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  • 1
    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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  • 2
    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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  • 3
    Online Resource
    Online Resource
    The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells
    American Society for Microbiology ; 1992
    In:  Infection and Immunity Vol. 60, No. 9 ( 1992-09), p. 3909-3912
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 60, No. 9 ( 1992-09), p. 3909-3912
    Abstract: Yersinia pseudotuberculosis is able to enter normally nonphagocytic host cells by multiple pathways, the most efficient of which is mediated by invasin, a 986-amino-acid bacterial outer membrane protein. It has previously been shown that the C-terminal 192 amino acids of invasin are sufficient to bind mammalian cells. To determine if additional regions of the invasin protein are necessary to promote entry, we developed a novel assay that tests the ability of various invasin derivatives to confer on Staphylococcus aureus the ability to enter animal cells. We determined that the 192-amino-acid cell-binding region of invasin, when used to coat the bacterial cell surface, was also sufficient to promote cellular penetration. These results suggest that the simple binding of invasin to its receptors is sufficient to mediate entry and that the bacterium plays a largely passive role in the entry process.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.60.9.3909-3912.1992
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1483247-1
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  • 4
    Online Resource
    Online Resource
    Recombination genes on the Escherichia coli sex factor specific for transposable elements.
    Proceedings of the National Academy of Sciences ; 1980
    In:  Proceedings of the National Academy of Sciences Vol. 77, No. 5 ( 1980-05), p. 2814-2818
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 77, No. 5 ( 1980-05), p. 2814-2818
    Abstract: The Escherichia coli sex factor stimulates precise excision of transposons Tn5 and Tn10 from sites either within the bacterial chromosome or within the factor itself. We have isolated two kinds of mutations that affect this activity. The ferA mutations eliminate the stimulation; the ferB mutations enhance it in the presence of FerA+. We conclude that ferA defines a sex factor gene that stimulates precise excision. The ferB mutations also specifically increase the rate of recombination between two IS3 elements on F' lac-pro (F'128) in a reaction that requires the product of recA. The stimulation of this recombination by ferB also requires an active ferA gene, which implies that the ferA gene stimulates this reaction as well as precise excision. A ferA mutation was mapped at 84.2 kilobases on the F factor, and a ferB mutation was mapped at 82.5 kilobases. The fer mutants were obtained by an approach that permits the isolation of mutants affecting precise excision.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.77.5.2814
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1980
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Cultured mammalian cells attach to the invasin protein of Yersinia pseudotuberculosis.
    Proceedings of the National Academy of Sciences ; 1988
    In:  Proceedings of the National Academy of Sciences Vol. 85, No. 18 ( 1988-09), p. 6682-6686
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 85, No. 18 ( 1988-09), p. 6682-6686
    Abstract: The expression of invasin, the product of the Yersinia pseudotuberculosis inv gene, allows enteric bacteria to enter cultured mammalian cells. The ability of invasin to bind animal cells and the potential significance of this interaction in the entry process were investigated. It was found that HEp-2 cells could attach to surfaces coated with bacterial membranes containing invasin. By fractionating bacterial membrane proteins on NaDodSO4/polyacrylamide gels and transferring the protein to filters, we demonstrated that the cell-binding component of the membranes comigrated with invasin. Mutations that changed the electrophoretic mobility of the protein also caused a corresponding shift in the migration of the cell-binding activity, showing that the comigrating protein was indeed invasin. Monoclonal antibodies directed against invasin that blocked invasin-HEp-2 cell interaction also inhibited bacteria from penetrating HEp-2 cells, indicating that interaction of this protein with animal cells is critical for cellular penetration.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.85.18.6682
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1988
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Binding of cultured mammalian cells to immobilized bacteria
    American Society for Microbiology ; 1992
    In:  Infection and Immunity Vol. 60, No. 2 ( 1992-02), p. 683-686
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 60, No. 2 ( 1992-02), p. 683-686
    Abstract: The invasin protein of Yersinia pseudotuberculosis binds to integrin receptors on mammalian cells and promotes cellular penetration. We demonstrate here that the cell attachment activity of invasin can be detected in bacterial colonies that have been immobilized on filter membranes. Invasin expressed in either Escherichia coli K-12 or Y. pseudotuberculosis mediated binding to membranes, and as few as 10(5) Y. pseudotuberculosis resulted in detectable attachment of cultured epithelial cells. A similar binding activity was detected in clinical isolates of the related pathogen Y. enterocolitica but not in environmental isolates. Although there exist multiple mechanisms for the binding of wild-type organisms to host cells, efficient mammalian cell binding to immobilized Y. pseudotuberculosis required expression of a functional invasin protein. Several pathogens that are known to bind or penetrate mammalian cells were also tested, and only one of these bound cultured mammalian cells efficiently.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.60.2.683-686.1992
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1483247-1
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  • 7
    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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