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• W2077302634 endingPage "30" @default.
• W2077302634 startingPage "23" @default.
• W2077302634 abstract "The Mip ('macrophage infectivity potentiator') protein of Legionella pneumophila has been shown to be an essential virulence factor, exhibiting peptidyl-prolyl cis/trans isomerase (PPIase) activity that can be inhibited by the immunosuppressant FK506. The cloning and sequencing of mip genes from three different L. pneumophila strains revealed a single amino acid substitution which did not affect the isomerase property of the enzyme. Mip proteins isolated from two wild-type L. pneumophila strains and from two corresponding Escherichia coli K-12 recombinant clones derived from these strains exhibited identical enzymatic properties and the precursor proteins are processed at identical cleavage sites. The mature Mip proteins exist in an oligomeric form. Site-directed mutagenesis demonstrated that a substitution of an Asp residue at position 142 by a Leu residue affects PPIase activity of Mip." @default.
• W2077302634 created "2016-06-24" @default.
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• W2077302634 date "1994-05-01" @default.
• W2077302634 modified "2023-10-16" @default.
• W2077302634 title "Characterization of Mip proteins of<i>Legionella pneumophila</i>" @default.
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• W2077302634 doi "https://doi.org/10.1111/j.1574-6968.1994.tb06798.x" @default.
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