메뉴 건너뛰기




Volumn 67, Issue 9, 1999, Pages 4490-4498

Legionella pneumophila invasion of MRC-5 cells induces tyrosine protein phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYCLOHEXIMIDE; GENISTEIN; TUBULIN; VIMENTIN;

EID: 0032806048     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.9.4490-4498.1999     Document Type: Article
Times cited : (6)

References (39)
  • 1
    • 0028869097 scopus 로고
    • Invasion of HeLa cells by Mycoplasma penetrans and the induction of tyrosine phosphorylation of a 145-kDa host cell protein
    • Andreev, J., Z. Borovsky, I. Rosenshine, and S. Rottem. 1995. Invasion of HeLa cells by Mycoplasma penetrans and the induction of tyrosine phosphorylation of a 145-kDa host cell protein. FEMS Microbiol. Lett. 132:189-194.
    • (1995) FEMS Microbiol. Lett. , vol.132 , pp. 189-194
    • Andreev, J.1    Borovsky, Z.2    Rosenshine, I.3    Rottem, S.4
  • 2
    • 0028131926 scopus 로고
    • Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation during uptake by HeLa cells
    • Birkelund, S., H. Johnsen, and G. Christiansen. 1994. Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation during uptake by HeLa cells. Infect. Immun. 62:4900-4908.
    • (1994) Infect. Immun. , vol.62 , pp. 4900-4908
    • Birkelund, S.1    Johnsen, H.2    Christiansen, G.3
  • 3
    • 0027401507 scopus 로고
    • The role of host tyrosine phosphorylation in bacterial pathogenesis
    • Bliska, J. B., and S. Falkow. 1993. The role of host tyrosine phosphorylation in bacterial pathogenesis. Trends Genet. 9:85-89.
    • (1993) Trends Genet. , vol.9 , pp. 85-89
    • Bliska, J.B.1    Falkow, S.2
  • 4
    • 0027141518 scopus 로고
    • Expression and phosphorylation of the Listeria monocytogenes ActA protein in mammalian cells
    • Brundage, R. A., G. A. Smith, A. Camilli, J. A. Theriot, and D. A. Portnoy. 1993. Expression and phosphorylation of the Listeria monocytogenes ActA protein in mammalian cells. Proc. Natl. Acad. Sci. USA 90:11890-11894.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11890-11894
    • Brundage, R.A.1    Smith, G.A.2    Camilli, A.3    Theriot, J.A.4    Portnoy, D.A.5
  • 5
    • 0021346071 scopus 로고
    • Evidence for differences in the mechanism of cell cycle arrest between senescent and serum-deprived human fibroblasts: Heterokaryon and metabolic inhibitor studies
    • Burmer, G. C., P. S. Rabinovitch, and T. H. Norwood. 1984. Evidence for differences in the mechanism of cell cycle arrest between senescent and serum-deprived human fibroblasts: heterokaryon and metabolic inhibitor studies. J. Cell. Physiol. 118:97-103.
    • (1984) J. Cell. Physiol. , vol.118 , pp. 97-103
    • Burmer, G.C.1    Rabinovitch, P.S.2    Norwood, T.H.3
  • 6
    • 0022450114 scopus 로고
    • Phosphorylation of an Escherichia coli protein at tyrosine
    • Cortay, J. C., B. Duclos, and A. J. Cozzone. 1986. Phosphorylation of an Escherichia coli protein at tyrosine. J. Mol. Biol. 187:305-308.
    • (1986) J. Mol. Biol. , vol.187 , pp. 305-308
    • Cortay, J.C.1    Duclos, B.2    Cozzone, A.J.3
  • 7
    • 0031841257 scopus 로고    scopus 로고
    • Signal transduction during Legionella pneumophila entry into human monocytes
    • Coxon, P. Y., J. T. Summersgill, J. A. Ramirez, and R. D. Miller. 1998. Signal transduction during Legionella pneumophila entry into human monocytes. Infect. Immun. 66:2905-2913.
    • (1998) Infect. Immun. , vol.66 , pp. 2905-2913
    • Coxon, P.Y.1    Summersgill, J.T.2    Ramirez, J.A.3    Miller, R.D.4
  • 8
    • 0024149321 scopus 로고
    • Protein phosphorylation in prokaryotes
    • Cozzone, A. J. 1988. Protein phosphorylation in prokaryotes. Annu. Rev. Microbiol. 42:97-125.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 97-125
    • Cozzone, A.J.1
  • 9
    • 0027511372 scopus 로고
    • ATP-dependent protein kinases in bacteria
    • Cozzone, A. J, 1993. ATP-dependent protein kinases in bacteria. J. Cell. Biochem. 51:7-13.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 7-13
    • Cozzone, A.J.1
  • 10
    • 0025690271 scopus 로고
    • Evidence of protein-tyrosine kinase activity in the bacterium Acinetobacter calcoaceticus
    • Dadssi, M., and A. J. Cozzone. 1990. Evidence of protein-tyrosine kinase activity in the bacterium Acinetobacter calcoaceticus. J. Biol. Chem. 265: 20996-20999.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20996-20999
    • Dadssi, M.1    Cozzone, A.J.2
  • 12
    • 0026642506 scopus 로고
    • A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber, M., and M. Loos. 1992. A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect. Immun. 60:3072-3078.
    • (1992) Infect. Immun. , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 13
    • 0031919615 scopus 로고    scopus 로고
    • BipA: A tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells
    • Farris, M., A. Grant, T. B. Richardson, and C. D. O'Connor. 1998. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells. Mol. Microbiol. 28:265-279.
    • (1998) Mol. Microbiol. , vol.28 , pp. 265-279
    • Farris, M.1    Grant, A.2    Richardson, T.B.3    O'Connor, C.D.4
  • 14
    • 0030782168 scopus 로고    scopus 로고
    • Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin
    • Fawaz, F. S., C. van Ooij, E. Homola, S. C. Mutka, and J. N. Engel. 1997. Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin. Infect. Immun. 65:5301-5308.
    • (1997) Infect. Immun. , vol.65 , pp. 5301-5308
    • Fawaz, F.S.1    Van Ooij, C.2    Homola, E.3    Mutka, S.C.4    Engel, J.N.5
  • 15
    • 0024227182 scopus 로고
    • Virulence factors associated with Salmonella species
    • Finlay, B. B., and S. Falkow, 1988. Virulence factors associated with Salmonella species. Microbiol. Sci. 5:324-328.
    • (1988) Microbiol. Sci. , vol.5 , pp. 324-328
    • Finlay, B.B.1    Falkow, S.2
  • 16
    • 0032465372 scopus 로고    scopus 로고
    • Different fates of Legionella pneumophila pmi and mil mutants within macrophages and alveolar epithelial cells
    • Gao, L.-V., B. J. Stone, J. K. Brieland, and Y. Abu Kwaik. 1998. Different fates of Legionella pneumophila pmi and mil mutants within macrophages and alveolar epithelial cells. Microb. Pathog. 25:291-306.
    • (1998) Microb. Pathog. , vol.25 , pp. 291-306
    • Gao, L.-V.1    Stone, B.J.2    Brieland, J.K.3    Abu Kwaik, Y.4
  • 17
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992 Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89:8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 18
    • 0022881557 scopus 로고
    • Association between Legionella pneumophila and amoebae in water
    • Henke, M., and K. M. Seidel. 1986. Association between Legionella pneumophila and amoebae in water. Isr. J. Med. Sci. 22:690-695.
    • (1986) Isr. J. Med. Sci. , vol.22 , pp. 690-695
    • Henke, M.1    Seidel, K.M.2
  • 19
    • 0023723766 scopus 로고
    • Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis
    • Hess, J. F., R. B. Bourret, and M. I. Simon. 1988. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 336:139-143.
    • (1988) Nature , vol.336 , pp. 139-143
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 20
    • 0024314513 scopus 로고
    • Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen
    • Hoffman, P. S., C. A. Butler, and F. D. Quinn. 1989. Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen. Infect. Immun. 57:1731-1739.
    • (1989) Infect. Immun. , vol.57 , pp. 1731-1739
    • Hoffman, P.S.1    Butler, C.A.2    Quinn, F.D.3
  • 21
    • 0026583898 scopus 로고
    • Cloning and nucleotide sequence of a gene (ompS) encoding the major outer membrane protein of Legionella pneumophila
    • Hoffman, P. S., M. Ripley, and R. Weeratna. 1992. Cloning and nucleotide sequence of a gene (ompS) encoding the major outer membrane protein of Legionella pneumophila. J. Bacteriol. 174:914-920.
    • (1992) J. Bacteriol. , vol.174 , pp. 914-920
    • Hoffman, P.S.1    Ripley, M.2    Weeratna, R.3
  • 22
    • 0025033913 scopus 로고
    • Phosphorylated tyrosine in the flagellum filament protein of Pseudomonas aemginosa
    • Kelly-Wintenberg, K., T. Anderson, and T. C. Montie. 1990. Phosphorylated tyrosine in the flagellum filament protein of Pseudomonas aemginosa. J. Bacteriol. 172:5135-5139.
    • (1990) J. Bacteriol. , vol.172 , pp. 5135-5139
    • Kelly-Wintenberg, K.1    Anderson, T.2    Montie, T.C.3
  • 23
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., R. DeVinney, M. Stein, D. J. Reinscheid, E. A. Frey, and B. B. Finlay. 1997. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91:511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 24
    • 0025086161 scopus 로고
    • Quantitative analysis of cytoskeletal proteins throughout the cell cycle of the MRC-5 fibroblastic cell line
    • Leger, I., F. Giroud, and G. Brugal. 1990. Quantitative analysis of cytoskeletal proteins throughout the cell cycle of the MRC-5 fibroblastic cell line. Anal. Quant. Cytol. Histol. 12:321-326.
    • (1990) Anal. Quant. Cytol. Histol. , vol.12 , pp. 321-326
    • Leger, I.1    Giroud, F.2    Brugal, G.3
  • 25
    • 0031907375 scopus 로고    scopus 로고
    • Entry and intracellular localization of Legionella dumoffii in Vero cells
    • Maruta, K., M. Ogawa, H. Miyamoto, K. Izu, and S. I. Yoshida. 1998. Entry and intracellular localization of Legionella dumoffii in Vero cells. Microb. Pathog. 24:65-73.
    • (1998) Microb. Pathog. , vol.24 , pp. 65-73
    • Maruta, K.1    Ogawa, M.2    Miyamoto, H.3    Izu, K.4    Yoshida, S.I.5
  • 26
    • 0017662282 scopus 로고
    • Legionnaires' disease: Isolation of a bacterium and demonstration of its role in other respiratory disease
    • McDade, J. E., C. C. Shepard, D. W. Fraser, T. R. Tsai, M. A. Redus, and W. R. Dowdle. 1977. Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease. N. Engl. J. Med. 297:1197-1203.
    • (1977) N. Engl. J. Med. , vol.297 , pp. 1197-1203
    • McDade, J.E.1    Shepard, C.C.2    Fraser, D.W.3    Tsai, T.R.4    Redus, M.A.5    Dowdle, W.R.6
  • 27
    • 0027272531 scopus 로고
    • The major iron-containing protein of Legionella pneumophila is an aconitase homologous with the human iron-responsive element-binding protein
    • Mengaud, J. M., and M. A. Horwitz. 1993. The major iron-containing protein of Legionella pneumophila is an aconitase homologous with the human iron-responsive element-binding protein. J. Bacteriol. 175:5666-5676.
    • (1993) J. Bacteriol. , vol.175 , pp. 5666-5676
    • Mengaud, J.M.1    Horwitz, M.A.2
  • 28
    • 0021840153 scopus 로고
    • Adhesion, penetration and intracellular replication of Legionella pneumophila: An in vitro model of pathogenesis
    • Oldham, L. J., and F. G. Rodgers. 1985. Adhesion, penetration and intracellular replication of Legionella pneumophila: an in vitro model of pathogenesis. J. Gen. Microbiol. 131:697-706.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 697-706
    • Oldham, L.J.1    Rodgers, F.G.2
  • 29
    • 0028284101 scopus 로고
    • Genetic approaches to study Legionella pneumophila pathogenicity
    • Ott, M. 1994. Genetic approaches to study Legionella pneumophila pathogenicity. FEMS Microbiol. Rev. 14:161-176.
    • (1994) FEMS Microbiol. Rev. , vol.14 , pp. 161-176
    • Ott, M.1
  • 30
    • 0030888561 scopus 로고    scopus 로고
    • Chlamydia psittaci IncA is phosphorylated by the host cell and is exposed on the cytoplasmic face of the developing inclusion
    • Rockey, D. D., D. Grosenbach, D. E. Hruby, M. G. Peacock, R. A. Heinzen, and T. Hackstadt. 1997. Chlamydia psittaci IncA is phosphorylated by the host cell and is exposed on the cytoplasmic face of the developing inclusion. Mol. Microbiol. 24:217-228.
    • (1997) Mol. Microbiol. , vol.24 , pp. 217-228
    • Rockey, D.D.1    Grosenbach, D.2    Hruby, D.E.3    Peacock, M.G.4    Heinzen, R.A.5    Hackstadt, T.6
  • 31
    • 0026685068 scopus 로고
    • Tyrosine protein kinase inhibitors block invasin-promoted bacterial uptake by epithelial cells
    • Rosenshine, I., V. Duronio, and B. B. Finlay. 1992. Tyrosine protein kinase inhibitors block invasin-promoted bacterial uptake by epithelial cells. Infect. Immun. 60:2211-2217.
    • (1992) Infect. Immun. , vol.60 , pp. 2211-2217
    • Rosenshine, I.1    Duronio, V.2    Finlay, B.B.3
  • 32
    • 0028104144 scopus 로고
    • Salmonella typhimurium invasion of epithelial cells: Role of induced host cell tyrosine protein phosphorylation
    • Rosenshine, I., S. Ruschkowski, V. Foubister, and B. B. Finlay. 1994. Salmonella typhimurium invasion of epithelial cells: role of induced host cell tyrosine protein phosphorylation. Infect. Immun. 62:4969-4974.
    • (1994) Infect. Immun. , vol.62 , pp. 4969-4974
    • Rosenshine, I.1    Ruschkowski, S.2    Foubister, V.3    Finlay, B.B.4
  • 33
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., K. E. Magnusson, and W. H. Wolf. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:964-972.
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf, W.H.3
  • 34
    • 0004282518 scopus 로고
    • SAS Institute, Cary, N.C.
    • SAS Institute Inc. 1989. SAS/STAT user's guide, version 6, p. 943. SAS Institute, Cary, N.C.
    • (1989) SAS/STAT User's Guide, Version 6 , pp. 943
  • 35
    • 0025271478 scopus 로고
    • Signal transduction in bacteria
    • Stock, J. B., A. M. Stock, and J. M. Mottonen. 1990. Signal transduction in bacteria. Nature 344:395-400.
    • (1990) Nature , vol.344 , pp. 395-400
    • Stock, J.B.1    Stock, A.M.2    Mottonen, J.M.3
  • 36
    • 0029944643 scopus 로고    scopus 로고
    • De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells
    • Susa, M., J. Hacker, and R. Marre. 1996. De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells. Infect. Immun. 64:1679-1684.
    • (1996) Infect. Immun. , vol.64 , pp. 1679-1684
    • Susa, M.1    Hacker, J.2    Marre, R.3
  • 37
    • 0018827630 scopus 로고
    • Intracellular multiplication of Legionella pneumophila in cultured human embryonic lung fibroblasts
    • Wong, M. C., E. P. Ewing, Jr., C. S. Callaway, and W. L. Peacock, Jr. 1980. Intracellular multiplication of Legionella pneumophila in cultured human embryonic lung fibroblasts. Infect. Immun. 28:1014-1018.
    • (1980) Infect. Immun. , vol.28 , pp. 1014-1018
    • Wong, M.C.1    Ewing E.P., Jr.2    Callaway, C.S.3    Peacock W.L., Jr.4
  • 38
    • 0026697164 scopus 로고
    • Infection of macrophages with Legionella pneumophila induces phosphorylation of a 76-kilodalton protein
    • Yamamoto, Y., T. W. Klein, H. Shinomiya, M. Nakano, and H. Friedman. 1992. Infection of macrophages with Legionella pneumophila induces phosphorylation of a 76-kilodalton protein. Infect. Immun. 60:3452-3455.
    • (1992) Infect. Immun. , vol.60 , pp. 3452-3455
    • Yamamoto, Y.1    Klein, T.W.2    Shinomiya, H.3    Nakano, M.4    Friedman, H.5
  • 39
    • 0028960755 scopus 로고
    • Zymosantriggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes
    • Zaffran, Y., J. C. Escallier, S. Ruta, C. Capo, and J. L. Mege. 1995. Zymosantriggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes. J. Immun. 154:3488-3497.
    • (1995) J. Immun. , vol.154 , pp. 3488-3497
    • Zaffran, Y.1    Escallier, J.C.2    Ruta, S.3    Capo, C.4    Mege, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.