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  • 1
    Electronic Resource
    Electronic Resource
    The Caulobacter crescentus outer membrane protein Omp58 (RsaF) is not required for paracrystalline S-layer secretion (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 201 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: To identify the outer membrane protein component of the Caulobacter crescentus CB2 surface-layer export machinery we used the Serratia marcescens LipD protein to find homologs in the CB2 genome. From two homologous sequences found, one encodes a putative OMP with a predicted molecular mass of 57.5 kDa, termed Omp58 (formerly RsaF). Comparison of membrane protein profiles revealed a protein with an appropriate molecular mass present in wild-type, but not CB2 omp58::kanamycin, a mutant strain with an inactivated omp58 gene. Disruption of omp58 did not affect surface-layer production, suggesting that Omp58 is not involved in surface-layer protein secretion and, thus, may not be the outer membrane protein component of the C. crescentus surface-layer export system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10769.x
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  • 2
    Electronic Resource
    Electronic Resource
    Cytokinins: A Rapid Extraction and Purification Method (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 34 (1975), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A method is described for the isolation, purification and quantitation of free cytokinin bases and ribosides using ethyl acetate at pH 7.7 for the extraction. The extraction is almost complete (97.7%) as determined by using N6-(Δ2-isopentenyl)adenine-8-14C. The subsequent fast purification by chromatography on a standardized silica gel column in chloroform-methanol (7:3 v/v) is followed by thin layer chromatography (silica gel 60 F254) in chloroform-acetic acid (8:2 v/v). The recovery of N6-(Δ2-isopentenyl)adenine-8-14C after this two step purification was 78–82%. The efficiency of the method was determined by applying this procedure to N6-(Δ2-isopentenyl)adenine and N6(Δ2-isopentenyl)adenosine. Using gas liquid chromatography the recovery for N6-(Δ2-isopentenyl)adenosine was determined to be 61% and compared to 43% for N6-(Δ2-isopentenyl)adenosine, showing the suitability of the described method for gas liquid chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1975.tb03822.x
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  • 3
    Electronic Resource
    Electronic Resource
    Mucosal vaccination with a recombinant OprF-I vaccine of Pseudomonas aeruginosa in healthy volunteers: comparison of a systemic vs. a mucosal booster schedule (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 37 (2003), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We compared the immunogenicity of two vaccination schedules with either a systemic or a mucosal booster, both following a mucosal primary vaccination with a recombinant outer membrane fusion protein of Pseudomonas aeruginosa (OprF-I) in 12 healthy volunteers. The systemic booster induced higher levels of OprF-I-specific serum antibodies of IgG isotype, with a mean±S.E.M. of 32.6±7.8×107 enzyme-linked immunosorbent assay (ELISA) units (EU) as compared to the nasal booster with 14.6±2.1×107 EU (P=0.05). Specific serum IgA antibodies and antibodies in saliva did not differ between the two vaccination groups. We conclude that a combined mucosal/systemic vaccination with the OprF-I vaccine may offer an enhanced systemic immunogenicity. Further studies on the long-term immunogenicity and induction of antibodies on the respiratory airway surface are warranted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0928-8244(03)00094-4
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  • 4
    Electronic Resource
    Electronic Resource
    Secretory delivery of recombinant proteins in attenuated Salmonella strains: potential and limitations of Type I protein transporters (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 37 (2003), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Live attenuated Salmonella strains have been extensively explored as oral delivery systems for recombinant vaccine antigens and effector proteins with immunoadjuvant and immunomodulatory potential. The feasibility of this approach was demonstrated in human vaccination trials for various antigens. However, immunization efficiencies with live vaccines are generally significantly lower compared to those monitored in parenteral immunizations with the same vaccine antigen. This is, at least partly, due to the lack of secretory expression systems, enabling large-scale extracellular delivery of vaccine and effector proteins by these strains. Because of their low complexity and the terminal location of the secretion signal in the secreted protein, Type I (ATP-binding cassette) secretion systems appear to be particularly suited for development of such recombinant extracellular expression systems. So far, the Escherichia coli hemolysin system is the only Type I secretion system, which has been adapted to recombinant protein secretion in Salmonella. However, this system has a number of disadvantages, including low secretion capacity, complex genetic regulation, and structural restriction to the secreted protein, which eventually hinder high-level in vivo delivery of recombinant vaccines and effector proteins. Thus, the development of more efficient recombinant protein secretion systems, based on Type I exporters can help to improve efficacies of live recombinant Salmonella vaccines. Type I secretion systems, mediating secretion of bacterial surface layer proteins, such as RsaA in Caulobacter crescentus, are discussed as promising candidates for improved secretory delivery systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0928-8244(03)00092-0
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  • 5
    Electronic Resource
    Electronic Resource
    A Salmonella typhimurium strain genetically engineered to secrete effectively a bioactive human interleukin (hIL)-6 via the Escherichia coli hemolysin secretion apparatus (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 20 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Human interleukin-6 (hIL-6) cDNA was genetically fused with the Escherichia coli hemolysin secretorial signal (hlyAS) sequence in a plasmid vector. Recombinant E. coli XL-1 Blue and attenuated Salmonella typhimurium secreted a 30 kDa hIL-6-HlyAS fusion protein, with an additional form of higher apparent molecular mass produced by S. typhimurium. In S. typhimurium cultures hIL-6-HlyAS concentrations entered a plateau at 500 to 600 ng ml−1 culture supernatant. In contrast to E. coli XL-1 Blue, in S. typhimurium culture supernatants hIL-6-HlyAS was accumulated faster reaching three-fold higher maximal concentrations. The cell proliferating activity of hIL-6-HlyAS fusion protein(s) was equivalent to that of mature recombinant hIL-6. Furthermore, hIL-6-secreting S. typhimurium were less invasive than the attenuated control strain. Therefore, the bulky hemolysin secretorial peptide at the C-terminus of the fusion protein does not markably affect hIL-6 activity, suggesting that the hemolysin secretion apparatus provides an excellent system to study immunomodulatory effects of in situ synthesized IL-6 in Salmonella vaccine strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01117.x
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of in situ expression of human interleukin-6 on antibody responses against Salmonella typhimurium antigens (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 37 (2003), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In an attempt to trigger increased mucosal secretory immune responses against bacterial surface antigens, we constructed an optimized human interleukin (hIL)-6-secreting Salmonella typhimurium strain (X4064(pCH1A+pYL3E)), utilizing the hemolysin (Hly) exporter for secretory delivery of a functional hIL-6-hemolysin fusion protein (hIL-6-HlyAs). Through stable introduction of a second hIL-6-HlyAs expression plasmid (pYL3E) in the previously described X4064(pCH1A) strain, hIL-6-HlyAs secretion efficiencies were increased by at least 10-fold. As pCH1A in the parental strain, pYL3E was stable in vitro in the absence of antibiotic selection and in vivo neither did plasmids interfere in their stabilities. Increased hIL-6-HlyAs expression did not adversely interfere with bacterial growth. Comparative immunization experiments in mice with oral application of the different hIL-6-secreting strains revealed that increased in situ hIL-6-production influenced systemic antibody responses against Salmonella antigens but had no marked effect on mucosal responses. In mice immunized with X4064(pCH1A+pYL3E) significantly higher sera IgG and IgA titers for lipopolysaccharide (LPS) were found compared to mice immunized with X4064(pCH1A) and a hIL-6-negative control strain. Higher sera antibody titers were accompanied by increased numbers of IgG- and IgA-specific antibody-secreting cells in spleens and Peyer's patches, respectively. These data suggest that systemic antibody responses against Salmonella LPS are largely effected by IL-6 and, moreover, the amount and the cellular location of recombinantly expressed IL-6 appears to be crucial for enhancement of immune responses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0928-8244(03)00066-X
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  • 7
    Electronic Resource
    Electronic Resource
    Molecular analysis of hemolysin-mediated secretion of a human interleukin-6 fusion protein in Salmonella typhimurium (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: Previously, we reported a plasmid-bearing Salmonella typhimurium strain capable of secreting human interleukin-6 (hIL-6) when genetically fused to the Escherichia coli hemolysin transport signal (HlyAS). Stationary phase culture supernatants of this strain revealed three major forms of hIL-6-HlyAS fusion protein (apparent molecular masses 32.4, 30.3, 27.0 kDa), at which the largest protein presumably represented full-length hIL-6-HlyAS. The biological activity of the hIL-6-HlyAS protein mixture was similar to that of mature hIL-6. Accumulation of hIL-6-HlyAS in the culture supernatant occurred only during the initial growth phase, whereas in stationary phase and under in vitro conditions successive cleavage into the two truncated forms was observed. On the other hand, in whole cell lysates only full-length hIL-6-HlyAS could be detected, accounting for more than 50% of the totally synthesized protein. Upon cell fractionation, cellular hIL-6-HlyAS was exclusively found in the membrane fraction. These results suggest, that in S. typhimurium production and secretion of hIL-6-HlyAS is restricted to growing cells. A specific processing by a Salmonella-derived protease did not affect the biological activity of the fusion protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01447.x
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation of RNA polymerases from the water mold Achlya (1982)
    Springer
    Planta 154 (1982), S. 53-59 
    Details
    ISSN: 1432-2048
    Keywords: Achlya ; Fungi RNA polymerase (DNA-dependent)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The DNA-dependent RNA polymerases I, II, and III (ribonucleosidetriphosphate: RNA nucleotidyl-transferase, EC 2.7.7.6) from Achlya ambisexualis E87 (male), have been isolated. The highly purified RNA polymerase I was found to be composed of polypeptides with the following molecular weights (·10-4): 18.5, 14, 11.8, 7.3, 6.1, 4.9, 4.4, 2.8. RNA polymerase II showed a 400-fold higher resistance against α-amanitin than mammalian or higher plant RNA polymerase II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385496
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  • 9
    Electronic Resource
    Electronic Resource
    Animal Meal: Production and Determination in Feedstuffs and the Origin of Bovine Spongiform Encephalopathy (1999)
    Springer
    Naturwissenschaften 86 (1999), S. 62-70 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001140050573
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  • 10
    Electronic Resource
    Electronic Resource
    Charakterisierung des Regenerationsprozesses im Caulonema eines Mooses durch autoradiographische Bestimmung der DNS-Synthese (1969)
    Springer
    Planta 88 (1969), S. 288-292 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ten-cell-long filaments of the caulonema of Funaria hygrometrica were isolated and labeled with 3H-thymidine. During the process of regeneration this precursor is incorporated into the nucleus and the chloroplasts. The nuclei of aged cells are preferentially labeled, even the nuclei of such cells which probably will no longer divide. From these facts it is concluded that DNA synthesis can occur during the process of regeneration irrespectively of a following cell division.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385072
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