title: Cytokine stimulation by Pseudomonas aeruginosa--strain variation and modulation by pulmonary surfactant.
abstract: Pulmonary surfactant and its components are part of the first-line immune defense within the lung. Here the authors show that the surfactant protein (SP) SP-D, but not SP-A, agglutinates some clinical isolates of Pseudomonas aeruginosa and Stenotrophomonas maltophilia. No agglutination of Staphylococcus aureus or Burkholderia cepacia was observed. The SP-D-induced agglutination of P. aeruginosa was not dependent on a specific lipopolysaccharide (LPS) serotype. The authors also show that SP-D, but not SP-A, increased the tumor necrosis factor (TNF alpha) release from human monocytic cells in response to a subset of P. aeruginosa and P. aeruginosa LPS. A clinical preparation of surfactant (Alveofact) blocked the TNF alpha release from monocytic cells induced by P. aeruginosa or its LPS. SP-A reversed the inhibitory effect of Alveofact in 6/8 strains of P. aeruginosa and 2/9 preparations of P. aeruginosa LPS. SP-D did not significantly alter the TNF alpha production induced by vital P. aeruginosa in the presence of Alveofact but markedly increased the TNF alpha release induced by a preparation of rough and smooth P. aeruginosa LPS. In summary, this study shows that the immunomodulatory properties of SP-A and SP-D specifically depend on the colonizing strain of P. aeruginosa. In addition, the authors show that the function of SP-A and SP-D is modulated in the presence of surfactant lipids.
authors.affiliation: Dr. von Haunersches Kinderspital, University of Munich, Lindwarmstr. D-80337 Munich, Germany.
authors.forename: Philip
authors.initials: P
authors.lastname: Bufler
authors.forename: Daniela
authors.initials: D
authors.lastname: Schikor
authors.forename: Bettina
authors.initials: B
authors.lastname: Schmidt
authors.forename: Matthias
authors.initials: M
authors.lastname: Griese
mesh_terms: D001422:Bacterial Adhesion / Q000187:drug effects; D002460:Cell Line; D003550:Cystic Fibrosis / Q000276:immunology; D015536:Down-Regulation / Q000187:drug effects; D006801:Humans; D008055:Lipids / Q000494:pharmacology; D008070:Lipopolysaccharides / Q000494:pharmacology; D009000:Monocytes / Q000166:cytology / Q000378:metabolism / Q000382:microbiology*; D010743:Phospholipids / Q000494:pharmacology; D011552:Pseudomonas Infections / Q000276:immunology / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000145:classification / Q000276:immunology*; D037662:Pulmonary Surfactant-Associated Protein A / Q000494:pharmacology*; D037663:Pulmonary Surfactant-Associated Protein D / Q000494:pharmacology; D013045:Species Specificity; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism*
chemical_list: D008055:Lipids; D008070:Lipopolysaccharides; D010743:Phospholipids; D037662:Pulmonary Surfactant-Associated Protein A; D037663:Pulmonary Surfactant-Associated Protein D; C078272:SF-RI 1, bovine surfactant preparation; D014409:Tumor Necrosis Factor-alpha