title: Inhibition of human natural killer cell activity by Legionella pneumophila protease.
abstract: The present study was undertaken to define the effect of Legionella pneumophila protease on natural killer (NK) cell function in vitro. Lysis of target cells by human NK cells was determined using a 51Cr-release assay. The protease inhibited the NK cell cytolytic activity in a concentration- and time-dependent manner. The inhibitory effect of the protease was not affected by alpha interferon or interleukin 2. Legionella pneumophila protease partly inhibited the binding of effector cells to target cells as studied in a single cell agarose assay of monocyte-depleted cell populations. This effect of the protease on the binding of NK cells to target cells could interfere with the previously described enhanced NK cell activity induced by Legionella pneumophila. We could demonstrate in vitro inhibition of NK cell activity by Legionella pneumophila protease at very low concentrations, suggesting a possible relevance of this mechanism in the pathogenesis of Legionnaires' disease.
authors.affiliation: Department of Clinical Microbiology, Statens Seruminstitut, Copenhagen, Denmark.
authors.forename: C
authors.initials: C
authors.lastname: Rechnitzer
authors.forename: M
authors.initials: M
authors.lastname: Diamant
authors.forename: B K
authors.initials: BK
authors.lastname: Pedersen
mesh_terms: D003602:Cytotoxicity, Immunologic; D006801:Humans; D007370:Interferon Type I / Q000494:pharmacology; D007376:Interleukin-2 / Q000494:pharmacology; D007694:Killer Cells, Natural / Q000276:immunology*; D007875:Legionella / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000494:pharmacology*
chemical_list: D007370:Interferon Type I; D007376:Interleukin-2; D010447:Peptide Hydrolases