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Volumn 5, Issue , 2014, Pages

Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPASE A2 TYPE IIA; SECRETORY PHOSPHOLIPASE A2; UNCLASSIFIED DRUG; BACTERIAL TOXIN; EXOENZYME S; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHOLIPASE A2 GROUP II; PLA2G2A PROTEIN, HUMAN;

EID: 84923273698     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6105     Document Type: Article
Times cited : (99)

References (70)
  • 1
    • 79957946294 scopus 로고    scopus 로고
    • Managing cystic fibrosis: Strategies that increase life expectancy and improve quality of life
    • Cohen-Cymberknoh, M., Shoseyov, D. & Kerem, E. Managing cystic fibrosis: strategies that increase life expectancy and improve quality of life. Am. J. Respir. Crit. Care Med. 183, 1463-1471 (2011).
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , pp. 1463-1471
    • Cohen-Cymberknoh, M.1    Shoseyov, D.2    Kerem, E.3
  • 2
    • 77950682572 scopus 로고    scopus 로고
    • The changing microbial epidemiology in cystic fibrosis
    • Lipuma, J. J. The changing microbial epidemiology in cystic fibrosis. Clin. Microbiol. Rev. 23, 299-323 (2010).
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 299-323
    • Lipuma, J.J.1
  • 3
    • 0024423668 scopus 로고
    • Identification of the cystic fibrosis gene: Genetic analysis
    • Kerem, B. et al. Identification of the cystic fibrosis gene: genetic analysis. Science 245, 1073-1080 (1989).
    • (1989) Science , vol.245 , pp. 1073-1080
    • Kerem, B.1
  • 4
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan, J. R. et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066-1073 (1989).
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1
  • 5
    • 0036258208 scopus 로고    scopus 로고
    • Cystic fibrosis: A worldwide analysis of CFTR mutations - Correlation with incidence data and application to screening
    • Bobadilla, J. L., Macek, Jr M., Fine, J. P. & Farrell, P. M. Cystic fibrosis: a worldwide analysis of CFTR mutations - correlation with incidence data and application to screening. Hum. Mutat. 19, 575-606 (2002).
    • (2002) Hum. Mutat. , vol.19 , pp. 575-606
    • Bobadilla, J.L.1    Macek, M.2    Fine, J.P.3    Farrell, P.M.4
  • 6
    • 84859620802 scopus 로고    scopus 로고
    • Cystic fibrosis: A mucosal immunodeficiency syndrome
    • Cohen, T. S. & Prince, A. Cystic fibrosis: a mucosal immunodeficiency syndrome. Nat. Med. 18, 509-519 (2012).
    • (2012) Nat. Med. , vol.18 , pp. 509-519
    • Cohen, T.S.1    Prince, A.2
  • 7
    • 70350233621 scopus 로고    scopus 로고
    • Cystic fibrosis infections: Treatment strategies and prospects
    • George, A. M., Jones, P. M. & Middleton, P. G. Cystic fibrosis infections: treatment strategies and prospects. FEMS Microbiol. Lett. 300, 153-164 (2009).
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 153-164
    • George, A.M.1    Jones, P.M.2    Middleton, P.G.3
  • 8
    • 78751559949 scopus 로고    scopus 로고
    • Clinical significance of microbial infection and adaptation in cystic fibrosis
    • Hauser, A. R., Jain, M., Bar-Meir, M. & McColley, S. A. Clinical significance of microbial infection and adaptation in cystic fibrosis. Clin. Microbiol. Rev. 24, 29-70 (2011).
    • (2011) Clin. Microbiol. Rev. , vol.24 , pp. 29-70
    • Hauser, A.R.1    Jain, M.2    Bar-Meir, M.3    McColley, S.A.4
  • 9
    • 79958089335 scopus 로고    scopus 로고
    • Chronic Pseudomonas aeruginosa infection definition: EuroCareCF Working Group report
    • Pressler, T. et al. Chronic Pseudomonas aeruginosa infection definition: EuroCareCF Working Group report. J. Cyst. Fibros. 10(Suppl 2): S75-S78 (2011).
    • (2011) J. Cyst. Fibros. , vol.10 , pp. S75-S78
    • Pressler, T.1
  • 10
    • 0030768159 scopus 로고    scopus 로고
    • Lower airway inflammation in infants and young children with cystic fibrosis
    • Armstrong, D. S. et al. Lower airway inflammation in infants and young children with cystic fibrosis. Am. J. Respir. Crit. Care Med. 156, 1197-1204 (1997).
    • (1997) Am. J. Respir. Crit. Care Med. , vol.156 , pp. 1197-1204
    • Armstrong, D.S.1
  • 11
    • 34247210823 scopus 로고    scopus 로고
    • Microbial ecology of the cystic fibrosis lung
    • Harrison, F. Microbial ecology of the cystic fibrosis lung. Microbiology 153, 917-923 (2007).
    • (2007) Microbiology , vol.153 , pp. 917-923
    • Harrison, F.1
  • 12
    • 70349815600 scopus 로고    scopus 로고
    • Respiratory microbiology of patients with cystic fibrosis in the United States, 1995 to 2005
    • Razvi, S. et al. Respiratory microbiology of patients with cystic fibrosis in the United States, 1995 to 2005. Chest 136, 1554-1560 (2009).
    • (2009) Chest , vol.136 , pp. 1554-1560
    • Razvi, S.1
  • 13
    • 84869219279 scopus 로고    scopus 로고
    • Adaptation of Pseudomonas aeruginosa to the cystic fibrosis airway: An evolutionary perspective
    • Folkesson, A. et al. Adaptation of Pseudomonas aeruginosa to the cystic fibrosis airway: an evolutionary perspective. Nat. Rev. Microbiol. 10, 841-851 (2012).
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 841-851
    • Folkesson, A.1
  • 15
    • 0035750309 scopus 로고    scopus 로고
    • Mammalian secreted phospholipases A2 and their pathophysiological significance in inflammatory diseases
    • Touqui, L. & Alaoui-El-Azher, M. Mammalian secreted phospholipases A2 and their pathophysiological significance in inflammatory diseases. Curr. Mol. Med. 1, 739-754 (2001).
    • (2001) Curr. Mol. Med. , vol.1 , pp. 739-754
    • Touqui, L.1    Alaoui-El-Azher, M.2
  • 16
  • 17
    • 77953287244 scopus 로고    scopus 로고
    • Type-IIA secreted phospholipase A2 is an endogenous antibioticlike protein of the host
    • Wu, Y. et al. Type-IIA secreted phospholipase A2 is an endogenous antibioticlike protein of the host. Biochimie 92, 583-587 (2010).
    • (2010) Biochimie , vol.92 , pp. 583-587
    • Wu, Y.1
  • 18
    • 79952080909 scopus 로고    scopus 로고
    • Recent progress in phospholipase A(2) research: From cells to animals to humans
    • Murakami, M. et al. Recent progress in phospholipase A(2) research: from cells to animals to humans. Prog. Lipid Res. 50, 152-192 (2011).
    • (2011) Prog. Lipid Res. , vol.50 , pp. 152-192
    • Murakami, M.1
  • 19
    • 27744432345 scopus 로고    scopus 로고
    • In vivo protective role of human group IIa phospholipase A2 against experimental anthrax
    • Piris-Gimenez, A. et al. In vivo protective role of human group IIa phospholipase A2 against experimental anthrax. J. Immunol. 175, 6786-6791 (2005).
    • (2005) J. Immunol , vol.175 , pp. 6786-6791
    • Piris-Gimenez, A.1
  • 20
    • 0033104949 scopus 로고    scopus 로고
    • Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria
    • Foreman-Wykert, A. K., Weinrauch, Y., Elsbach, P. & Weiss, J. Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria. J. Clin. Invest. 103, 715-721 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 715-721
    • Foreman-Wykert, A.K.1    Weinrauch, Y.2    Elsbach, P.3    Weiss, J.4
  • 21
    • 0031596818 scopus 로고    scopus 로고
    • Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears
    • Qu, X. D. & Lehrer, R. I. Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears. Infect. Immun. 66, 2791-2797 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 2791-2797
    • Qu, X.D.1    Lehrer, R.I.2
  • 22
    • 84868121259 scopus 로고    scopus 로고
    • Biochemical characterization of selective inhibitors of human group IIA secreted phospholipase A(2) and hyaluronic acid-linked inhibitor conjugates
    • Oslund, R. C. & Gelb, M. H. Biochemical characterization of selective inhibitors of human group IIA secreted phospholipase A(2) and hyaluronic acid-linked inhibitor conjugates. Biochemistry 51, 8617-8626 (2012).
    • (2012) Biochemistry , vol.51 , pp. 8617-8626
    • Oslund, R.C.1    Gelb, M.H.2
  • 23
    • 84897118527 scopus 로고    scopus 로고
    • Secreted group IIA phospholipase A2 protects humans against the group B streptococcus: Experimental and clinical evidence
    • Movert, E. et al. Secreted group IIA phospholipase A2 protects humans against the group B streptococcus: experimental and clinical evidence. J. Infect. Dis. 208, 2025-2035 (2013).
    • (2013) J. Infect. Dis. , vol.208 , pp. 2025-2035
    • Movert, E.1
  • 24
    • 18044393018 scopus 로고    scopus 로고
    • Time-resolved fluoroimmunoassays of the complete set of secreted phospholipases A2 in human serum
    • Nevalainen, T. J. et al. Time-resolved fluoroimmunoassays of the complete set of secreted phospholipases A2 in human serum. Biochim. Biophys. Acta 1733, 210-223 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1733 , pp. 210-223
    • Nevalainen, T.J.1
  • 25
    • 0029882783 scopus 로고    scopus 로고
    • Expression of human group II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate
    • Grass, D. S. et al. Expression of human group II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate. J. Clin. Invest. 97, 2233-2241 (1996).
    • (1996) J. Clin. Invest. , vol.97 , pp. 2233-2241
    • Grass, D.S.1
  • 26
    • 33746290411 scopus 로고    scopus 로고
    • Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels
    • Eerola, L. I. et al. Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels. Biochim. Biophys. Acta 1761, 745-756 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 745-756
    • Eerola, L.I.1
  • 27
    • 0031182988 scopus 로고    scopus 로고
    • Endotoxin induces expression of type II phospholipase A2 in macrophages during acute lung injury in guinea pigs: Involvement of TNFalpha in lipopolysaccharide-induced type II phospholipase A2 synthesis
    • Arbibe, L. et al. Endotoxin induces expression of type II phospholipase A2 in macrophages during acute lung injury in guinea pigs: involvement of TNFalpha in lipopolysaccharide-induced type II phospholipase A2 synthesis. J. Immunol. 159, 391-400 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 391-400
    • Arbibe, L.1
  • 28
    • 0026148375 scopus 로고
    • A cystic fibrosis bronchial epithelial cell line: Immortalization by adeno-12-SV40 infection
    • Zeitlin, P. L. et al. A cystic fibrosis bronchial epithelial cell line: immortalization by adeno-12-SV40 infection. Am. J. Respir. Cell Mol. Biol. 4, 313-319 (1991).
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 313-319
    • Zeitlin, P.L.1
  • 29
    • 15544380187 scopus 로고    scopus 로고
    • Activities of Pseudomonas aeruginosa effectors secreted by the Type III secretion system in vitro and during infection
    • Lee, V. T., Smith, R. S., Tummler, B. & Lory, S. Activities of Pseudomonas aeruginosa effectors secreted by the Type III secretion system in vitro and during infection. Infect. Immun. 73, 1695-1705 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 1695-1705
    • Lee, V.T.1    Smith, R.S.2    Tummler, B.3    Lory, S.4
  • 30
    • 69249157248 scopus 로고    scopus 로고
    • The type III secretion system of Pseudomonas aeruginosa: Infection by injection
    • Hauser, A. R. The type III secretion system of Pseudomonas aeruginosa: infection by injection. Nat. Rev. Microbiol. 7, 654-665 (2009).
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 654-665
    • Hauser, A.R.1
  • 31
    • 0041322625 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa exoenzyme S as a bifunctional enzyme in J774A.1 macrophages
    • Rocha, C. L., Coburn, J., Rucks, E. A. & Olson, J. C. Characterization of Pseudomonas aeruginosa exoenzyme S as a bifunctional enzyme in J774A.1 macrophages. Infect. Immun. 71, 5296-5305 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 5296-5305
    • Rocha, C.L.1    Coburn, J.2    Rucks, E.A.3    Olson, J.C.4
  • 32
    • 33749241159 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa infection of airway epithelial cells modulates expression of Kruppel-like factors 2 and 6 via RsmA-mediated regulation of type III exoenzymes S and y
    • O'Grady, E. P., Mulcahy, H., O'Callaghan, J., Adams, C. & O'Gara, F. Pseudomonas aeruginosa infection of airway epithelial cells modulates expression of Kruppel-like factors 2 and 6 via RsmA-mediated regulation of type III exoenzymes S and Y. Infect. Immun. 74, 5893-5902 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 5893-5902
    • O'grady, E.P.1    Mulcahy, H.2    O'callaghan, J.3    Adams, C.4    O'gara, F.5
  • 33
    • 33845929250 scopus 로고    scopus 로고
    • Selection for Staphylococcus aureus small-colony variants due to growth in the presence of Pseudomonas aeruginosa
    • Hoffman, L. R. et al. Selection for Staphylococcus aureus small-colony variants due to growth in the presence of Pseudomonas aeruginosa. Proc. Natl Acad. Sci. USA 103, 19890-19895 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 19890-19895
    • Hoffman, L.R.1
  • 34
    • 0025881764 scopus 로고
    • Interaction between Pseudomonas aeruginosa and Staphylococcus aureus: Description of an anti-staphylococcal substance
    • Machan, Z. A. et al. Interaction between Pseudomonas aeruginosa and Staphylococcus aureus: description of an anti-staphylococcal substance. J. Med. Microbiol. 34, 213-217 (1991).
    • (1991) J. Med. Microbiol. , vol.34 , pp. 213-217
    • Machan, Z.A.1
  • 35
    • 11844260138 scopus 로고    scopus 로고
    • Staphylococcus aureus serves as an iron source for Pseudomonas aeruginosa during in vivo coculture
    • Mashburn, L. M., Jett, A. M., Akins, D. R. & Whiteley, M. Staphylococcus aureus serves as an iron source for Pseudomonas aeruginosa during in vivo coculture. J. Bacteriol. 187, 554-566 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 554-566
    • Mashburn, L.M.1    Jett, A.M.2    Akins, D.R.3    Whiteley, M.4
  • 36
    • 79960360061 scopus 로고    scopus 로고
    • Pattern differentiation in co-culture biofilms formed by Staphylococcus aureus and Pseudomonas aeruginosa
    • Yang, L. et al. Pattern differentiation in co-culture biofilms formed by Staphylococcus aureus and Pseudomonas aeruginosa. FEMS Immunol. Med. Microbiol. 62, 339-347 (2011).
    • (2011) FEMS Immunol. Med. Microbiol. , vol.62 , pp. 339-347
    • Yang, L.1
  • 37
    • 0034739464 scopus 로고    scopus 로고
    • Roles of secretory phospholipases A(2) in inflammatory diseases and trauma
    • Nevalainen, T. J., Haapamaki, M. M. & Gronroos, J. M. Roles of secretory phospholipases A(2) in inflammatory diseases and trauma. Biochim. Biophys. Acta 1488, 83-90 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 83-90
    • Nevalainen, T.J.1    Haapamaki, M.M.2    Gronroos, J.M.3
  • 38
    • 1542644985 scopus 로고    scopus 로고
    • Bactericidal properties of group IIa secreted phospholipase A(2) against Pseudomonas aeruginosa clinical isolates
    • Dubouix, A. et al. Bactericidal properties of group IIa secreted phospholipase A(2) against Pseudomonas aeruginosa clinical isolates. J. Med. Microbiol. 52, 1039-1045 (2003).
    • (2003) J. Med. Microbiol. , vol.52 , pp. 1039-1045
    • Dubouix, A.1
  • 39
    • 42949115487 scopus 로고    scopus 로고
    • Wall teichoic acid deficiency in Staphylococcus aureus confers selective resistance to mammalian group IIA phospholipase A(2) and human beta-defensin. 3
    • Koprivnjak, T., Weidenmaier, C., Peschel, A. & Weiss, J. P. Wall teichoic acid deficiency in Staphylococcus aureus confers selective resistance to mammalian group IIA phospholipase A(2) and human beta-defensin. 3. Infect. Immun. 76, 2169-2176 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 2169-2176
    • Koprivnjak, T.1    Weidenmaier, C.2    Peschel, A.3    Weiss, J.P.4
  • 40
    • 0028928122 scopus 로고
    • Human neutrophils store type II 14-kDa phospholipase A2 in granules and secrete active enzyme in response to soluble stimuli
    • Rosenthal, M. D. et al. Human neutrophils store type II 14-kDa phospholipase A2 in granules and secrete active enzyme in response to soluble stimuli. Biochem. Biophys. Res. Commun. 208, 650-656 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 650-656
    • Rosenthal, M.D.1
  • 41
    • 0029994903 scopus 로고    scopus 로고
    • Determinants of activation by complement of group II phospholipase A2 acting against Escherichia coli
    • Madsen, L. M., Inada, M. & Weiss, J. Determinants of activation by complement of group II phospholipase A2 acting against Escherichia coli. Infect. Immun. 64, 2425-2430 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 2425-2430
    • Madsen, L.M.1    Inada, M.2    Weiss, J.3
  • 42
    • 27144514336 scopus 로고    scopus 로고
    • Impact of CFTR DeltaF508 mutation on prostaglandin E2 production and type IIA phospholipase A2 expression by pulmonary epithelial cells
    • Medjane, S., Raymond, B., Wu, Y. & Touqui, L. Impact of CFTR DeltaF508 mutation on prostaglandin E2 production and type IIA phospholipase A2 expression by pulmonary epithelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol 289, L816-L824 (2005).
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.289 , pp. L816-L824
    • Medjane, S.1    Raymond, B.2    Wu, Y.3    Touqui, L.4
  • 43
    • 59849110833 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa type III effectors in disease
    • Engel, J. & Balachandran, P. Role of Pseudomonas aeruginosa type III effectors in disease. Curr. Opin. Microbiol. 12, 61-66 (2009).
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 61-66
    • Engel, J.1    Balachandran, P.2
  • 44
    • 0034103142 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa cystic fibrosis isolates induce rapid, type III secretion-dependent, but ExoU-independent, oncosis of macrophages and polymorphonuclear neutrophils
    • Dacheux, D. et al. Pseudomonas aeruginosa cystic fibrosis isolates induce rapid, type III secretion-dependent, but ExoU-independent, oncosis of macrophages and polymorphonuclear neutrophils. Infect. Immun. 68, 2916-2924 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 2916-2924
    • Dacheux, D.1
  • 45
    • 0035877065 scopus 로고    scopus 로고
    • Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections
    • Roy-Burman, A. et al. Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections. J. Infect. Dis. 183, 1767-1774 (2001).
    • (2001) J. Infect. Dis. , vol.183 , pp. 1767-1774
    • Roy-Burman, A.1
  • 46
    • 78149481592 scopus 로고    scopus 로고
    • Mammalian Kruppel-like factors in health and diseases
    • McConnell, B. B. & Yang, V. W. Mammalian Kruppel-like factors in health and diseases. Physiol. Rev. 90, 1337-1381 (2010).
    • (2010) Physiol. Rev. , vol.90 , pp. 1337-1381
    • McConnell, B.B.1    Yang, V.W.2
  • 47
    • 2542500709 scopus 로고    scopus 로고
    • KLF2 is a novel transcriptional regulator of endothelial proinflammatory activation
    • SenBanerjee, S. et al. KLF2 Is a novel transcriptional regulator of endothelial proinflammatory activation. J. Exp. Med. 199, 1305-1315 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1305-1315
    • Senbanerjee, S.1
  • 48
    • 33646236121 scopus 로고    scopus 로고
    • Kruppel-like factor 2 (KLF2) regulates proinflammatory activation of monocytes
    • Das, H. et al. Kruppel-like factor 2 (KLF2) regulates proinflammatory activation of monocytes. Proc. Natl Acad. Sci. USA 103, 6653-6658 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6653-6658
    • Das, H.1
  • 49
    • 45249102660 scopus 로고    scopus 로고
    • Abrogation of anti-inflammatory transcription factor LKLF in neutrophil-dominated airways
    • Saavedra, M. T. et al. Abrogation of anti-inflammatory transcription factor LKLF in neutrophil-dominated airways. Am. J. Respir. Cell Mol. Biol. 38, 679-688 (2008).
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.38 , pp. 679-688
    • Saavedra, M.T.1
  • 50
    • 72449182630 scopus 로고    scopus 로고
    • Bacterial toxins induce sustained mRNA expression of the silencing transcription factor klf2 via inactivation of RhoA and Rhophilin. 1
    • Dach, K. et al. Bacterial toxins induce sustained mRNA expression of the silencing transcription factor klf2 via inactivation of RhoA and Rhophilin. 1. Infect. Immun. 77, 5583-5592 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 5583-5592
    • Dach, K.1
  • 51
    • 77956217437 scopus 로고    scopus 로고
    • TLR2-and nucleotide-binding oligomerization domain 2-dependent Kruppel-like factor 2 expression downregulates NF-kappa B-related gene expression
    • Zahlten, J. et al. TLR2-and nucleotide-binding oligomerization domain 2-dependent Kruppel-like factor 2 expression downregulates NF-kappa B-related gene expression. J. Immunol. 185, 597-604 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 597-604
    • Zahlten, J.1
  • 52
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPaseactivating protein for Rho GTPases
    • Goehring, U. M., Schmidt, G., Pederson, K. J., Aktories, K. & Barbieri, J. T. The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPaseactivating protein for Rho GTPases. J. Biol. Chem. 274, 36369-36372 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36369-36372
    • Goehring, U.M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 53
    • 2942702104 scopus 로고    scopus 로고
    • High bactericidal efficiency of type iia phospholipase A2 against Bacillus anthracis and inhibition of its secretion by the lethal toxin
    • Gimenez, A. P. et al. High bactericidal efficiency of type iia phospholipase A2 against Bacillus anthracis and inhibition of its secretion by the lethal toxin. J. Immunol. 173, 521-530 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 521-530
    • Gimenez, A.P.1
  • 54
    • 0037097770 scopus 로고    scopus 로고
    • Bactericidal group IIA phospholipase A2 in serum of patients with bacterial infections
    • Gronroos, J. O., Laine, V. J. & Nevalainen, T. J. Bactericidal group IIA phospholipase A2 in serum of patients with bacterial infections. J. Infect. Dis. 185, 1767-1772 (2002).
    • (2002) J. Infect. Dis. , vol.185 , pp. 1767-1772
    • Gronroos, J.O.1    Laine, V.J.2    Nevalainen, T.J.3
  • 55
    • 83755183819 scopus 로고    scopus 로고
    • A novel bacterial resistance mechanism against human group IIA-secreted phospholipase A2: Role of Streptococcus pyogenes sortase A
    • Movert, E., Wu, Y., Lambeau, G., Touqui, L. & Areschoug, T. A novel bacterial resistance mechanism against human group IIA-secreted phospholipase A2: role of Streptococcus pyogenes sortase A. J. Immunol. 187, 6437-6446 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 6437-6446
    • Movert, E.1    Wu, Y.2    Lambeau, G.3    Touqui, L.4    Areschoug, T.5
  • 56
    • 0028872519 scopus 로고
    • Bactericidal properties of murine intestinal phospholipase A2
    • Harwig, S. S. et al. Bactericidal properties of murine intestinal phospholipase A2. J. Clin. Invest. 95, 603-610 (1995).
    • (1995) J. Clin. Invest. , vol.95 , pp. 603-610
    • Harwig, S.S.1
  • 57
    • 0038312912 scopus 로고    scopus 로고
    • The antimicrobial activity of the cathelicidin LL37 is inhibited by F-actin bundles and restored by gelsolin
    • Weiner, D. J., Bucki, R. & Janmey, P. A. The antimicrobial activity of the cathelicidin LL37 is inhibited by F-actin bundles and restored by gelsolin. Am. J. Respir. Cell. Mol. Biol. 28, 738-745 (2003).
    • (2003) Am. J. Respir. Cell. Mol. Biol. , vol.28 , pp. 738-745
    • Weiner, D.J.1    Bucki, R.2    Janmey, P.A.3
  • 58
    • 1642405248 scopus 로고    scopus 로고
    • Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen, C. I., Schaller-Bals, S., Paul, K. P., Wahn, U. & Bals, R. Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. J. Cyst. Fibros. 3, 45-50 (2004).
    • (2004) J. Cyst. Fibros. , vol.3 , pp. 45-50
    • Chen, C.I.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 59
    • 84863476402 scopus 로고    scopus 로고
    • Reduced airway surface pH impairs bacterial killing in the porcine cystic fibrosis lung
    • Pezzulo, A. A. et al. Reduced airway surface pH impairs bacterial killing in the porcine cystic fibrosis lung. Nature 487, 109-113 (2012).
    • (2012) Nature , vol.487 , pp. 109-113
    • Pezzulo, A.A.1
  • 60
    • 0041440107 scopus 로고    scopus 로고
    • Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: Evidence for a possible association between O serotypes and exo genes
    • Berthelot, P. et al. Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: evidence for a possible association between O serotypes and exo genes. J. Infect. Dis. 188, 512-518 (2003).
    • (2003) J. Infect. Dis. , vol.188 , pp. 512-518
    • Berthelot, P.1
  • 61
    • 0029987492 scopus 로고    scopus 로고
    • Isolation of an IHF-deficient mutant of a Pseudomonas aeruginosa mucoid isolate and evaluation of the role of IHF in algD gene expression
    • Delic-Attree, I., Toussaint, B., Froger, A., Willison, J. C. & Vignais, P. M. Isolation of an IHF-deficient mutant of a Pseudomonas aeruginosa mucoid isolate and evaluation of the role of IHF in algD gene expression. Microbiology 142(Pt 10): 2785-2793 (1996).
    • (1996) Microbiology , vol.142 , pp. 2785-2793
    • Delic-Attree, I.1    Toussaint, B.2    Froger, A.3    Willison, J.C.4    Vignais, P.M.5
  • 62
    • 47949127946 scopus 로고    scopus 로고
    • Control of Pseudomonas aeruginosa in the lung requires the recognition of either lipopolysaccharide or flagellin
    • Ramphal, R. et al. Control of Pseudomonas aeruginosa in the lung requires the recognition of either lipopolysaccharide or flagellin. J. Immunol. 181, 586-592 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 586-592
    • Ramphal, R.1
  • 63
    • 0029152947 scopus 로고
    • A natural disruption of the secretory group II phospholipase A2 gene in inbred mouse strains
    • Kennedy, B. P. et al. A natural disruption of the secretory group II phospholipase A2 gene in inbred mouse strains. J. Biol. Chem. 270, 22378-22385 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22378-22385
    • Kennedy, B.P.1
  • 64
    • 77952425348 scopus 로고    scopus 로고
    • IL-10 delivery by AAV5 vector attenuates inflammation in mice with Pseudomonas pneumonia
    • Buff, S. M. et al. IL-10 delivery by AAV5 vector attenuates inflammation in mice with Pseudomonas pneumonia. Gene Ther. 17, 567-576 (2010).
    • (2010) Gene Ther , vol.17 , pp. 567-576
    • Buff, S.M.1
  • 65
    • 0028212809 scopus 로고
    • Reduction in viscosity of cystic fibrosis sputum in vitro by gelsolin
    • Vasconcellos, C. A. et al. Reduction in viscosity of cystic fibrosis sputum in vitro by gelsolin. Science 263, 969-971 (1994).
    • (1994) Science , vol.263 , pp. 969-971
    • Vasconcellos, C.A.1
  • 66
    • 0029099327 scopus 로고
    • DNA concentration and length in sputum of patients with cystic fibrosis during inhalation with recombinant human DNase
    • Brandt, T., Breitenstein, S., von der Hardt, H. & Tummler, B. DNA concentration and length in sputum of patients with cystic fibrosis during inhalation with recombinant human DNase. Thorax 50, 880-882 (1995).
    • (1995) Thorax , vol.50 , pp. 880-882
    • Brandt, T.1    Breitenstein, S.2    Von Der Hardt, H.3    Tummler, B.4
  • 67
    • 0017082276 scopus 로고
    • Reversible envelope effects during and after killing of Escherichia coli w by a highly-purified rabbit polymorpho-nuclear leukocyte fraction
    • Weiss, J., Franson, C., Schmeidler, K. & Elsbach, P. Reversible envelope effects during and after killing of Escherichia coli w by a highly-purified rabbit polymorpho-nuclear leukocyte fraction. Biochim. Biophys. Acta 436, 154-169 (1976).
    • (1976) Biochim. Biophys. Acta , vol.436 , pp. 154-169
    • Weiss, J.1    Franson, C.2    Schmeidler, K.3    Elsbach, P.4
  • 68
    • 0029985501 scopus 로고    scopus 로고
    • Involvement of secretory phospholipase A2 activity in the zymosan rat air pouch model of inflammation
    • Paya, M., Terencio, M. C., Ferrandiz, M. L. & Alcaraz, M. J. Involvement of secretory phospholipase A2 activity in the zymosan rat air pouch model of inflammation. Br. J. Pharmacol. 117, 1773-1779 (1996).
    • (1996) Br. J. Pharmacol. , vol.117 , pp. 1773-1779
    • Paya, M.1    Terencio, M.C.2    Ferrandiz, M.L.3    Alcaraz, M.J.4
  • 69
    • 6444222548 scopus 로고    scopus 로고
    • Intranasal steroids decrease eosinophils but not mucin expression in nasal polyps
    • Burgel, P. R., Cardell, L. O., Ueki, I. F. & Nadel, J. A. Intranasal steroids decrease eosinophils but not mucin expression in nasal polyps. Eur. Respir. J. 24, 594-600 (2004).
    • (2004) Eur. Respir. J. , vol.24 , pp. 594-600
    • Burgel, P.R.1    Cardell, L.O.2    Ueki, I.F.3    Nadel, J.A.4
  • 70
    • 84890011741 scopus 로고    scopus 로고
    • CFTR dysfunction induces vascular endothelial growth factor synthesis in airway epithelium
    • Martin, C. et al. CFTR dysfunction induces vascular endothelial growth factor synthesis in airway epithelium. Eur. Respir. J. 42, 1553-1562 (2013).
    • (2013) Eur. Respir. J. , vol.42 , pp. 1553-1562
    • Martin, C.1


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