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  • 1
    Electronic Resource
    Electronic Resource
    COMPARATIVE CHEMICAL ANALYSIS OF TWO VARIANTS OF THE ESCHERICHIA COLI K2 ANTIGEN (1980)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 7 (1980), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6941.1980.tb01580.x
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of monoclonal antibodies directed against domains of pertussis toxin involved in receptor recognition (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 76 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The exotoxin pertussis toxin (PT) produced by virulent Bordetella pertussis bacteria is regarded as the main virulence factor of the organism and held responsible for most of its pathological effects. Identification of functional sites on PT would greatly facilitate site-specific detoxification and thus also the development of a new vaccine. For the investigation of structure-function aspects of PT we have prepared and characterized eleven monoclonal antibodies (mAbs) (UB-A1, UB-A2, UB-A10, UB-B7, UB-B12, UB-D4, UB-D7, UB-D10, UB-F7, UB-G1, and UB-G12) directed at the native toxin. Only UB-B12 and UB-D10 recognized PT in Western blotting indicating that most of the mAbs were directed against conformational epitopes. The mAbs were assayed for their ability to interfere with the binding of PT in model receptor systems like a solid phase binding assay using fetuin as receptor moiety, hemagglutination of chymotrypsin-sensitized goose erythrocytes, and the PT-mediated induction of the clustered growth pattern (CGP) of Chinese hamster ovary (CHO) cells. Five of the eleven mAbs (UB-A1, UB-A2, UB-B7, UB-B12, and UB-D7) interfered with the binding of PT to fetuin on solid phase and with PT-mediated hemagglutination. UB-A2, UB-B7, and UB-B12 also inhibited the induction of the clustered growth pattern of CHO-cells. This indicates that the determinants recognized by these mAbs are associated with the formation of the carbohydrate recognition sites of PT. Thus, the monoclonal antibodies described in this study will be valuable tools in the further analysis of the structure-function relationship of pertussis toxin with respect to receptor recognition and binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04223.x
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  • 3
    Electronic Resource
    Electronic Resource
    Phospholipid substitution of capsular (K) polysaccharide antigens from Escherichia coli causing extraintestinal infections (1982)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 14 (1982), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1982.tb08637.x
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  • 4
    Electronic Resource
    Electronic Resource
    Electron density studies of KCl and LiF by γ-ray diffractometry (1985)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 41 (1985), S. 171-175 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Use of hard electromagnetic radiation (λ = 0.12 Å) in diffraction experiments, in conjunction with thin crystals in transmission geometry (Laue case), minimizes multiple scattering, often referred to as the 'extinction problem'. A large crystal slab, completely intercepting the incident beam, was used in this experiment. Several structure factors have been measured in LiF and KCl, with greater accuracy than ever before, using the γ-ray spectrometer of the University of Missouri at Columbia. In the case of LiF the results indicates some compression of the valence electron densities, similar to what has been found earlier for NaF. In the case of KCl all reflections agree well with the values calculated from free-atom Hartree-Fock wave functions except for the 004 and 006, which are appreciably weaker than corresponding reflections with similar or identical sin θ/λ values. This result indicates asphericity of the valence electron density. The 111 is also much weaker than the calculated value, indicating that the negative ions are slightly compressed and the positive ions slightly expanded with respect to the free-ion charge densities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108767385000344
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of Export Proteins from Mycobacterium tuberculosis That Interact with SecA (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 797 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb52964.x
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  • 6
    Electronic Resource
    Electronic Resource
    RecA-dependent viral burst in bacterial colonies during the entry into stationary phase (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 170 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We have explored the nature of the sudden viral amplification observed during the ageing of P22-infected lysogenic colonies of Salmonella typhimurium [Ramı́rez, E, and Villaverde, A. (1997) Gene 202, 147–149]. By a comparative analysis of the wild-type P22 and a P22 integration mutant, it has been shown that the conditions promoting prophage induction occur in only a small portion of the bacterial population and briefly during the transition between the exponential growth and the stationary phase. The viral burst is RecA-dependent and cannot be reproduced in continuous culture by a mere decrease of the growth rate. This suggests that the limited viral propagation in colonies is probably linked to heterogeneous physiological conditions within colonial populations, distinct from those of the homogeneous liquid cultures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13389.x
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  • 7
    Electronic Resource
    Electronic Resource
    Proposed Experimental Investigation of Uncertainty Relations by Measuring the Velocity Dispersion of Localized Neutrons (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 480 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb12476.x
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  • 8
    Electronic Resource
    Electronic Resource
    Intestinal immunity of Escherichia coli NISSLE 1917: a safe carrier for therapeutic molecules (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 43 (2005), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The development of novel approaches that allow accurate targeting of therapeutics to the intestinal mucosa is a major task in the research on intestinal inflammation. For the first time, a live genetically modified bacterial strain has been approved by Dutch authorities as a therapeutic agent for experimental therapy of intestinal bowel disease (IBD) in humans. Genetically modified probiotics can very well be used as carriers for localized antigen delivery into the intestine. Therapeutic safety, however, of such a carrier organism, is crucial, especially when a specific probiotic strain has to be used under diseased conditions. In this study, we tested the potential of Escherichia coli NISSLE 1917 to serve as a safe carrier for targeted delivery of recombinant proteins to the intestinal mucosa. In a well-defined and very sensitive immunological system, we demonstrate that intestinal recombinant E. coli NISSLE 1917 has no effect on migration, clonal expansion and activation status of specific CD4+ T cells, neither in healthy mice nor in animals with acute colitis. Furthermore, recombinant E. coli NISSLE 1917 has no effect on the induction or breakdown of peripheral T-cell tolerance in an autoimmune environment. The excellent colonization properties of E. coli NISSLE 1917 render this strain an ideal candidate as carrier organism for gut-focused in situ synthesis of therapeutic molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsim.2004.10.023
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  • 9
    Electronic Resource
    Electronic Resource
    Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 27 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: For the efficient surface presentation and release of virulence factors especially pathogenic Gram-negative bacteria have developed several distinct secretion mechanisms. An increasing number of pathogens in various species employs a mechanism denoted the ‘autotransporter’ pathway. This pathway is characterised by an outer membrane translocator module representing the C-terminal domain of the transported protein itself. An intriguing potential application of such systems involves the transport and surface expression of recombinant proteins or peptides, like e.g. the presentation of antigens for the generation of live oral vectors as vaccine carriers. Here we report on the incorporation of heterologous (poly-) peptides in permissive sites of the translocator module of the adhesin-involved-in-diffuse-adherence (AIDA) autotransporter system. We demonstrate the presentation of the B subunit of the heat labile enterotoxin of Escherichia coli (LTB) as well as of functional T-cell epitopes of Yersinia enterocolitica heat-shock protein 60 (Y-hsp60) on the surface of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01446.x
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  • 10
    Electronic Resource
    Electronic Resource
    Processing of the AIDA-I precursor: removal of AIDAC and evidence for the outer membrane anchoring as a β-barrel structure (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 22 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The AIDA-I adhesin known to be responsible for the diffuse adherence (DA) phenotype of the diarrhoea-genie Escherichia coli (DAEC) strain 2787 has been shown previously to be synthesized as a precursor protein and to undergo additional C-terminal processing. Here, the C-terminal processing of the AIDA-I precursor and the outer membrane topology of the cleaved C-terminal fragment, AIDAC, were investigated. By isolation of the cleaved AIDAC fragment and N-terminal sequencing, the C-terminal cleavage site was identified between Ser-846 and Ala-847 thereby indicating a molecular mass of 47.5 kDa for AIDAC. The correct processing to AIDA-I and AIDAC in OmpT, OmpP and DegP protease-deficient E. coli strains as well as in avirulent salmonellae and shigellae points to an autocatalytic cleavage mechanism. The cleaved AIDAC was localized in the outer membrane. A leader sequence-AIDAC fusion was efficiently routed to the outer membrane. Analysis by protease digestion, secondary-structure prediction and modelling, by comparison with structurally related bacterial proteins like the lgA1 protease from neisseria, the vacuolating toxin from Helicobacter pylori, and the VirG protein of Shigella flexneri, strongly indicates that AIDAC is present in the outer membrane as a β-barrel structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1996.tb02653.x
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