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Volumn 190, Issue 10, 2008, Pages 3757-3767

Chlamydia pneumoniae GroEL1 protein is cell surface associated and required for infection of HEp-2 cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GROEL1 PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; CHAPERONIN;

EID: 47049107204     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01638-07     Document Type: Article
Times cited : (39)

References (91)
  • 1
    • 0035174615 scopus 로고    scopus 로고
    • Series introduction: The transcription factor NF-kappaB and human disease
    • Baldwin, A. S., Jr. 2001. Series introduction: the transcription factor NF-kappaB and human disease. J. Clin. Investig. 107: 3-6.
    • (2001) J. Clin. Investig , vol.107 , pp. 3-6
    • Baldwin Jr, A.S.1
  • 2
    • 0022410728 scopus 로고
    • Differences in outer membrane proteins of the lymphogranuloma venereum and trachoma biovars of Chlamydia trachomatis
    • Batteiger, B. E., W. J. T. Newhall, and R. B. Jones. 1985. Differences in outer membrane proteins of the lymphogranuloma venereum and trachoma biovars of Chlamydia trachomatis. Infect. Immun. 50: 488-494.
    • (1985) Infect. Immun , vol.50 , pp. 488-494
    • Batteiger, B.E.1    Newhall, W.J.T.2    Jones, R.B.3
  • 3
    • 0025270538 scopus 로고
    • A soluble 60 kilodalton antigen of Chlamydia spp. is a homologue of Escherichia coli GroEL
    • Bavoil, P., R. S. Stephens, and S. Falkow. 1990. A soluble 60 kilodalton antigen of Chlamydia spp. is a homologue of Escherichia coli GroEL. Mol. Microbiol. 4: 461-469.
    • (1990) Mol. Microbiol , vol.4 , pp. 461-469
    • Bavoil, P.1    Stephens, R.S.2    Falkow, S.3
  • 4
    • 29644437923 scopus 로고    scopus 로고
    • GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: Potential role in interactions with the host and the gastric pathogen Helicobacter pylori
    • Bergonzelli, G. E., D. Granato, R. D. Pridmore, L. F. Marvin-Guy, D. Donnicola, and I. E. Corthesy-Theulaz. 2006. GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori. Infect. Immun. 74: 425-434.
    • (2006) Infect. Immun , vol.74 , pp. 425-434
    • Bergonzelli, G.E.1    Granato, D.2    Pridmore, R.D.3    Marvin-Guy, L.F.4    Donnicola, D.5    Corthesy-Theulaz, I.E.6
  • 5
    • 0025372746 scopus 로고
    • The 75-kilodalton cytoplasmic Chlamydia trachomatis L2 polypeptide is a DnaK-like protein
    • Birkelund, S., A. G. Lundemose, and G. Christiansen. 1990. The 75-kilodalton cytoplasmic Chlamydia trachomatis L2 polypeptide is a DnaK-like protein. Infect. Immun. 58: 2098-2104.
    • (1990) Infect. Immun , vol.58 , pp. 2098-2104
    • Birkelund, S.1    Lundemose, A.G.2    Christiansen, G.3
  • 6
    • 0037161370 scopus 로고    scopus 로고
    • Foam cell formation inhibits growth of Chlamydia pneumoniae but does not attenuate Chlamydia pneumoniae-induced secretion of proinflammatory cytokines
    • Blessing, E., C. C. Kuo, T. M. Lin, L. A. Campbell, F. Bea, B. Chesebro, and M. E. Rosenfeld. 2002. Foam cell formation inhibits growth of Chlamydia pneumoniae but does not attenuate Chlamydia pneumoniae-induced secretion of proinflammatory cytokines. Circulation 105: 1976-1982.
    • (2002) Circulation , vol.105 , pp. 1976-1982
    • Blessing, E.1    Kuo, C.C.2    Lin, T.M.3    Campbell, L.A.4    Bea, F.5    Chesebro, B.6    Rosenfeld, M.E.7
  • 7
    • 0028032538 scopus 로고
    • Chlamydia trachomatis antigens: Role in immunity and pathogenesis
    • Brunham, R. C., and R. W. Peeling. 1994. Chlamydia trachomatis antigens: role in immunity and pathogenesis. Infect. Agents Dis. 3: 218-233.
    • (1994) Infect. Agents Dis , vol.3 , pp. 218-233
    • Brunham, R.C.1    Peeling, R.W.2
  • 8
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 9
    • 0036467447 scopus 로고    scopus 로고
    • Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway
    • Bulut, Y., E. Faure, L. Thomas, H. Karahashi, K. S. Michelsen, O. Equils, S. G. Morrison, R. P. Morrison, and M. Arditi. 2002. Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway. J. Immunol. 168: 1435-1440.
    • (2002) J. Immunol , vol.168 , pp. 1435-1440
    • Bulut, Y.1    Faure, E.2    Thomas, L.3    Karahashi, H.4    Michelsen, K.S.5    Equils, O.6    Morrison, S.G.7    Morrison, R.P.8    Arditi, M.9
  • 10
    • 34250307303 scopus 로고    scopus 로고
    • Interactions of Chlamydia with the host cells that mediate attachment and uptake
    • P. M. Bavoil and P. B. Wyrick ed, Norfolk, United Kingdom
    • Campbell, L. A., and C. C. Kuo. 2006. Interactions of Chlamydia with the host cells that mediate attachment and uptake, p. 505-522. In P. M. Bavoil and P. B. Wyrick (ed.), Chlamydia genomics and pathogenesis. Horizon Bioscience, Norfolk, United Kingdom.
    • (2006) Chlamydia genomics and pathogenesis. Horizon Bioscience , pp. 505-522
    • Campbell, L.A.1    Kuo, C.C.2
  • 11
    • 33845415066 scopus 로고    scopus 로고
    • Chlamydia attachment to mammalian cells requires protein disulfide isomerase
    • Conant, C. G., and R. S. Stephens. 2007. Chlamydia attachment to mammalian cells requires protein disulfide isomerase. Cell. Microbiol. 9: 222-232.
    • (2007) Cell. Microbiol , vol.9 , pp. 222-232
    • Conant, C.G.1    Stephens, R.S.2
  • 14
    • 0036084291 scopus 로고    scopus 로고
    • Protein disulfide isomerase, a component of the estrogen receptor complex, is associated with Chlamydia trachomatis serovar E attached to human endometrial epithelial cells
    • Davis, C. H., J. E. Raulston, and P. B. Wyrick. 2002. Protein disulfide isomerase, a component of the estrogen receptor complex, is associated with Chlamydia trachomatis serovar E attached to human endometrial epithelial cells. Infect. Immun. 70: 3413-3418.
    • (2002) Infect. Immun , vol.70 , pp. 3413-3418
    • Davis, C.H.1    Raulston, J.E.2    Wyrick, P.B.3
  • 15
    • 0033613066 scopus 로고    scopus 로고
    • Chlamydia pneumoniae infection of vascular smooth muscle and endothelial cells activates NF-kappaB and induces tissue factor and PAI-1 expression: A potential link to accelerated arteriosclerosis
    • Dechend, R., M. Maass, J. Gieffers, R. Dietz, C. Scheidereit, A. Leutz, and D. C. Gulba. 1999. Chlamydia pneumoniae infection of vascular smooth muscle and endothelial cells activates NF-kappaB and induces tissue factor and PAI-1 expression: a potential link to accelerated arteriosclerosis. Circulation 100: 1369-1373.
    • (1999) Circulation , vol.100 , pp. 1369-1373
    • Dechend, R.1    Maass, M.2    Gieffers, J.3    Dietz, R.4    Scheidereit, C.5    Leutz, A.6    Gulba, D.C.7
  • 16
    • 0033105366 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
    • Dersch, P., and R. R. Isberg. 1999. A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association. EMBO J. 18: 1199-1213.
    • (1999) EMBO J , vol.18 , pp. 1199-1213
    • Dersch, P.1    Isberg, R.R.2
  • 17
    • 0030924854 scopus 로고    scopus 로고
    • Prevalence and correlates of antibody to chlamydial heat shock protein in women attending sexually transmitted disease clinics and women with confirmed pelvic inflammatory disease
    • Eckert, L. O., S. E. Hawes, P. Wolner Hanssen, D. M. Money, R. W. Peeling, R. C. Brunham, C. E. Stevens, D. A. Eschenbach, and W. E. Stamm. 1997. Prevalence and correlates of antibody to chlamydial heat shock protein in women attending sexually transmitted disease clinics and women with confirmed pelvic inflammatory disease. J. Infect. Dis. 175: 1453-1458.
    • (1997) J. Infect. Dis , vol.175 , pp. 1453-1458
    • Eckert, L.O.1    Hawes, S.E.2    Wolner Hanssen, P.3    Money, D.M.4    Peeling, R.W.5    Brunham, R.C.6    Stevens, C.E.7    Eschenbach, D.A.8    Stamm, W.E.9
  • 19
    • 33845939630 scopus 로고    scopus 로고
    • Chlamydia trachomatis OmcB protein is a surface-exposed glycosaminoglycan-dependent adhesin
    • Fadel, S., and A. Eley. 2007. Chlamydia trachomatis OmcB protein is a surface-exposed glycosaminoglycan-dependent adhesin. J. Med. Microbiol. 56: 15-22.
    • (2007) J. Med. Microbiol , vol.56 , pp. 15-22
    • Fadel, S.1    Eley, A.2
  • 20
    • 23344446694 scopus 로고    scopus 로고
    • Endogenous extra-cellular heat shock protein 72: Releasing signal(s) and function
    • Fleshner, M., and J. D. Johnson. 2005. Endogenous extra-cellular heat shock protein 72: releasing signal(s) and function. Int. J. Hyperthermia 21: 457-471.
    • (2005) Int. J. Hyperthermia , vol.21 , pp. 457-471
    • Fleshner, M.1    Johnson, J.D.2
  • 21
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduno, R. A., E. Garduno, and P. S. Hoffman. 1998. Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect. Immun. 66: 4602-4610.
    • (1998) Infect. Immun , vol.66 , pp. 4602-4610
    • Garduno, R.A.1    Garduno, E.2    Hoffman, P.S.3
  • 22
    • 0141817941 scopus 로고    scopus 로고
    • Chlamydia pneumoniae activates epithelial cell proliferation via NF-κB and the glucocorticoid receptor
    • Gencay, M. M., M. Tamm, A. Glanville, A. P. Perruchoud, and M. Roth. 2003. Chlamydia pneumoniae activates epithelial cell proliferation via NF-κB and the glucocorticoid receptor. Infect. Immun. 71: 5814-5822.
    • (2003) Infect. Immun , vol.71 , pp. 5814-5822
    • Gencay, M.M.1    Tamm, M.2    Glanville, A.3    Perruchoud, A.P.4    Roth, M.5
  • 24
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato, D., G. E. Bergonzelli, R. D. Pridmore, L. Marvin, M. Rouvet, and I. E. Corthesy-Theulaz. 2004. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 72: 2160-2169.
    • (2004) Infect. Immun , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 25
    • 0024593926 scopus 로고
    • Chlamydia pneumoniae, strain TWAR
    • Grayston, J. T. 1989. Chlamydia pneumoniae, strain TWAR. Chest 95: 664-669.
    • (1989) Chest , vol.95 , pp. 664-669
    • Grayston, J.T.1
  • 26
    • 0031796521 scopus 로고    scopus 로고
    • Can acute Chlamydia pneumoniae respiratory tract infection initiate chronic asthma?
    • Hahn, D. L., and R. McDonald. 1998. Can acute Chlamydia pneumoniae respiratory tract infection initiate chronic asthma? Ann. Allergy Asthma Immunol. 81: 339-344.
    • (1998) Ann. Allergy Asthma Immunol , vol.81 , pp. 339-344
    • Hahn, D.L.1    McDonald, R.2
  • 27
    • 33745589526 scopus 로고    scopus 로고
    • Stress wars: The direct role of host and bacterial molecular chaperones in bacterial infection
    • Henderson, B., E. Allan, and A. R. Coates. 2006. Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect. Immun. 74: 3693-3706.
    • (2006) Infect. Immun , vol.74 , pp. 3693-3706
    • Henderson, B.1    Allan, E.2    Coates, A.R.3
  • 29
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca, M., S. Borgia, P. Hoffman, and C. A. Lingwood. 1996. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect. Immun. 64: 2643-2648.
    • (1996) Infect. Immun , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 30
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske, K., and R. S. Stephens. 2007. Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc. Natl. Acad. Sci. USA 104: 11430-11435.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.S.2
  • 34
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery, C. J. 1999. Moonlighting proteins. Trends Biochem. Sci. 24: 8-11.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 38
    • 0030772159 scopus 로고    scopus 로고
    • Helicobacter pylori infection activates NF-kappa B in gastric epithelial cells
    • Keates, S., Y. S. Hitti, M. Upton, and C. P. Kelly. 1997. Helicobacter pylori infection activates NF-kappa B in gastric epithelial cells. Gastroenterology 113: 1099-1109.
    • (1997) Gastroenterology , vol.113 , pp. 1099-1109
    • Keates, S.1    Hitti, Y.S.2    Upton, M.3    Kelly, C.P.4
  • 39
    • 0032945716 scopus 로고    scopus 로고
    • Identification of two novel genes encoding 97- to 99-kilodalton outer membrane proteins of Chlamydia pneumoniae
    • Knudsen, K., A. S. Madsen, P. Mygind, G. Christiansen, and S. Birkelund. 1999. Identification of two novel genes encoding 97- to 99-kilodalton outer membrane proteins of Chlamydia pneumoniae. Infect. Immun. 67: 375-383.
    • (1999) Infect. Immun , vol.67 , pp. 375-383
    • Knudsen, K.1    Madsen, A.S.2    Mygind, P.3    Christiansen, G.4    Birkelund, S.5
  • 40
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol, A., T. Bourcier, A. H. Lichtman, and P. Libby. 1999. Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. J. Clin. Investig. 103: 571-577.
    • (1999) J. Clin. Investig , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 41
    • 0033975855 scopus 로고    scopus 로고
    • Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol, A., A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones. 2000. Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J. Immunol. 164: 13-17.
    • (2000) J. Immunol , vol.164 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 45
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn, M. J., and N. C. Kesty. 2005. Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev. 19: 2645-2655.
    • (2005) Genes Dev , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 47
    • 0030455618 scopus 로고    scopus 로고
    • An N linked high mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to Hela cells
    • Kuo, C. C., N. Takahashi, A. F. Swanson, Y. Ozeki, and S. I. Hakomori. 1996. An N linked high mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to Hela cells. J. Clin. Investig. 98: 2813-2818.
    • (1996) J. Clin. Investig , vol.98 , pp. 2813-2818
    • Kuo, C.C.1    Takahashi, N.2    Swanson, A.F.3    Ozeki, Y.4    Hakomori, S.I.5
  • 48
    • 33745603048 scopus 로고    scopus 로고
    • Identification, recombinant expression, immunolocalization in macrophages, and T-cell responsiveness of the major extracellular proteins of Francisella tularensis
    • Lee, B. Y., M. A. Horwitz, and D. L. Clemens. 2006. Identification, recombinant expression, immunolocalization in macrophages, and T-cell responsiveness of the major extracellular proteins of Francisella tularensis. Infect. Immun. 74: 4002-4013.
    • (2006) Infect. Immun , vol.74 , pp. 4002-4013
    • Lee, B.Y.1    Horwitz, M.A.2    Clemens, D.L.3
  • 49
    • 0037223264 scopus 로고    scopus 로고
    • Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages
    • Long, K. H., F. J. Gomez, R. E. Morris, and S. L. Newman. 2003. Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. J. Immunol. 170: 487-494.
    • (2003) J. Immunol , vol.170 , pp. 487-494
    • Long, K.H.1    Gomez, F.J.2    Morris, R.E.3    Newman, S.L.4
  • 50
    • 0025277696 scopus 로고
    • Characterization and identification of early proteins in Chlamydia trachomatis serovar L2 by two-dimensional gel electrophoresis
    • Lundemose, A. G., S. Birkelund, P. M. Larsen, S. J. Fey, and G. Christiansen. 1990. Characterization and identification of early proteins in Chlamydia trachomatis serovar L2 by two-dimensional gel electrophoresis. Infect. Immun. 58: 2478-2486.
    • (1990) Infect. Immun , vol.58 , pp. 2478-2486
    • Lundemose, A.G.1    Birkelund, S.2    Larsen, P.M.3    Fey, S.J.4    Christiansen, G.5
  • 51
    • 19544373825 scopus 로고    scopus 로고
    • Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes
    • Maguire, M., S. Poole, A. R. Coates, P. Tormay, C. Wheeler-Jones, and B. Henderson. 2005. Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes. Immunology 115: 231-238.
    • (2005) Immunology , vol.115 , pp. 231-238
    • Maguire, M.1    Poole, S.2    Coates, A.R.3    Tormay, P.4    Wheeler-Jones, C.5    Henderson, B.6
  • 54
    • 0344420152 scopus 로고    scopus 로고
    • Mitogenic effect of Bartonella bacilliformis on human vascular endothelial cells and involvement of GroEL
    • Minnick, M. F., L. S. Smitherman, and D. S. Samuels. 2003. Mitogenic effect of Bartonella bacilliformis on human vascular endothelial cells and involvement of GroEL. Infect. Immun. 71: 6933-6942.
    • (2003) Infect. Immun , vol.71 , pp. 6933-6942
    • Minnick, M.F.1    Smitherman, L.S.2    Samuels, D.S.3
  • 55
    • 37349053423 scopus 로고    scopus 로고
    • The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding
    • Moelleken, K., and J. H. Hegemann. 2008. The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding. Mol. Microbiol. 67: 403-419.
    • (2008) Mol. Microbiol , vol.67 , pp. 403-419
    • Moelleken, K.1    Hegemann, J.H.2
  • 56
    • 0033020421 scopus 로고    scopus 로고
    • Infection of human endothelial cells with Chlamydia pneumoniae stimulates transendothelial migration of neutrophils and monocytes
    • Molestina, R. E., R. D. Miller, J. A. Ramirez, and J. T. Summersgill. 1999. Infection of human endothelial cells with Chlamydia pneumoniae stimulates transendothelial migration of neutrophils and monocytes. Infect. Immun. 67: 1323-1330.
    • (1999) Infect. Immun , vol.67 , pp. 1323-1330
    • Molestina, R.E.1    Miller, R.D.2    Ramirez, J.A.3    Summersgill, J.T.4
  • 57
    • 0025932077 scopus 로고
    • Chlamydial hsp60 and the immunopathogenesis of chlamydial disease
    • Morrison, R. P. 1991. Chlamydial hsp60 and the immunopathogenesis of chlamydial disease. Semin. Immunol. 3: 25-33.
    • (1991) Semin. Immunol , vol.3 , pp. 25-33
    • Morrison, R.P.1
  • 58
    • 18844369636 scopus 로고    scopus 로고
    • Detection of HSP60 on the membrane surface of stressed human endothelial cells by atomic force and confocal microscopy
    • Pfister, G., C. M. Stroh, H. Perschinka, M. Kind, M. Knoflach, P. Hinterdorfer, and G. Wick. 2005. Detection of HSP60 on the membrane surface of stressed human endothelial cells by atomic force and confocal microscopy. J. Cell Sci. 118: 1587-1594.
    • (2005) J. Cell Sci , vol.118 , pp. 1587-1594
    • Pfister, G.1    Stroh, C.M.2    Perschinka, H.3    Kind, M.4    Knoflach, M.5    Hinterdorfer, P.6    Wick, G.7
  • 59
    • 0029022662 scopus 로고
    • Systemic immunization with Hsp60 alters the development of chlamydial ocular disease
    • Rank, R. G., C. Dascher, A. K. Bowlin, and P. M. Bavoil. 1995. Systemic immunization with Hsp60 alters the development of chlamydial ocular disease. Investig. Ophthalmol. Vis. Sci. 36: 1344-1351.
    • (1995) Investig. Ophthalmol. Vis. Sci , vol.36 , pp. 1344-1351
    • Rank, R.G.1    Dascher, C.2    Bowlin, A.K.3    Bavoil, P.M.4
  • 60
    • 0036151140 scopus 로고    scopus 로고
    • Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds
    • Raulston, J. E., C. H. Davis, T. R. Paul, J. D. Hobbs, and P. B. Wyrick. 2002. Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds. Infect. Immun. 70: 535-543.
    • (2002) Infect. Immun , vol.70 , pp. 535-543
    • Raulston, J.E.1    Davis, C.H.2    Paul, T.R.3    Hobbs, J.D.4    Wyrick, P.B.5
  • 61
    • 0031922926 scopus 로고    scopus 로고
    • Localization of Chlamydia trachomatis heat shock proteins 60 and 70 during infection of a human endometrial epithelial cell line in vitro
    • Raulston, J. E., T. R. Paul, S. T. Knight, and P. B. Wyrick. 1998. Localization of Chlamydia trachomatis heat shock proteins 60 and 70 during infection of a human endometrial epithelial cell line in vitro. Infect. Immun. 66: 2323-2329.
    • (1998) Infect. Immun , vol.66 , pp. 2323-2329
    • Raulston, J.E.1    Paul, T.R.2    Knight, S.T.3    Wyrick, P.B.4
  • 63
    • 0025916624 scopus 로고
    • Endocytic mechanisms utilized by chlamydiae and their influence on induction of productive infection
    • Reynolds, D. J., and J. H. Pearce. 1991. Endocytic mechanisms utilized by chlamydiae and their influence on induction of productive infection. Infect. Immun. 59: 3033-3039.
    • (1991) Infect. Immun , vol.59 , pp. 3033-3039
    • Reynolds, D.J.1    Pearce, J.H.2
  • 64
    • 0023770125 scopus 로고
    • Serological evidence of an association of a novel Chlamydia, TWAR, with chronic coronary heart disease and acute myocardial infarction
    • Saikku, P., M. Leinonen, K. Mattila, M. R. Ekman, M. S. Nieminen, P. H. Makela, J. K. Huttunen, and V. Valtonen. 1988. Serological evidence of an association of a novel Chlamydia, TWAR, with chronic coronary heart disease and acute myocardial infarction. Lancet ii: 983-986.
    • (1988) Lancet , vol.2 , pp. 983-986
    • Saikku, P.1    Leinonen, M.2    Mattila, K.3    Ekman, M.R.4    Nieminen, M.S.5    Makela, P.H.6    Huttunen, J.K.7    Valtonen, V.8
  • 65
    • 0032877283 scopus 로고    scopus 로고
    • Identification of immunoreactive proteins of Chlamydia trachomatis by Western blot analysis of a two-dimensional electrophoresis map with patient sera
    • Sanchez-Campillo, M., L. Bini, M. Comanducci, R. Raggiaschi, B. Marzocchi, V. Pallini, and G. Ratti. 1999. Identification of immunoreactive proteins of Chlamydia trachomatis by Western blot analysis of a two-dimensional electrophoresis map with patient sera. Electrophoresis 20: 2269-2279.
    • (1999) Electrophoresis , vol.20 , pp. 2269-2279
    • Sanchez-Campillo, M.1    Bini, L.2    Comanducci, M.3    Raggiaschi, R.4    Marzocchi, B.5    Pallini, V.6    Ratti, G.7
  • 66
    • 0035800883 scopus 로고    scopus 로고
    • Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via Toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation
    • Sasu, S., D. LaVerda, N. Qureshi, D. T. Golenbock, and D. Beasley. 2001. Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via Toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation. Circ. Res. 89: 244-250.
    • (2001) Circ. Res , vol.89 , pp. 244-250
    • Sasu, S.1    LaVerda, D.2    Qureshi, N.3    Golenbock, D.T.4    Beasley, D.5
  • 67
    • 0031252807 scopus 로고    scopus 로고
    • Activation of NF-kappaB in intestinal epithelial cells by enteropathogenic Escherichia coli
    • Savkovic, S. D., A. Koutsouris, and G. Hecht. 1997. Activation of NF-kappaB in intestinal epithelial cells by enteropathogenic Escherichia coli. Am. J. Physiol. 273C: 1160-1167.
    • (1997) Am. J. Physiol , vol.273 C , pp. 1160-1167
    • Savkovic, S.D.1    Koutsouris, A.2    Hecht, G.3
  • 69
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H., and R. D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16: 339-346.
    • (1989) Curr. Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 70
    • 0026072160 scopus 로고
    • Recombinant Escherichia coli clones expressing Chlamydia trachomatis gene products attach to human endometrial epithelial cells
    • Schmiel, D. H., S. T. Knight, J. E. Raulston, J. Choong, C. H. Davis, and P. B. Wyrick. 1991. Recombinant Escherichia coli clones expressing Chlamydia trachomatis gene products attach to human endometrial epithelial cells. Infect. Immun. 59: 4001-4012.
    • (1991) Infect. Immun , vol.59 , pp. 4001-4012
    • Schmiel, D.H.1    Knight, S.T.2    Raulston, J.E.3    Choong, J.4    Davis, C.H.5    Wyrick, P.B.6
  • 72
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194: 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 74
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 76
    • 0035008930 scopus 로고    scopus 로고
    • Heparin-binding outer membrane protein of chlamydiae
    • Stephens, R. S., K. Koshiyama, E. Lewis, and A. Kubo. 2001. Heparin-binding outer membrane protein of chlamydiae. Mol. Microbiol. 40: 691-699.
    • (2001) Mol. Microbiol , vol.40 , pp. 691-699
    • Stephens, R.S.1    Koshiyama, K.2    Lewis, E.3    Kubo, A.4
  • 77
    • 0242402075 scopus 로고    scopus 로고
    • Association of Chlamydia pneumoniae with central nervous system disease
    • Stratton, C. W., and S. Sriram. 2003. Association of Chlamydia pneumoniae with central nervous system disease. Microbes Infect. 5: 1249-1253.
    • (2003) Microbes Infect , vol.5 , pp. 1249-1253
    • Stratton, C.W.1    Sriram, S.2
  • 78
    • 0029743307 scopus 로고    scopus 로고
    • A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells
    • Su, H., L. Raymond, D. D. Rockey, E. Fischer, T. Hackstadt, and H. D. Caldwell. 1996. A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells. Proc. Natl. Acad. Sci. USA 93: 11143-11148.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11143-11148
    • Su, H.1    Raymond, L.2    Rockey, D.D.3    Fischer, E.4    Hackstadt, T.5    Caldwell, H.D.6
  • 80
    • 0029123843 scopus 로고
    • Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface
    • Ting, L. M., R. C. Hsia, C. G. Haidaris, and P. M. Bavoil. 1995. Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface. Infect. Immun. 63: 3600-3608.
    • (1995) Infect. Immun , vol.63 , pp. 3600-3608
    • Ting, L.M.1    Hsia, R.C.2    Haidaris, C.G.3    Bavoil, P.M.4
  • 81
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas, R. M., P. Ahmad-Nejad, C. da Costa, T. Miethke, C. J. Kirschning, H. Hacker, and H. Wagner. 2001. Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J. Biol. Chem. 276: 31332-31339.
    • (2001) J. Biol. Chem , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    da Costa, C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 82
    • 0345170046 scopus 로고    scopus 로고
    • Chlamydia pneumoniae induces the expression of inhibitor of apoptosis 2 (c-IAP2) in a human monocytic cell line by an NF-kappaB-dependent pathway
    • Wahl, C., S. Maier, R. Marre, and A. Essig. 2003. Chlamydia pneumoniae induces the expression of inhibitor of apoptosis 2 (c-IAP2) in a human monocytic cell line by an NF-kappaB-dependent pathway. Int. J. Med. Microbiol. 293: 377-381.
    • (2003) Int. J. Med. Microbiol , vol.293 , pp. 377-381
    • Wahl, C.1    Maier, S.2    Marre, R.3    Essig, A.4
  • 83
    • 0034778553 scopus 로고    scopus 로고
    • Survival of Chlamydia pneumoniae-infected Mono Mac 6 cells is dependent on NF-κB binding activity
    • Wahl, C., F. Oswald, U. Simnacher, S. Weiss, R. Marre, and A. Essig. 2001. Survival of Chlamydia pneumoniae-infected Mono Mac 6 cells is dependent on NF-κB binding activity. Infect. Immun. 69: 7039-7045.
    • (2001) Infect. Immun , vol.69 , pp. 7039-7045
    • Wahl, C.1    Oswald, F.2    Simnacher, U.3    Weiss, S.4    Marre, R.5    Essig, A.6
  • 84
    • 0002215039 scopus 로고    scopus 로고
    • Mechanisms of chlamydia-induced disease
    • R. S. Stephens ed, ASM Press, Washington, DC
    • Ward, M. E. 1999. Mechanisms of chlamydia-induced disease, p. 171-210. In R. S. Stephens (ed.), Chlamydia: intracellular biology, pathogenesis, and immunity. ASM Press, Washington, DC.
    • (1999) Chlamydia: Intracellular biology, pathogenesis, and immunity , pp. 171-210
    • Ward, M.E.1
  • 85
    • 0942301210 scopus 로고    scopus 로고
    • From the inside out-processing of the chlamydial autotransporter PmpD and its role in bacterial adhesion and activation of human host cells
    • Wehrl, W., V. Brinkmann, P. R. Jungblut, T. F. Meyer, and A. J. Szczepek. 2004. From the inside out-processing of the chlamydial autotransporter PmpD and its role in bacterial adhesion and activation of human host cells. Mol. Microbiol. 51: 319-334.
    • (2004) Mol. Microbiol , vol.51 , pp. 319-334
    • Wehrl, W.1    Brinkmann, V.2    Jungblut, P.R.3    Meyer, T.F.4    Szczepek, A.J.5
  • 86
    • 0042882763 scopus 로고    scopus 로고
    • Infections, heat shock proteins, and atherosclerosis
    • Xu, Q. 2003. Infections, heat shock proteins, and atherosclerosis. Curr. Opin. Cardiol. 18: 245-252.
    • (2003) Curr. Opin. Cardiol , vol.18 , pp. 245-252
    • Xu, Q.1
  • 88
    • 0026742218 scopus 로고
    • Monoclonal antibodies define genus-specific, species-specific, and cross-reactive epitopes of the chlamydial 60-kilodalton heat shock protein (hsp60): Specific immunodetection and purification of chlamydial hsp60
    • Yuan, Y., K. Lyng, Y. X. Zhang, D. D. Rockey, and R. P. Morrison. 1992. Monoclonal antibodies define genus-specific, species-specific, and cross-reactive epitopes of the chlamydial 60-kilodalton heat shock protein (hsp60): specific immunodetection and purification of chlamydial hsp60. Infect. Immun. 60: 2288-2296.
    • (1992) Infect. Immun , vol.60 , pp. 2288-2296
    • Yuan, Y.1    Lyng, K.2    Zhang, Y.X.3    Rockey, D.D.4    Morrison, R.P.5
  • 89
    • 0034986059 scopus 로고    scopus 로고
    • Chlamydia pneumoniae infection of the central nervous system
    • Yucesan, C., and S. Sriram. 2001. Chlamydia pneumoniae infection of the central nervous system. Curr. Opin. Neurol. 14: 355-359.
    • (2001) Curr. Opin. Neurol , vol.14 , pp. 355-359
    • Yucesan, C.1    Sriram, S.2
  • 90
    • 0026622894 scopus 로고
    • Mechanism of C. trachomatis attachment to eukaryotic host cells
    • Zhang, J. P., and R. S. Stephens. 1992. Mechanism of C. trachomatis attachment to eukaryotic host cells. Cell 69: 861-869.
    • (1992) Cell , vol.69 , pp. 861-869
    • Zhang, J.P.1    Stephens, R.S.2
  • 91
    • 0038737428 scopus 로고    scopus 로고
    • Role of heat shock proteins in protection from and pathogenesis of infectious diseases
    • Zügel, U., and S. H. E. Kaufmann. 1999. Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin. Microbiol. Rev. 12: 19-39.
    • (1999) Clin. Microbiol. Rev , vol.12 , pp. 19-39
    • Zügel, U.1    Kaufmann, S.H.E.2


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