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Volumn 8, Issue 6, 2006, Pages 1579-1591

Ultrastructural analysis of chlamydial antigen-containing vesicles everting from the Chlamydia trachomatis inclusion

Author keywords

Antigen escape; Azithromycin; Chlamydia trachomatis; Inclusion membrane proteins (Inc); Vesicle formation

Indexed keywords

ANTIBIOTIC AGENT; AZITHROMYCIN; BACTERIAL ANTIGEN; HEAT SHOCK PROTEIN 60; ISOPROTEIN; MEMBRANE PROTEIN;

EID: 33745142612     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2006.01.018     Document Type: Article
Times cited : (31)

References (80)
  • 1
    • 0033129951 scopus 로고    scopus 로고
    • What is the minimally effective treatment for Chlamydia trachomatis infection? The compliance paradox
    • Schachter J. What is the minimally effective treatment for Chlamydia trachomatis infection? The compliance paradox. Sex. Transm. Dis. 26 (1999) 279-280
    • (1999) Sex. Transm. Dis. , vol.26 , pp. 279-280
    • Schachter, J.1
  • 2
    • 0037108382 scopus 로고    scopus 로고
    • CDC sexually transmitted diseases treatment guidelines
    • Workowski K.A., and Berman S.M. CDC sexually transmitted diseases treatment guidelines. Clin. Infect. Dis. 35 (2002) S135-S137
    • (2002) Clin. Infect. Dis. , vol.35
    • Workowski, K.A.1    Berman, S.M.2
  • 3
    • 0030961304 scopus 로고    scopus 로고
    • Delivery of azithromycin to Chlamydia trachomatis-infected polarized human endometrial epithelial cells by polymorphonuclear leucocytes
    • Paul T.R., Knight S.T., Raulston J.E., and Wyrick P.B. Delivery of azithromycin to Chlamydia trachomatis-infected polarized human endometrial epithelial cells by polymorphonuclear leucocytes. J. Antimicrob. Chemother. 39 (1997) 623-630
    • (1997) J. Antimicrob. Chemother. , vol.39 , pp. 623-630
    • Paul, T.R.1    Knight, S.T.2    Raulston, J.E.3    Wyrick, P.B.4
  • 4
    • 0028561956 scopus 로고
    • Pharmacokinetics of azithromycin and erythromycin in human endometrial epithelial cells and in cells infected with Chlamydia trachomatis
    • Raulston J.E. Pharmacokinetics of azithromycin and erythromycin in human endometrial epithelial cells and in cells infected with Chlamydia trachomatis. J. Antimicrob. Chemother. 34 (1994) 765-776
    • (1994) J. Antimicrob. Chemother. , vol.34 , pp. 765-776
    • Raulston, J.E.1
  • 5
    • 0026731756 scopus 로고
    • Azithromycin-induced block of elementary body formation in Chlamydia trachomatis
    • Engel J.N. Azithromycin-induced block of elementary body formation in Chlamydia trachomatis. Antimicrob. Agents Chemother. 36 (1992) 2304-2309
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 2304-2309
    • Engel, J.N.1
  • 6
    • 0028046568 scopus 로고
    • Effect of clinically relevant culture conditions on antimicrobial susceptibility of Chlamydia trachomatis
    • Wyrick P.B., Davis C.H., Raulston J.E., Knight S.T., and Choong J. Effect of clinically relevant culture conditions on antimicrobial susceptibility of Chlamydia trachomatis. Clin. Infect. Dis. 19 (1994) 931-936
    • (1994) Clin. Infect. Dis. , vol.19 , pp. 931-936
    • Wyrick, P.B.1    Davis, C.H.2    Raulston, J.E.3    Knight, S.T.4    Choong, J.5
  • 7
    • 0024336748 scopus 로고
    • Interaction of azithromycin and human phagocytic cells. Uptake of the antibiotic and the effect on the survival of ingested bacteria in phagocytes
    • Wildfeuer A., Laufen H., Muller-Wening D., and Haferkamp O. Interaction of azithromycin and human phagocytic cells. Uptake of the antibiotic and the effect on the survival of ingested bacteria in phagocytes. Arzneimittelforschung 39 (1989) 755-758
    • (1989) Arzneimittelforschung , vol.39 , pp. 755-758
    • Wildfeuer, A.1    Laufen, H.2    Muller-Wening, D.3    Haferkamp, O.4
  • 8
    • 0026502163 scopus 로고
    • In vitro evaluation of activities of azithromycin, erythromycin, and tetracycline against Chlamydia trachomatis and Chlamydia pneumoniae
    • Welsh L.E., Gaydos C.A., and Quinn T.C. In vitro evaluation of activities of azithromycin, erythromycin, and tetracycline against Chlamydia trachomatis and Chlamydia pneumoniae. Antimicrob. Agents Chemother. 36 (1992) 291-294
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 291-294
    • Welsh, L.E.1    Gaydos, C.A.2    Quinn, T.C.3
  • 9
    • 0027479138 scopus 로고
    • In-vitro activity of azithromycin on Chlamydia trachomatis infected, polarized human endometrial epithelial cells
    • Wyrick P.B., Davis C.H., Knight S.T., and Choong J. In-vitro activity of azithromycin on Chlamydia trachomatis infected, polarized human endometrial epithelial cells. J. Antimicrob. Chemother. 31 (1993) 139-150
    • (1993) J. Antimicrob. Chemother. , vol.31 , pp. 139-150
    • Wyrick, P.B.1    Davis, C.H.2    Knight, S.T.3    Choong, J.4
  • 11
    • 0025765319 scopus 로고
    • The role of azalide antibiotics in the treatment of Chlamydia
    • Johnson R.B. The role of azalide antibiotics in the treatment of Chlamydia. Am. J. Obstet. Gynecol. 164 (1991) 1794-1796
    • (1991) Am. J. Obstet. Gynecol. , vol.164 , pp. 1794-1796
    • Johnson, R.B.1
  • 12
    • 0026778726 scopus 로고
    • A controlled trial of a single dose of azithromycin for the treatment of chlamydial urethritis and cervicitis. The Azithromycin for Chlamydial Infections Study Group
    • Martin D.H., Mroczkowski T.F., Dalu Z.A., McCarty J., Jones R.B., Hopkins S.J., and Johnson R.B. A controlled trial of a single dose of azithromycin for the treatment of chlamydial urethritis and cervicitis. The Azithromycin for Chlamydial Infections Study Group. N. Engl. J. Med. 327 (1992) 921-925
    • (1992) N. Engl. J. Med. , vol.327 , pp. 921-925
    • Martin, D.H.1    Mroczkowski, T.F.2    Dalu, Z.A.3    McCarty, J.4    Jones, R.B.5    Hopkins, S.J.6    Johnson, R.B.7
  • 13
    • 0032900971 scopus 로고    scopus 로고
    • Persistent chlamydial envelope antigens in antibiotic-exposed infected cells trigger neutrophil chemotaxis
    • Wyrick P.B., Knight S.T., Paul T.R., Rank R.G., and Barbier C.S. Persistent chlamydial envelope antigens in antibiotic-exposed infected cells trigger neutrophil chemotaxis. J. Infect. Dis. 179 (1999) 954-966
    • (1999) J. Infect. Dis. , vol.179 , pp. 954-966
    • Wyrick, P.B.1    Knight, S.T.2    Paul, T.R.3    Rank, R.G.4    Barbier, C.S.5
  • 14
    • 4844226351 scopus 로고    scopus 로고
    • Chlamydia and apoptosis: life and death decisions of an intracellular pathogen
    • Byrne G.I., and Ojcius D.M. Chlamydia and apoptosis: life and death decisions of an intracellular pathogen. Nat. Rev. Microbiol. 2 (2004) 802-808
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 802-808
    • Byrne, G.I.1    Ojcius, D.M.2
  • 15
    • 0027952283 scopus 로고
    • Chlamydia trachomatis antigens on the surface of infected human endometrial epithelial cells
    • Wyrick P., Choong J., Knight S., Goyeau D., Stuart E.S., and Macdonald A. Chlamydia trachomatis antigens on the surface of infected human endometrial epithelial cells. Immun. Infect. Dis. 4 (1994) 131-141
    • (1994) Immun. Infect. Dis. , vol.4 , pp. 131-141
    • Wyrick, P.1    Choong, J.2    Knight, S.3    Goyeau, D.4    Stuart, E.S.5    Macdonald, A.6
  • 16
    • 0035896736 scopus 로고    scopus 로고
    • Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors
    • Zhong G., Fan P., Ji H., Dong F., and Huang Y. Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors. J. Exp. Med. 193 (2001) 935-942
    • (2001) J. Exp. Med. , vol.193 , pp. 935-942
    • Zhong, G.1    Fan, P.2    Ji, H.3    Dong, F.4    Huang, Y.5
  • 17
    • 0041476085 scopus 로고    scopus 로고
    • Expression and translocation of chlamydial protease during acute and persistent infection of the epithelial HEp-2 cells with Chlamydophila (Chlamydia) pneumoniae
    • Heuer D., Brinkmann V., Meyer T.F., and Szczepek A.J. Expression and translocation of chlamydial protease during acute and persistent infection of the epithelial HEp-2 cells with Chlamydophila (Chlamydia) pneumoniae. Cell. Microbiol. 5 (2003) 315-322
    • (2003) Cell. Microbiol. , vol.5 , pp. 315-322
    • Heuer, D.1    Brinkmann, V.2    Meyer, T.F.3    Szczepek, A.J.4
  • 18
    • 20844434204 scopus 로고    scopus 로고
    • Significant reduction in inflammatory response in the macaque model of chlamydial pelvic inflammatory disease with azithromycin treatment
    • Patton D.L., Sweeney Y.T.C., and Stamm W.E. Significant reduction in inflammatory response in the macaque model of chlamydial pelvic inflammatory disease with azithromycin treatment. J. Infect. Dis. 192 (2005) 129-135
    • (2005) J. Infect. Dis. , vol.192 , pp. 129-135
    • Patton, D.L.1    Sweeney, Y.T.C.2    Stamm, W.E.3
  • 19
    • 0036263421 scopus 로고    scopus 로고
    • Immunity to murine chlamydial genital infection
    • Morrison R.P., and Caldwell H.D. Immunity to murine chlamydial genital infection. Infect. Immun. 70 (2002) 2741-2751
    • (2002) Infect. Immun. , vol.70 , pp. 2741-2751
    • Morrison, R.P.1    Caldwell, H.D.2
  • 20
    • 33745155390 scopus 로고    scopus 로고
    • Vaccination with the Chlamydia trachomatis (CT) major outer membrane protein (MOMP) can induce protection against a genital challenge
    • Deak J. (Ed), Pauker Nyomdaipari Kft, Budapest, Hungary
    • Pal S., Peterson E., and de la Maza L. Vaccination with the Chlamydia trachomatis (CT) major outer membrane protein (MOMP) can induce protection against a genital challenge. In: Deak J. (Ed). Proceedings: Fifth Meeting of the European Society for Chlamydia Research (2004), Pauker Nyomdaipari Kft, Budapest, Hungary 394
    • (2004) Proceedings: Fifth Meeting of the European Society for Chlamydia Research , pp. 394
    • Pal, S.1    Peterson, E.2    de la Maza, L.3
  • 21
    • 0037318057 scopus 로고    scopus 로고
    • Endotoxic activity and chemical structure of lipopolysaccharides from Chlamydia trachomatis serotypes E and L2 and Chlamydophila psittaci 6BC
    • Heine H., Muller-Loennies S., Brade L., Lindner B., and Brade H. Endotoxic activity and chemical structure of lipopolysaccharides from Chlamydia trachomatis serotypes E and L2 and Chlamydophila psittaci 6BC. Eur. J. Biochem. 270 (2003) 440-450
    • (2003) Eur. J. Biochem. , vol.270 , pp. 440-450
    • Heine, H.1    Muller-Loennies, S.2    Brade, L.3    Lindner, B.4    Brade, H.5
  • 22
    • 0024468050 scopus 로고
    • Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein
    • Morrison R.P., Belland R.J., Lyng K., and Caldwell H.D. Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein. J. Exp. Med. 170 (1989) 1271-1283
    • (1989) J. Exp. Med. , vol.170 , pp. 1271-1283
    • Morrison, R.P.1    Belland, R.J.2    Lyng, K.3    Caldwell, H.D.4
  • 23
    • 0025001399 scopus 로고
    • Differential human serologic response to two 60,000 molecular weight Chlamydia trachomatis antigens
    • Wagar E.A., Schachter J., Bavoil P., and Stephens R.S. Differential human serologic response to two 60,000 molecular weight Chlamydia trachomatis antigens. J. Infect. Dis. 162 (1990) 922-927
    • (1990) J. Infect. Dis. , vol.162 , pp. 922-927
    • Wagar, E.A.1    Schachter, J.2    Bavoil, P.3    Stephens, R.S.4
  • 24
    • 0028032538 scopus 로고
    • Chlamydia trachomatis antigens: role in immunity and pathogenesis
    • Brunham R.C., and Peeling R.W. Chlamydia trachomatis antigens: role in immunity and pathogenesis. Infect. Agents. Dis. 3 (1994) 218-233
    • (1994) Infect. Agents. Dis. , vol.3 , pp. 218-233
    • Brunham, R.C.1    Peeling, R.W.2
  • 25
    • 0029160847 scopus 로고
    • Serologic responses of infertile women to the 60-kd chlamydial heat shock protein (hsp60)
    • Arno J.N., Yuan Y., Cleary R.E., and Morrison R.P. Serologic responses of infertile women to the 60-kd chlamydial heat shock protein (hsp60). Fertil. Steril. 64 (1995) 730-735
    • (1995) Fertil. Steril. , vol.64 , pp. 730-735
    • Arno, J.N.1    Yuan, Y.2    Cleary, R.E.3    Morrison, R.P.4
  • 26
    • 0031036415 scopus 로고    scopus 로고
    • The presence of serum antibody to the chlamydial heat shock protein (CHSP60) as a diagnostic test for tubal factor infertility
    • Claman P., Honey L., Peeling R.W., Jessamine P., and Toye B. The presence of serum antibody to the chlamydial heat shock protein (CHSP60) as a diagnostic test for tubal factor infertility. Fertil. Steril. 67 (1997) 501-504
    • (1997) Fertil. Steril. , vol.67 , pp. 501-504
    • Claman, P.1    Honey, L.2    Peeling, R.W.3    Jessamine, P.4    Toye, B.5
  • 28
    • 0842326271 scopus 로고    scopus 로고
    • Heat shock protein 60 is the major antigen which stimulates delayed-type hypersensitivity reaction in the macaque model of Chlamydia trachomatis salpingitis
    • Lichtenwalner A.B., Patton D.L., Van Voorhis W.C., Sweeney Y.T., and Kuo C.C. Heat shock protein 60 is the major antigen which stimulates delayed-type hypersensitivity reaction in the macaque model of Chlamydia trachomatis salpingitis. Infect. Immun. 72 (2004) 1159-1161
    • (2004) Infect. Immun. , vol.72 , pp. 1159-1161
    • Lichtenwalner, A.B.1    Patton, D.L.2    Van Voorhis, W.C.3    Sweeney, Y.T.4    Kuo, C.C.5
  • 29
    • 0037233027 scopus 로고    scopus 로고
    • The cellular paradigm of chlamydial pathogenesis
    • Stephens R.S. The cellular paradigm of chlamydial pathogenesis. Trends Microbiol. 11 (2003) 44-51
    • (2003) Trends Microbiol. , vol.11 , pp. 44-51
    • Stephens, R.S.1
  • 30
    • 0036568789 scopus 로고    scopus 로고
    • Reduced levels of gamma-interferon secretion in response to chlamydial 60 kDa heat shock protein amongst women with pelvic inflammatory disease and a history of repeated Chlamydia trachomatis infections
    • Debattista J., Timms P., and Allan J. Reduced levels of gamma-interferon secretion in response to chlamydial 60 kDa heat shock protein amongst women with pelvic inflammatory disease and a history of repeated Chlamydia trachomatis infections. Immunol. Lett. 81 (2002) 205-210
    • (2002) Immunol. Lett. , vol.81 , pp. 205-210
    • Debattista, J.1    Timms, P.2    Allan, J.3
  • 32
    • 0344393674 scopus 로고    scopus 로고
    • Differential expression of three Chlamydia trachomatis hsp60-encoding genes in active vs. persistent infections
    • Gerard H.C., Whittum-Hudson J.A., Schumacher H.R., and Hudson A.P. Differential expression of three Chlamydia trachomatis hsp60-encoding genes in active vs. persistent infections. Microb. Pathog. 36 (2004) 35-39
    • (2004) Microb. Pathog. , vol.36 , pp. 35-39
    • Gerard, H.C.1    Whittum-Hudson, J.A.2    Schumacher, H.R.3    Hudson, A.P.4
  • 33
    • 0026714747 scopus 로고
    • Eukaryotic cells grown on microcarrier beads offer a cost-efficient way to propagate Chlamydia trachomatis
    • Tam J.E., Knight S.T., Davis C.H., and Wyrick P.B. Eukaryotic cells grown on microcarrier beads offer a cost-efficient way to propagate Chlamydia trachomatis. Biotechniques 13 (1992) 374-378
    • (1992) Biotechniques , vol.13 , pp. 374-378
    • Tam, J.E.1    Knight, S.T.2    Davis, C.H.3    Wyrick, P.B.4
  • 34
    • 0029920511 scopus 로고    scopus 로고
    • Accelerated development of genital Chlamydia trachomatis serovar E in McCoy cells grown on microcarrier beads
    • Wyrick P.B., Gerbig Jr. D.G., Knight S.T., and Raulston J.E. Accelerated development of genital Chlamydia trachomatis serovar E in McCoy cells grown on microcarrier beads. Microb. Pathog. 20 (1996) 31-40
    • (1996) Microb. Pathog. , vol.20 , pp. 31-40
    • Wyrick, P.B.1    Gerbig Jr., D.G.2    Knight, S.T.3    Raulston, J.E.4
  • 35
    • 0027431484 scopus 로고
    • An in vitro human epithelial cell culture system for studying the pathogenesis of Chlamydia trachomatis
    • Wyrick P.B., Davis C.H., Knight S.T., Choong J., Raulston J.E., and Schramm N. An in vitro human epithelial cell culture system for studying the pathogenesis of Chlamydia trachomatis. Sex. Transm. Dis. 20 (1993) 248-256
    • (1993) Sex. Transm. Dis. , vol.20 , pp. 248-256
    • Wyrick, P.B.1    Davis, C.H.2    Knight, S.T.3    Choong, J.4    Raulston, J.E.5    Schramm, N.6
  • 36
    • 0033854130 scopus 로고    scopus 로고
    • Chlamydial infection of polarized HeLa cells induces PMN chemotaxis but the cytokine profile varies between disseminating and non-disseminating strains
    • Dessus-Babus S., Knight S.T., and Wyrick P.B. Chlamydial infection of polarized HeLa cells induces PMN chemotaxis but the cytokine profile varies between disseminating and non-disseminating strains. Cell. Microbiol. 2 (2000) 317-327
    • (2000) Cell. Microbiol. , vol.2 , pp. 317-327
    • Dessus-Babus, S.1    Knight, S.T.2    Wyrick, P.B.3
  • 37
    • 0031863420 scopus 로고    scopus 로고
    • Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane
    • Bannantine J.P., Rockey D.D., and Hackstadt T. Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane. Mol. Microbiol. 28 (1998) 1017-1026
    • (1998) Mol. Microbiol. , vol.28 , pp. 1017-1026
    • Bannantine, J.P.1    Rockey, D.D.2    Hackstadt, T.3
  • 38
    • 0031796118 scopus 로고    scopus 로고
    • Chlamydia trachomatis IncA is localized to the inclusion membrane and is recognized by antisera from infected humans and primates
    • Bannantine J.P., Stamm W.E., Suchland R.J., and Rockey D.D. Chlamydia trachomatis IncA is localized to the inclusion membrane and is recognized by antisera from infected humans and primates. Infect. Immun. 66 (1998) 6017-6021
    • (1998) Infect. Immun. , vol.66 , pp. 6017-6021
    • Bannantine, J.P.1    Stamm, W.E.2    Suchland, R.J.3    Rockey, D.D.4
  • 39
    • 0033188168 scopus 로고    scopus 로고
    • The Chlamydia trachomatis IncA protein is required for homotypic vesicle fusion
    • Hackstadt T., Scidmore-Carlson M.A., Shaw E.I., and Fischer E.R. The Chlamydia trachomatis IncA protein is required for homotypic vesicle fusion. Cell. Microbiol. 1 (1999) 119-130
    • (1999) Cell. Microbiol. , vol.1 , pp. 119-130
    • Hackstadt, T.1    Scidmore-Carlson, M.A.2    Shaw, E.I.3    Fischer, E.R.4
  • 40
    • 0032775116 scopus 로고    scopus 로고
    • Identification and characterization of a Chlamydia trachomatis early operon encoding four novel inclusion membrane proteins
    • Scidmore-Carlson M.A., Shaw E.I., Dooley C.A., Fischer E.R., and Hackstadt T. Identification and characterization of a Chlamydia trachomatis early operon encoding four novel inclusion membrane proteins. Mol. Microbiol. 33 (1999) 753-765
    • (1999) Mol. Microbiol. , vol.33 , pp. 753-765
    • Scidmore-Carlson, M.A.1    Shaw, E.I.2    Dooley, C.A.3    Fischer, E.R.4    Hackstadt, T.5
  • 41
    • 0034001114 scopus 로고    scopus 로고
    • A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane
    • Bannantine J.P., Griffiths R.S., Viratyosin W., Brown W.J., and Rockey D.D. A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane. Cell. Microbiol. 2 (2000) 35-47
    • (2000) Cell. Microbiol. , vol.2 , pp. 35-47
    • Bannantine, J.P.1    Griffiths, R.S.2    Viratyosin, W.3    Brown, W.J.4    Rockey, D.D.5
  • 43
    • 0036441158 scopus 로고    scopus 로고
    • The chlamydial inclusion: escape from the endocytic pathway
    • Fields K.A., and Hackstadt T. The chlamydial inclusion: escape from the endocytic pathway. Annu. Rev. Cell. Dev. Biol. 18 (2002) 221-245
    • (2002) Annu. Rev. Cell. Dev. Biol. , vol.18 , pp. 221-245
    • Fields, K.A.1    Hackstadt, T.2
  • 44
    • 0037974695 scopus 로고    scopus 로고
    • Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion
    • Carabeo R.A., Mead D.J., and Hackstadt T. Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion. Proc. Natl. Acad. Sci. USA 100 (2003) 6771-6776
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6771-6776
    • Carabeo, R.A.1    Mead, D.J.2    Hackstadt, T.3
  • 45
    • 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., Paul T.R., Knight S.T., and Wyrick P.B. Localization of Chlamydia trachomatis heat shock proteins 60 and 70 during infection of a human endometrial epithelial cell line in vitro. Infect. Immun. 66 (1998) 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
  • 46
    • 0019803190 scopus 로고
    • Localization of chlamydial group Antigen in McCoy cell monolayers infected with Chlamydia trachomatis or Chlamydia psittaci
    • Richmond S.J., and Stirling P. Localization of chlamydial group Antigen in McCoy cell monolayers infected with Chlamydia trachomatis or Chlamydia psittaci. Infect. Immun. 34 (1981) 561-570
    • (1981) Infect. Immun. , vol.34 , pp. 561-570
    • Richmond, S.J.1    Stirling, P.2
  • 47
    • 0024382808 scopus 로고
    • Accumulation of chlamydial lipopolysaccharide antigen in the plasma membranes of infected cells
    • Karimi S.T., Schloemer R.H., and Wilde III C.E. Accumulation of chlamydial lipopolysaccharide antigen in the plasma membranes of infected cells. Infect. Immun. 57 (1989) 1780-1785
    • (1989) Infect. Immun. , vol.57 , pp. 1780-1785
    • Karimi, S.T.1    Schloemer, R.H.2    Wilde III, C.E.3
  • 48
    • 0013537953 scopus 로고
    • Cell surface alterations during chlamydial infection
    • Leive L., and Bonventre P.F. (Eds), ASM Press, Washington, DC, USA
    • Wilde C.E., Karimi S., and Haak R.A. Cell surface alterations during chlamydial infection. In: Leive L., and Bonventre P.F. (Eds). Microbiology-1986 (1986), ASM Press, Washington, DC, USA 96-98
    • (1986) Microbiology-1986 , pp. 96-98
    • Wilde, C.E.1    Karimi, S.2    Haak, R.A.3
  • 49
    • 0014702522 scopus 로고
    • Electron microscopic observations on the effects of penicillin on the morphology of Chlamydia psittaci
    • Matsumoto A., and Manire G.P. Electron microscopic observations on the effects of penicillin on the morphology of Chlamydia psittaci. J. Bacteriol. 101 (1970) 278-285
    • (1970) J. Bacteriol. , vol.101 , pp. 278-285
    • Matsumoto, A.1    Manire, G.P.2
  • 50
    • 0036786504 scopus 로고    scopus 로고
    • Chlamydial antigens colocalize within IncA-laden fibers extending from the inclusion membrane into the host cytosol
    • Brown W.J., Skeiky Y.A., Probst P., and Rockey D.D. Chlamydial antigens colocalize within IncA-laden fibers extending from the inclusion membrane into the host cytosol. Infect. Immun. 70 (2002) 5860-5864
    • (2002) Infect. Immun. , vol.70 , pp. 5860-5864
    • Brown, W.J.1    Skeiky, Y.A.2    Probst, P.3    Rockey, D.D.4
  • 51
    • 0024563822 scopus 로고
    • Export and intercellular transfer of DNA via membrane blebs of Neisseria gonorrhoeae
    • Dorward D.W., Garon C.F., and Judd R.C. Export and intercellular transfer of DNA via membrane blebs of Neisseria gonorrhoeae. J. Bacteriol. 171 (1989) 2499-2505
    • (1989) J. Bacteriol. , vol.171 , pp. 2499-2505
    • Dorward, D.W.1    Garon, C.F.2    Judd, R.C.3
  • 52
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge T.J. Structures of gram-negative cell walls and their derived membrane vesicles. J. Bacteriol. 181 (1999) 4725-4733
    • (1999) J. Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 53
    • 0032959537 scopus 로고    scopus 로고
    • Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7
    • Kolling G.L., and Matthews K.R. Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7. Appl. Environ. Microbiol. 65 (1999) 1843-1848
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1843-1848
    • Kolling, G.L.1    Matthews, K.R.2
  • 54
    • 0346457133 scopus 로고    scopus 로고
    • Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles
    • Kesty N.C., and Kuehn M.J. Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles. J. Biol. Chem. 279 (2004) 2069-2076
    • (2004) J. Biol. Chem. , vol.279 , pp. 2069-2076
    • Kesty, N.C.1    Kuehn, M.J.2
  • 55
    • 10644226878 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty N.C., Mason K.M., Reedy M., Miller S.E., and Kuehn M.J. Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells. EMBO J. 23 (2004) 4538-4549
    • (2004) EMBO J. , vol.23 , pp. 4538-4549
    • Kesty, N.C.1    Mason, K.M.2    Reedy, M.3    Miller, S.E.4    Kuehn, M.J.5
  • 56
    • 8744275514 scopus 로고    scopus 로고
    • Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae: oligomerization of IncA mediates interaction between facing membranes
    • Delevoye C., Nilges M., Dautry-Varsat A., and Subtil A. Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae: oligomerization of IncA mediates interaction between facing membranes. J. Biol. Chem. 279 (2004) 46896-46906
    • (2004) J. Biol. Chem. , vol.279 , pp. 46896-46906
    • Delevoye, C.1    Nilges, M.2    Dautry-Varsat, A.3    Subtil, A.4
  • 57
    • 0033985761 scopus 로고    scopus 로고
    • Isolates of Chlamydia trachomatis that occupy nonfusogenic inclusions lack IncA, a protein localized to the inclusion membrane
    • Suchland R.J., Rockey D.D., Bannantine J.P., and Stamm W.E. Isolates of Chlamydia trachomatis that occupy nonfusogenic inclusions lack IncA, a protein localized to the inclusion membrane. Infect. Immun. 68 (2000) 360-367
    • (2000) Infect. Immun. , vol.68 , pp. 360-367
    • Suchland, R.J.1    Rockey, D.D.2    Bannantine, J.P.3    Stamm, W.E.4
  • 58
    • 0141669008 scopus 로고    scopus 로고
    • Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner
    • Rzomp K.A., Scholtes L.D., Briggs B.J., Whittaker G.R., and Scidmore M.A. Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner. Infect. Immun. 71 (2003) 5855-5870
    • (2003) Infect. Immun. , vol.71 , pp. 5855-5870
    • Rzomp, K.A.1    Scholtes, L.D.2    Briggs, B.J.3    Whittaker, G.R.4    Scidmore, M.A.5
  • 59
    • 0027939186 scopus 로고
    • Role for CD8+ T cells in antichlamydial immunity defined by Chlamydia-specific T-lymphocyte clones
    • Igietseme J.U., Magee D.M., Williams D.M., and Rank R.G. Role for CD8+ T cells in antichlamydial immunity defined by Chlamydia-specific T-lymphocyte clones. Infect. Immun. 62 (1994) 5195-5197
    • (1994) Infect. Immun. , vol.62 , pp. 5195-5197
    • Igietseme, J.U.1    Magee, D.M.2    Williams, D.M.3    Rank, R.G.4
  • 61
    • 0142210412 scopus 로고    scopus 로고
    • An inclusion membrane protein from Chlamydia trachomatis enters the MHC class I pathway and stimulates a CD8+ T cell response
    • Starnbach M.N., Loomis W.P., Ovendale P., Regan D., Hess B., Alderson M.R., and Fling S.P. An inclusion membrane protein from Chlamydia trachomatis enters the MHC class I pathway and stimulates a CD8+ T cell response. J. Immunol. 171 (2003) 4742-4749
    • (2003) J. Immunol. , vol.171 , pp. 4742-4749
    • Starnbach, M.N.1    Loomis, W.P.2    Ovendale, P.3    Regan, D.4    Hess, B.5    Alderson, M.R.6    Fling, S.P.7
  • 62
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • Kovacsovics-Bankowski M., and Rock K.L. A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules. Science 267 (1995) 243-246
    • (1995) Science , vol.267 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.2
  • 66
    • 0041920932 scopus 로고    scopus 로고
    • Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum
    • Celli J., de Chastellier C., Franchini D.M., Pizarro-Cerda J., Moreno E., and Gorvel J.P. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J. Exp. Med. 198 (2003) 545-556
    • (2003) J. Exp. Med. , vol.198 , pp. 545-556
    • Celli, J.1    de Chastellier, C.2    Franchini, D.M.3    Pizarro-Cerda, J.4    Moreno, E.5    Gorvel, J.P.6
  • 67
    • 0030664962 scopus 로고    scopus 로고
    • Host cell phospholipids are trafficked to and then modified by Chlamydia trachomatis
    • Wylie J.L., Hatch G.M., and McClarty G. Host cell phospholipids are trafficked to and then modified by Chlamydia trachomatis. J. Bacteriol. 179 (1997) 7233-7242
    • (1997) J. Bacteriol. , vol.179 , pp. 7233-7242
    • Wylie, J.L.1    Hatch, G.M.2    McClarty, G.3
  • 68
    • 0034193165 scopus 로고    scopus 로고
    • Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in Chlamydia-infected cells
    • Zhong G., Liu L., Fan T., Fan P., and Ji H. Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in Chlamydia-infected cells. J. Exp. Med. 191 (2000) 1525-1534
    • (2000) J. Exp. Med. , vol.191 , pp. 1525-1534
    • Zhong, G.1    Liu, L.2    Fan, T.3    Fan, P.4    Ji, H.5
  • 70
    • 0031803740 scopus 로고    scopus 로고
    • Type III secretion in Chlamydia: a case of deja vu?
    • Bavoil P.M., and Hsia R.C. Type III secretion in Chlamydia: a case of deja vu?. Mol. Microbiol. 28 (1998) 860-862
    • (1998) Mol. Microbiol. , vol.28 , pp. 860-862
    • Bavoil, P.M.1    Hsia, R.C.2
  • 71
    • 0034533953 scopus 로고    scopus 로고
    • Evidence for the secretion of Chlamydia trachomatis CopN by a type III secretion mechanism
    • Fields K.A., and Hackstadt T. Evidence for the secretion of Chlamydia trachomatis CopN by a type III secretion mechanism. Mol. Microbiol. 38 (2000) 1048-1060
    • (2000) Mol. Microbiol. , vol.38 , pp. 1048-1060
    • Fields, K.A.1    Hackstadt, T.2
  • 72
    • 0038011417 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion: evidence for a functional apparatus during early-cycle development
    • Fields K.A., Mead D.J., Dooley C.A., and Hackstadt T. Chlamydia trachomatis type III secretion: evidence for a functional apparatus during early-cycle development. Mol. Microbiol. 48 (2003) 671-683
    • (2003) Mol. Microbiol. , vol.48 , pp. 671-683
    • Fields, K.A.1    Mead, D.J.2    Dooley, C.A.3    Hackstadt, T.4
  • 74
    • 0035131373 scopus 로고    scopus 로고
    • Secretion of predicted Inc proteins of Chlamydia pneumoniae by a heterologous type III machinery
    • Subtil A., Parsot C., and Dautry-Varsat A. Secretion of predicted Inc proteins of Chlamydia pneumoniae by a heterologous type III machinery. Mol. Microbiol. 39 (2001) 792-800
    • (2001) Mol. Microbiol. , vol.39 , pp. 792-800
    • Subtil, A.1    Parsot, C.2    Dautry-Varsat, A.3
  • 75
    • 12844268208 scopus 로고    scopus 로고
    • The Salmonella enterica serovar typhimurium-encoded type III secretion systems can translocate Chlamydia trachomatis proteins into the cytosol of host cells
    • Ho T.D., and Starnbach M.N. The Salmonella enterica serovar typhimurium-encoded type III secretion systems can translocate Chlamydia trachomatis proteins into the cytosol of host cells. Infect. Immun. 73 (2005) 905-911
    • (2005) Infect. Immun. , vol.73 , pp. 905-911
    • Ho, T.D.1    Starnbach, M.N.2
  • 76
    • 0002139713 scopus 로고
    • Structural characteristics of chlamydial bodies
    • Barron A.L. (Ed), CRC Press, Boca Raton, FL, USA
    • Matsumoto A. Structural characteristics of chlamydial bodies. In: Barron A.L. (Ed). Microbiology of Chlamydia (1988), CRC Press, Boca Raton, FL, USA 21-45
    • (1988) Microbiology of Chlamydia , pp. 21-45
    • Matsumoto, A.1
  • 77
    • 0035578719 scopus 로고    scopus 로고
    • Polymorphic proteins of Chlamydia spp.-autotransporters beyond the Proteobacteria
    • Henderson I.R., and Lam A.C. Polymorphic proteins of Chlamydia spp.-autotransporters beyond the Proteobacteria. Trends Microbiol. 9 (2001) 573-578
    • (2001) Trends Microbiol. , vol.9 , pp. 573-578
    • Henderson, I.R.1    Lam, A.C.2
  • 78
    • 0032037664 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the genes coding for the highly immunogenic cluster of 90-kilodalton envelope proteins from the Chlamydia psittaci subtype that causes abortion in sheep
    • Longbottom D., Russell M., Dunbar S.M., Jones G.E., and Herring A.J. Molecular cloning and characterization of the genes coding for the highly immunogenic cluster of 90-kilodalton envelope proteins from the Chlamydia psittaci subtype that causes abortion in sheep. Infect. Immun. 66 (1998) 1317-1324
    • (1998) Infect. Immun. , vol.66 , pp. 1317-1324
    • Longbottom, D.1    Russell, M.2    Dunbar, S.M.3    Jones, G.E.4    Herring, A.J.5
  • 79
    • 33745178099 scopus 로고    scopus 로고
    • Chlamydia structure-A molecular approach to understand the structure of Chlamydia
    • Schacter J., Christiansen G., Clarke I.N., Hammerschlag M.R., Kaltenboeck B., Kuo C.C., Rank R.G., Ridgway G.L., Saikku P., Stamm W.E., Stephens R.S., Summersgill J.T., Timms P., and Wyrick P.B. (Eds), GRAFMAT Basim ve Reklam Sanayi Tic. Ltd. Sti., Basim Yeri
    • Christiansen G., and Birkelund S. Chlamydia structure-A molecular approach to understand the structure of Chlamydia. In: Schacter J., Christiansen G., Clarke I.N., Hammerschlag M.R., Kaltenboeck B., Kuo C.C., Rank R.G., Ridgway G.L., Saikku P., Stamm W.E., Stephens R.S., Summersgill J.T., Timms P., and Wyrick P.B. (Eds). Chlamydial Infections-Proceedings of the Tenth International Symposium on Human Chlamydial Infections (2002), GRAFMAT Basim ve Reklam Sanayi Tic. Ltd. Sti., Basim Yeri 537-546
    • (2002) Chlamydial Infections-Proceedings of the Tenth International Symposium on Human Chlamydial Infections , pp. 537-546
    • Christiansen, G.1    Birkelund, S.2
  • 80
    • 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., Brinkmann V., Jungblut P.R., Meyer T.F., and Szczepek A.J. 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 (2004) 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


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