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  • Blackwell Publishing Ltd  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Host cell protein tyrosine kinases are activated during the entry of Listeria monocytogenes (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 162 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Listeria monocytogenes is able to invade a wide range of cell types by inducing its own internalization. Little is known, however, about the host cell proteins affecting the entry process which involves triggering the host cell signal transduction mechanism. We report here that entry of L. monocytogenes strains (serotypes 4b and 1/2a) into Caco-2 cells induced tyrosine phosphorylation of several host cell proteins including pp60c-src substrates. Using specific synthetic peptide substrates, we showed that L. monocytogenes activates, as early as 5 min after bacteria-cell contact, the pp60c-src family-related (srcFR) proteins by an inlAB-dependent pathway. The activation of srcFR proteins seems to be crucial in the entry of L. monocytogenes into Caco-2 cells. Indeed, specific inhibition of the srcFR signal by herbimycin A blocked the entry of L. monocytogenes strains. Taken together, our data show that L. monocytogenes enhances cell tyrosine phosphorylations and activates the pp60c-src family-related proteins by an inlAB-dependent pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb12995.x
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  • 2
    Electronic Resource
    Electronic Resource
    Precise excision and secondary transposition of TnphoA in non-motile mutants of a Salmonella enterica serovar Enteritidis clinical isolate (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 245 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Mutagenesis with TnphoA has been widely used in many bacteria. Here, we report the excision and secondary transposition of this transposon in three non-motile (fliC, fliF and motB) mutants of Salmonella enterica serovar Enteritidis (S. Enteritidis). Isolation of motile revertants showed that they were kanamycin resistant and conserved a copy of TnphoA in their genome in an insertion site different from the initial one. They also expressed an intact flagella. Characterization of the motile revertant derived from the fliC mutant showed that TnphoA excised precisely from the fliC gene, resulting in an equivalent amount of FliC secreted protein in the revertant compared to that of the wild-type strain. These results show that TnphoA mutants should be used with care and underline the value of using transposon derivatives lacking the transposase gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.03.018
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    Paper (German National Licenses)
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