be determined by the rate of initial attack. The absorption spectra of phenylhexadienoates formed correlated with the presence or absence of a chlorine substituent at an ortho position.
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        Inducible cell lysis system for the study of natural transformation and environmental fate of DNA released by cell death.

        Kloos, D U; Strätz, M; Güttler, A; Steffan, R J; Timmis, K N (1994-12)
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        Cross talk between catabolic pathways in Pseudomonas putida: XylS-dependent and -independent activation of the TOL meta operon requires the same cis-acting sequences within the Pm promoter.

        Kessler, B; Marqués, S; Köhler, T; Ramos, J L; Timmis, K N; de Lorenzo, V (1994-09)
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        Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets".

        Niebuhr, K; Chakraborty, T; Rohde, Manfred; Gazlig, T; Jansen, B; Köllner, P; Wehland, J (1993-07)
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        Construction of stable LamB-Shiga toxin B subunit hybrids: analysis of expression in Salmonella typhimurium aroA strains and stimulation of B subunit-specific mucosal and serum antibody responses.

        Su, G F; Brahmbhatt, H N; Wehland, J; Rohde, Manfred; Timmis, K N (1992-08)
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        Characterization of murine monoclonal antibodies that recognize defined epitopes of pertussis toxin and neutralize its toxic effect on Chinese hamster ovary cells.

        Walker, M J; Wehland, J; Timmis, K N; Raupach, B; Schmidt, M A (1991-11)
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        Construction of minitransposons for constitutive and inducible expression of pertussis toxin in bvg-negative Bordetella bronchiseptica.

        Walker, M J; Rohde, Manfred; Wehland, J; Timmis, K N (1991-11)
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        Direct expression of Bordetella pertussis filamentous hemagglutinin in Escherichia coli and Salmonella typhimurium aroA.

        Guzmán, C A; Walker, M J; Rohde, Manfred; Timmis, K N (1991-10)
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        Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin.

        Kadurugamuwa, J L; Rohde, Manfred; Wehland, J; Timmis, K N (1991-10)
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        Production of recombinant Bordetella pertussis serotype 2 fimbriae in Bordetella parapertussis and Bordetella bronchiseptica: utility of Escherichia coli gene expression signals.

        Walker, M J; Guzmán, C A; Rohde, Manfred; Timmis, K N (1991-05)
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        Immunocytochemical localization of the coenzyme F420-reducing hydrogenase in Methanosarcina barkeri Fusaro.

        Lünsdorf, H; Niedrig, M; Fiebig, K (1991-02)
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