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  • 1
    Online Resource
    Online Resource
    Analysis of the Legionella pneumophila fliI gene: intracellular growth of a defined mutant defective for flagellum biosynthesis
    American Society for Microbiology ; 1997
    In:  Infection and Immunity Vol. 65, No. 6 ( 1997-06), p. 2497-2501
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 65, No. 6 ( 1997-06), p. 2497-2501
    Abstract: Using a PCR-based strategy and degenerate oligonucleotides, we isolated a Legionella pneumophila gene that showed high sequence similarity to members of the fliI gene family. An insertion mutation that disrupted the fliI open reading frame was recombined onto the L. pneumophila chromosome and analyzed for its effects on production of flagella and intracellular growth. The mutation resulted in loss of surface-localized flagellin protein but had no effect on the ability of the bacteria to grow within cultured cells. Therefore, in spite of the fact that some aflagellar mutations render L. pneumophila unable to grow within macrophages, the isolation of this defined mutant confirms that production of flagella is not required for intracellular growth.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.65.6.2497-2501.1997
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 1483247-1
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  • 2
    Online Resource
    Online Resource
    Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages
    American Society for Microbiology ; 1997
    In:  Infection and Immunity Vol. 65, No. 2 ( 1997-02), p. 571-578
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 65, No. 2 ( 1997-02), p. 571-578
    Abstract: The Legionella pneumophila dotA gene is required for intracellular growth of the bacterium in macrophages. In this study, a structure-function analysis of the DotA protein was conducted to elucidate the role of this protein in L. pneumophila pathogenesis. Translational fusions of dotA to the Escherichia coli phoA and lacZ genes indicated that DotA is an integral cytoplasmic membrane protein with eight membrane-spanning domains. DotA contains two large periplasmic domains of approximately 503 and 73 amino acids and a carboxyl-terminal cytoplasmic domain of 122 amino acids. Protein fractionation studies were consistent with DotA residing in the inner membrane. An alkaline phosphatase fusion located 9 amino acids upstream from the C terminus of DotA still retained function and was able to restore intracellular growth when harbored by two L. pneumophila dotA mutants. A hybrid protein from which the carboxyl-terminal 48 amino acids of DotA were deleted was unable to complement the intracellular growth defect in the dotA mutants, indicating that this cytoplasmic region is required for function.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.65.2.571-578.1997
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 1483247-1
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  • 3
    Online Resource
    Online Resource
    ChemInform Abstract: CIS-DIMETHYLDIAZENE
    Wiley ; 1977
    In:  Chemischer Informationsdienst Vol. 8, No. 21 ( 1977-05-24), p. no-no
    Details
    In: Chemischer Informationsdienst, Wiley, Vol. 8, No. 21 ( 1977-05-24), p. no-no
    Type of Medium: Online Resource
    ISSN: 0009-2975
    URL: Issue
    URL: Article
    DOI: 10.1002/chin.v8.21
    DOI: 10.1002/chin.197721145
    Language: German
    Publisher: Wiley
    Publication Date: 1977
    detail.hit.zdb_id: 2110203-X
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  • 4
    Online Resource
    Online Resource
    The Legionella Effector RavZ Inhibits Host Autophagy Through Irreversible Atg8 Deconjugation
    American Association for the Advancement of Science (AAAS) ; 2012
    In:  Science Vol. 338, No. 6110 ( 2012-11-23), p. 1072-1076
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 338, No. 6110 ( 2012-11-23), p. 1072-1076
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.1227026
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2012
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
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  • 5
    Online Resource
    Online Resource
    Mapping and topographic localization of epitopes of the Yersinia pseudotuberculosis invasin protein
    American Society for Microbiology ; 1991
    In:  Infection and Immunity Vol. 59, No. 10 ( 1991-10), p. 3424-3433
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 59, No. 10 ( 1991-10), p. 3424-3433
    Abstract: The Yersinia pseudotuberculosis invasin protein is a 986-amino-acid outer membrane protein that promotes bacterial penetration into mammalian cells by binding to beta 1-chain integrin receptors. We previously showed that the integrin binding domain is encoded by the carboxyl-terminal 192 amino acids. To further investigate the structure of this protein, we characterized a set of 32 monoclonal antibodies (MAbs) directed against invasin. Invasin deletion derivatives and fusion proteins carrying different segments of invasin were used to map the epitopes of this set of MAbs into 10 overlapping but distinct intervals. Indirect immunofluorescence of intact bacteria expressing invasin demonstrated that two large regions of invasin contain epitopes exposed on the bacterial surface. To assess the role of these surface-exposed regions in the binding and invasion of mammalian cells, each of the MAbs was tested for its ability to inhibit these processes. All of the MAbs that recognized bacterial surface-exposed epitopes in the cell binding domain of invasin inhibited both cell attachment and cell penetration, and no other MAbs inhibited either activity.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.59.10.3424-3433.1991
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1483247-1
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  • 6
    Online Resource
    Online Resource
    Control of the Balb/c-3T3 cell cycle by nutrients and serum factors: Analysis using platelet-derived growth factor and platelet-poor plasma
    Wiley ; 1979
    In:  Journal of Cellular Physiology Vol. 99, No. 3 ( 1979-06), p. 395-405
    Details
    In: Journal of Cellular Physiology, Wiley, Vol. 99, No. 3 ( 1979-06), p. 395-405
    Type of Medium: Online Resource
    ISSN: 0021-9541 , 1097-4652
    URL: Issue
    URL: Journal
    URL: Article
    DOI: 10.1002/jcp.v99:3
    DOI: 10.1002/(ISSN)1097-4652
    DOI: 10.1002/jcp.1040990314
    Language: English
    Publisher: Wiley
    Publication Date: 1979
    detail.hit.zdb_id: 1478143-8
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    American Society for Microbiology ; 1995
    In:  Infection and Immunity Vol. 63, No. 9 ( 1995-09), p. 3609-3620
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 63, No. 9 ( 1995-09), p. 3609-3620
    Abstract: Legionella pneumophila replicates within a membrane-bounded compartment that is studded with ribosomes. In this study we investigated whether these ribosomes originate from the cytoplasmic pool or are associated with host endoplasmic reticulum (ER). Immunofluorescence and electron microscopic localization studies of ER proteins in macrophages infected with L. pneumophila indicated that the bacteria reside in a compartment surrounded by ER. An L. pneumophila mutant that grows slowly in macrophages was slow to associate with host ER, providing genetic evidence in support of the hypothesis that this specialized vacuole is required for intracellular bacterial growth. Ultrastructural studies, in which the ER luminal protein BiP was labeled by immunoperoxidase cytochemistry, revealed that L. pneumophila replication vacuoles resemble nascent autophagosomes. Furthermore, short-term amino acid starvation of macrophages, which stimulated host autophagosomes. Furthermore, short-term amino acid starvation of macrophages, which stimulated host autophagy, increased association of the bacteria with the ER and enhanced bacterial growth. These results are compatible with the hypothesis that L. pneumophila exploits the autophagy machinery of macrophages to establish an intracellular niche favorable for replication.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.63.9.3609-3620.1995
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 1483247-1
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  • 8
    Online Resource
    Online Resource
    New gene in Escherichia coli K-12 (drpA): does its product play a role in RNA synthesis?
    American Society for Microbiology ; 1985
    In:  Journal of Bacteriology Vol. 162, No. 1 ( 1985-04), p. 117-123
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 162, No. 1 ( 1985-04), p. 117-123
    Abstract: The mutation drpA1 defines a new gene in Escherichia coli K-12 that maps at about 5.2 min. This mutation was obtained after enriching a population of cells for temperature sensitive dna mutations with the [3H]thymidine "suicide" technique followed by screening for mutants defective in transposon Tn5 precise excision. When growing cells carrying the drpA1 allele were shifted to the nonpermissive temperature, we showed that DNA, RNA, and protein syntheses shut off quickly, with the cessation of RNA synthesis occurring first. A recombinant plasmid between pBR322 and an HindIII fragment from wild-type E. coli restores the growth defect in drpA1 mutants. Using transposon Tn5 mutagenesis of this plasmid, we have been able to correlate the presence of a 68-kilodalton protein, as observed with the maxicell technique, with the ability of this plasmid to restore growth to drpA1 mutants.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.162.1.117-123.1985
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1985
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    The psa locus is responsible for thermoinducible binding of Yersinia pseudotuberculosis to cultured cells
    American Society for Microbiology ; 1996
    In:  Infection and Immunity Vol. 64, No. 7 ( 1996-07), p. 2483-2489
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 64, No. 7 ( 1996-07), p. 2483-2489
    Abstract: Yersinia pseudotuberculosis inv mutant strains cured of the virulence plasmid exhibit thermoinducible adhesion to cultured mammalian cells. To identify the genes responsible for this phenotype, Y. pseudotuberculosis homologs of the Y. enterocolitica ail and the Y. pestis psa loci were identified. Mutations in the Y. pseudotuberculosis ail and psa loci were constructed and tested for thermoinducible binding. Results of cellular binding assays indicated that only mutations in psa, not in ail, resulted in defects for thermoinducible binding, with inv yadA psa strains showing no detectable cell adhesion. In addition, an inv psa strain was defective for hemagglutination of sheep erythrocytes, in contrast to an inv psa+ strain which was fully competent for hemagglutination. The introduction of a plasmid containing a 6.7-kb KpnI-ClaI fragment of Y. pseudotuberculosis encompassing the psa locus was sufficient to complement both the cell adhesion and hemagglutination defects of the psa mutant. Results from subcloning and transposon mutagenesis indicated that the complete 6.7-kb region was required for thermoinducible binding and hemagglutination.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.64.7.2483-2489.1996
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1996
    detail.hit.zdb_id: 1483247-1
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  • 10
    Online Resource
    Online Resource
    Analysis of expression and thermoregulation of the Yersinia pseudotuberculosis inv gene with hybrid proteins
    American Society for Microbiology ; 1988
    In:  Infection and Immunity Vol. 56, No. 8 ( 1988-08), p. 2133-2138
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 56, No. 8 ( 1988-08), p. 2133-2138
    Abstract: A series of translational fusions between the Yersinia pseudotuberculosis inv locus and lacZ was constructed. Each Lac+ fusion strain expressed a hybrid protein containing invasin, the product of the inv locus, at its amino-terminal end. Analysis of these gene fusions allowed determination of the direction of translation of the inv gene. Previous studies of Y. pseudotuberculosis invasion have shown that entry into animal cells is temperature regulated. It is shown here that control of expression of the inv gene is also temperature regulated. phoA gene fusions to inv, when present in Y. pseudotuberculosis, were expressed at lower levels when bacteria were grown at 37 degrees C rather than at 28 degrees C. Similar fusions, in contrast, were regulated in a temperature-independent fashion in Escherichia coli, as was the wild-type inv gene. This implies that Y. pseudotuberculosis has chromosomally encoded trans-acting functions that normally thermoregulate expression of inv.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.56.8.2133-2138.1988
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1988
    detail.hit.zdb_id: 1483247-1
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