메뉴 건너뛰기




Volumn 11, Issue 6-7, 2009, Pages 671-679

Inhibition of the human neutrophil NADPH oxidase by Coxiella burnetii

Author keywords

Coxiella; NADPH oxidase; Neutrophil; Phagocytosis; Superoxide anion

Indexed keywords

ANTISERUM; PHORBOL 13 ACETATE 12 MYRISTATE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; ZYMOSAN;

EID: 67649213525     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2009.04.005     Document Type: Article
Times cited : (50)

References (36)
  • 1
    • 34748829871 scopus 로고    scopus 로고
    • Coxiella burnetii: host and bacterial responses to infection
    • Waag D.M. Coxiella burnetii: host and bacterial responses to infection. Vaccine 25 (2007) 7288-7295
    • (2007) Vaccine , vol.25 , pp. 7288-7295
    • Waag, D.M.1
  • 2
    • 33947141939 scopus 로고    scopus 로고
    • Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii
    • Voth D.E., and Heinzen R.A. Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii. Cell. Microbiol. 9 (2007) 829-840
    • (2007) Cell. Microbiol. , vol.9 , pp. 829-840
    • Voth, D.E.1    Heinzen, R.A.2
  • 3
    • 6044244833 scopus 로고    scopus 로고
    • Temporal analysis of Coxiella burnetii morphological differentiation
    • Coleman S.A., Fischer E.R., Howe D., Mead D.J., and Heinzen R.A. Temporal analysis of Coxiella burnetii morphological differentiation. J. Bacteriol. 186 (2004) 7344-7352
    • (2004) J. Bacteriol. , vol.186 , pp. 7344-7352
    • Coleman, S.A.1    Fischer, E.R.2    Howe, D.3    Mead, D.J.4    Heinzen, R.A.5
  • 5
    • 0021907261 scopus 로고
    • Lipopolysaccharide variation in Coxiella burnetti: intrastrain heterogeneity in structure and antigenicity
    • Hackstadt T., Peacock M.G., Hitchcock P.J., and Cole R.L. Lipopolysaccharide variation in Coxiella burnetti: intrastrain heterogeneity in structure and antigenicity. Infect. Immun. 48 (1985) 359-365
    • (1985) Infect. Immun. , vol.48 , pp. 359-365
    • Hackstadt, T.1    Peacock, M.G.2    Hitchcock, P.J.3    Cole, R.L.4
  • 6
    • 1842588028 scopus 로고    scopus 로고
    • Genetic control of natural resistance of mouse macrophages to Coxiella burnetii infection in vitro: macrophages from restrictive strains control parasitophorous vacuole maturation
    • Zamboni D.S. Genetic control of natural resistance of mouse macrophages to Coxiella burnetii infection in vitro: macrophages from restrictive strains control parasitophorous vacuole maturation. Infect. Immun. 72 (2004) 2395-2399
    • (2004) Infect. Immun. , vol.72 , pp. 2395-2399
    • Zamboni, D.S.1
  • 8
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with non-phagocyte oxidases
    • Quinn M.T., and Gauss K.A. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with non-phagocyte oxidases. J. Leukoc. Biol. 76 (2004) 760-781
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 9
    • 7044254894 scopus 로고    scopus 로고
    • Both inducible nitric oxide synthase and NADPH oxidase contribute to the control of virulent phase I Coxiella bumetii infections
    • Brennan R.E., Russell K., Zhang G.Q., and Samuel J.E. Both inducible nitric oxide synthase and NADPH oxidase contribute to the control of virulent phase I Coxiella bumetii infections. Infect. Immun. 72 (2004) 6666-6675
    • (2004) Infect. Immun. , vol.72 , pp. 6666-6675
    • Brennan, R.E.1    Russell, K.2    Zhang, G.Q.3    Samuel, J.E.4
  • 10
    • 0242629010 scopus 로고    scopus 로고
    • Mechanisms of pathogenesis: evasion of killing by polymorphonuclear leukocytes
    • Allen L.A.H. Mechanisms of pathogenesis: evasion of killing by polymorphonuclear leukocytes. Microbes Infect. 5 (2003) 1329-1335
    • (2003) Microbes Infect. , vol.5 , pp. 1329-1335
    • Allen, L.A.H.1
  • 11
    • 0025038343 scopus 로고
    • Coxiella burnetii fails to stimulate human neutrophil superoxide anion production
    • Akporiaye E.T., Stefanovich D., Tsosie V., and Baca G. Coxiella burnetii fails to stimulate human neutrophil superoxide anion production. Acta Virol. 34 (1990) 64-70
    • (1990) Acta Virol. , vol.34 , pp. 64-70
    • Akporiaye, E.T.1    Stefanovich, D.2    Tsosie, V.3    Baca, G.4
  • 13
    • 0025023893 scopus 로고
    • Susceptibility of Coxiella burnetii to chemical disinfectants
    • Scott G.H., and Williams J.C. Susceptibility of Coxiella burnetii to chemical disinfectants. Ann. N.Y. Acad. Sci. 590 (1990) 291-296
    • (1990) Ann. N.Y. Acad. Sci. , vol.590 , pp. 291-296
    • Scott, G.H.1    Williams, J.C.2
  • 15
    • 45549093618 scopus 로고    scopus 로고
    • Diagnostic assays for chronic granulomatous disease and other neutrophil disorders
    • Elloumi H.Z., and Holland S.M. Diagnostic assays for chronic granulomatous disease and other neutrophil disorders. Methods Mol. Biol. 412 (2007) 505-523
    • (2007) Methods Mol. Biol. , vol.412 , pp. 505-523
    • Elloumi, H.Z.1    Holland, S.M.2
  • 16
    • 30644458331 scopus 로고    scopus 로고
    • A quantitative nitroblue tetrazolium assay for determining intracellular superoxide anion production in phagocytic cells
    • Choi H.S., Kim J.W., Cha Y.N., and Kim C. A quantitative nitroblue tetrazolium assay for determining intracellular superoxide anion production in phagocytic cells. J. Immunoassay Immunochem. 27 (2006) 31-44
    • (2006) J. Immunoassay Immunochem. , vol.27 , pp. 31-44
    • Choi, H.S.1    Kim, J.W.2    Cha, Y.N.3    Kim, C.4
  • 17
    • 41049098964 scopus 로고    scopus 로고
    • Fractionation and characterization of biologically-active polysaccharides from Artemisia tripartita
    • Xie G., Schepetkin I.A., Siemsen D.W., Kirpotina L.N., Wiley J.A., and Quinn M.T. Fractionation and characterization of biologically-active polysaccharides from Artemisia tripartita. Phytochemistry 69 (2008) 1359-1371
    • (2008) Phytochemistry , vol.69 , pp. 1359-1371
    • Xie, G.1    Schepetkin, I.A.2    Siemsen, D.W.3    Kirpotina, L.N.4    Wiley, J.A.5    Quinn, M.T.6
  • 18
    • 0029080863 scopus 로고
    • Dissociation of Rac translocation from p47-phox/p67-phox movements in human neutrophils by tyrosine kinase inhibitors
    • Dorseuil O., Quinn M.T., and Bokoch G.M. Dissociation of Rac translocation from p47-phox/p67-phox movements in human neutrophils by tyrosine kinase inhibitors. J. Leukoc. Biol. 58 (1995) 108-113
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 108-113
    • Dorseuil, O.1    Quinn, M.T.2    Bokoch, G.M.3
  • 20
    • 3342959166 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection
    • Carlyon J.A., Latif D.A., Pypaert M., Lacy P., and Fikrig E. Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection. Infect. Immun. 72 (2004) 4772-4783
    • (2004) Infect. Immun. , vol.72 , pp. 4772-4783
    • Carlyon, J.A.1    Latif, D.A.2    Pypaert, M.3    Lacy, P.4    Fikrig, E.5
  • 21
    • 0028473441 scopus 로고
    • Characteristics of the inhibition of NADPH oxidase activation in neutrophils by apocynin, a methoxy-substituted catechol
    • Stolk J., Hiltermann T.J., Dijkman J.H., and Verhoeven A.J. Characteristics of the inhibition of NADPH oxidase activation in neutrophils by apocynin, a methoxy-substituted catechol. Am. J. Respir. Cell Mol. Biol. 11 (1994) 95-102
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.11 , pp. 95-102
    • Stolk, J.1    Hiltermann, T.J.2    Dijkman, J.H.3    Verhoeven, A.J.4
  • 22
    • 0032741371 scopus 로고    scopus 로고
    • NADPH oxidase activation and assembly during phagocytosis
    • DeLeo F.R., Allen L.A., Apicella M., and Nauseef W.M. NADPH oxidase activation and assembly during phagocytosis. J. Immunol. 163 (1999) 6732-6740
    • (1999) J. Immunol. , vol.163 , pp. 6732-6740
    • DeLeo, F.R.1    Allen, L.A.2    Apicella, M.3    Nauseef, W.M.4
  • 23
    • 0032981358 scopus 로고    scopus 로고
    • Participation of cofilin in opsonized zymosan-triggered activation of neutrophil-like HL-60 cells through rapid dephosphorylation and translocation to plasma membranes
    • Nagaishi K., Adachi R., Kawanishi T., Yamaguchi T., Kasahara T., Hayakawa T., et al. Participation of cofilin in opsonized zymosan-triggered activation of neutrophil-like HL-60 cells through rapid dephosphorylation and translocation to plasma membranes. J. Biochem. 125 (1999) 891-898
    • (1999) J. Biochem. , vol.125 , pp. 891-898
    • Nagaishi, K.1    Adachi, R.2    Kawanishi, T.3    Yamaguchi, T.4    Kasahara, T.5    Hayakawa, T.6
  • 24
    • 14844355257 scopus 로고    scopus 로고
    • Helicobacter pylori disrupts NADPH oxidase targeting in human neutrophils to induce extracellular superoxide release
    • Allen L.A.H., Beecher B.R., Lynch J.T., Rohner O.V., and Wittine L.M. Helicobacter pylori disrupts NADPH oxidase targeting in human neutrophils to induce extracellular superoxide release. J. Immunol. 174 (2005) 3658-3667
    • (2005) J. Immunol. , vol.174 , pp. 3658-3667
    • Allen, L.A.H.1    Beecher, B.R.2    Lynch, J.T.3    Rohner, O.V.4    Wittine, L.M.5
  • 25
    • 33750611352 scopus 로고    scopus 로고
    • Leishmania donovani lipophosphoglycan blocks NADPH oxidase assembly at the phagosome membrane
    • Lodge R., Diallo T.O., and Descoteaux A. Leishmania donovani lipophosphoglycan blocks NADPH oxidase assembly at the phagosome membrane. Cell. Microbiol. 8 (2006) 1922-1931
    • (2006) Cell. Microbiol. , vol.8 , pp. 1922-1931
    • Lodge, R.1    Diallo, T.O.2    Descoteaux, A.3
  • 26
    • 33845383728 scopus 로고    scopus 로고
    • Francisella tularensis LVS evades killing by human neutrophils via inhibition of the respiratory burst and phagosome escape
    • McCaffrey R.L., and Allen L.A. Francisella tularensis LVS evades killing by human neutrophils via inhibition of the respiratory burst and phagosome escape. J. Leukoc. Biol. 80 (2006) 1224-1230
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 1224-1230
    • McCaffrey, R.L.1    Allen, L.A.2
  • 27
    • 33947101530 scopus 로고    scopus 로고
    • phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes
    • phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes. Cell. Microbiol. 9 (2007) 861-874
    • (2007) Cell. Microbiol. , vol.9 , pp. 861-874
    • Lin, M.1    Rikihisa, Y.2
  • 30
    • 14444282585 scopus 로고    scopus 로고
    • Regulation of Src homology 2-containing tyrosine phosphatase 1 during activation of human neutrophils - role of protein kinase C
    • Brumell J.H., Chan C.K., Butler J., Borregaard N., Siminovitch K.A., Grinstein S., et al. Regulation of Src homology 2-containing tyrosine phosphatase 1 during activation of human neutrophils - role of protein kinase C. J. Biol. Chem. 272 (1997) 875-882
    • (1997) J. Biol. Chem. , vol.272 , pp. 875-882
    • Brumell, J.H.1    Chan, C.K.2    Butler, J.3    Borregaard, N.4    Siminovitch, K.A.5    Grinstein, S.6
  • 31
    • 0035851121 scopus 로고    scopus 로고
    • SHP1 protein-tyrosine phosphatase inhibits gp91PHOX and p67PHOX expression by inhibiting interaction of PU.1, IRF1, interferon consensus sequence-binding protein, and CREB-binding protein with homologous Cis elements in the CYBB and NCF2 genes
    • Kautz B., Kakar R., David E., and Eklund E.A. SHP1 protein-tyrosine phosphatase inhibits gp91PHOX and p67PHOX expression by inhibiting interaction of PU.1, IRF1, interferon consensus sequence-binding protein, and CREB-binding protein with homologous Cis elements in the CYBB and NCF2 genes. J. Biol. Chem. 276 (2001) 37868-37878
    • (2001) J. Biol. Chem. , vol.276 , pp. 37868-37878
    • Kautz, B.1    Kakar, R.2    David, E.3    Eklund, E.A.4
  • 32
    • 20844444211 scopus 로고    scopus 로고
    • Regulation of the Leishmania-induced innate inflammatory response by the protein tyrosine phosphatase SHP-1
    • Forget G., Matte C., Siminovitch K.A., Rivest S., Pouliot P., and Olivier M. Regulation of the Leishmania-induced innate inflammatory response by the protein tyrosine phosphatase SHP-1. Eur. J. Immunol. 35 (2005) 1906-1917
    • (2005) Eur. J. Immunol. , vol.35 , pp. 1906-1917
    • Forget, G.1    Matte, C.2    Siminovitch, K.A.3    Rivest, S.4    Pouliot, P.5    Olivier, M.6
  • 33
    • 0020585752 scopus 로고
    • Superoxide anion production and superoxide dismutase and catalase activities in Coxiella burnetii
    • Akporiaye E.T., and Baca O.G. Superoxide anion production and superoxide dismutase and catalase activities in Coxiella burnetii. J. Bacteriol. 154 (1983) 520-523
    • (1983) J. Bacteriol. , vol.154 , pp. 520-523
    • Akporiaye, E.T.1    Baca, O.G.2
  • 34
    • 0026698104 scopus 로고
    • Coxiella burnetii superoxide dismutase gene: cloning, sequencing, and expression in Escherichia coli
    • Heinzen R.A., Frazier M.E., and Mallavia L.P. Coxiella burnetii superoxide dismutase gene: cloning, sequencing, and expression in Escherichia coli. Infect. Immun. 60 (1992) 3814-3823
    • (1992) Infect. Immun. , vol.60 , pp. 3814-3823
    • Heinzen, R.A.1    Frazier, M.E.2    Mallavia, L.P.3
  • 35
    • 0014137081 scopus 로고
    • Interaction of rickettsiae and phagocytic host cells. V. Phagocytic and opsonic interactions of phase 1 and phase 2 Coxiella burneti with normal and immune human leukocytes and antibodies
    • Wisseman Jr. C.L., Fiset P., and Ormsbee R.A. Interaction of rickettsiae and phagocytic host cells. V. Phagocytic and opsonic interactions of phase 1 and phase 2 Coxiella burneti with normal and immune human leukocytes and antibodies. J. Immunol. 99 (1967) 669-674
    • (1967) J. Immunol. , vol.99 , pp. 669-674
    • Wisseman Jr., C.L.1    Fiset, P.2    Ormsbee, R.A.3
  • 36
    • 3643115942 scopus 로고
    • Study of the antigenic structure of Coxiella burneti. IV. Phagocytosis and opsonization in relation to the phases of C. burneti
    • Brezina R., and Kazár J. Study of the antigenic structure of Coxiella burneti. IV. Phagocytosis and opsonization in relation to the phases of C. burneti. Acta Virol. 9 (1965) 268-274
    • (1965) Acta Virol. , vol.9 , pp. 268-274
    • Brezina, R.1    Kazár, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.