Inhibition of human natural killer cell activity by Pseudomonas aeruginosa alkaline protease and elastase.
The present study was designed to examine the effect of Pseudomonas aeruginosa alkaline protease (AP) and elastase (Ela) on human natural killer (NK) cell activity in vitro. AP and Ela were found to inhibit NK cell function. Addition of alpha interferon and interleukin-2 did not abolish this inhibition of NK cell activity. Adhesion of effector to target cells was studied in a single-cell agarose assay of monocyte-depleted NK-cell-enriched cell populations. AP and Ela were shown to inhibit effector/target cell conjugate formation. Furthermore, AP and Ela inhibited the binding of the monoclonal antibody Leu-11, which reacts with the Fc receptor of NK cells. The inhibition of NK cell binding to the target cell by P. aeruginosa proteases is most likely due to proteolytic cleavage of the surface receptors involved in the binding of the effector cell to the target cell.
D002478:Cells, Cultured; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D007111:Immunity, Cellular; D007113:Immunity, Innate; D007370:Interferon Type I / Q000494:pharmacology; D007376:Interleukin-2 / Q000494:pharmacology; D007694:Killer Cells, Natural / Q000276:immunology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000276:immunology; D011956:Receptors, Cell Surface / Q000378:metabolism; D012697:Serine Endopeptidases
D007370:Interferon Type I; D007376:Interleukin-2; D011956:Receptors, Cell Surface; D010450:Endopeptidases; D012697:Serine Endopeptidases; D010196:Pancreatic Elastase; C032923:microbial serine proteinases