메뉴 건너뛰기




Volumn 14, Issue 6, 2016, Pages 385-400

Chlamydia cell biology and pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; APOLIPOPROTEIN E4; BACTERIAL PROTEIN; BACTERIUM LIPOPOLYSACCHARIDE; EPHRIN RECEPTOR A2; FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR RECEPTOR; MYELOID DIFFERENTIATION FACTOR 88; PHOSPHOPROTEIN; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; PROTEOME; RAB PROTEIN; SNARE PROTEIN; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TRANSCRIPTOME; TRANSLOCATED ACTIN RECRUITING PHOSPHOPROTEIN; UNCLASSIFIED DRUG; TYPE V SECRETION SYSTEM;

EID: 84964240913     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro.2016.30     Document Type: Review
Times cited : (451)

References (176)
  • 1
    • 84905105696 scopus 로고    scopus 로고
    • Chlamydia genomics: Providing novel insights into chlamydial biology
    • Bachmann, N. L., Polkinghorne, A. & Timms, P. Chlamydia genomics: providing novel insights into chlamydial biology. Trends Microbiol. 22, 464-472 (2014).
    • (2014) Trends Microbiol. , vol.22 , pp. 464-472
    • Bachmann, N.L.1    Polkinghorne, A.2    Timms, P.3
  • 3
  • 5
    • 84901019331 scopus 로고    scopus 로고
    • Lymphogranuloma venereum among men who have sex with men. An epidemiological and clinical review
    • de Vrieze, N. H. & de Vries, H. J. Lymphogranuloma venereum among men who have sex with men. An epidemiological and clinical review. Expert Rev. Anti Infect. Ther. 12, 697-704 (2014).
    • (2014) Expert Rev. Anti Infect. Ther. , vol.12 , pp. 697-704
    • De Vrieze, N.H.1    De Vries, H.J.2
  • 8
    • 0032561496 scopus 로고    scopus 로고
    • Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis
    • Stephens, R. S. et al. Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis. Science 282, 754-759 (1998).
    • (1998) Science , vol.282 , pp. 754-759
    • Stephens, R.S.1
  • 10
    • 79959410785 scopus 로고    scopus 로고
    • The chlamydial type III secretion mechanism: Revealing cracks in a tough nut
    • Betts-Hampikian, H. J. & Fields, K. A. The chlamydial type III secretion mechanism: revealing cracks in a tough nut. Front. Microbiol. 1, 114 (2010).
    • (2010) Front. Microbiol. , vol.1 , pp. 114
    • Betts-Hampikian, H.J.1    Fields, K.A.2
  • 12
    • 84894242009 scopus 로고    scopus 로고
    • Reduced live organism recovery and lack of hydrosalpinx in mice infected with plasmid-free Chlamydia muridarum
    • Lei, L. et al. Reduced live organism recovery and lack of hydrosalpinx in mice infected with plasmid-free Chlamydia muridarum. Infect. Immun. 82, 983-992 (2014).
    • (2014) Infect. Immun. , vol.82 , pp. 983-992
    • Lei, L.1
  • 14
    • 84904066418 scopus 로고    scopus 로고
    • Chlamydial metabolism revisited: Interspecies metabolic variability and developmental stage-specific physiologic activities
    • Omsland, A., Sixt, B. S., Horn, M. & Hackstadt, T. Chlamydial metabolism revisited: interspecies metabolic variability and developmental stage-specific physiologic activities. FEMS Microbiol. Rev. 38, 779-801 (2014).
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 779-801
    • Omsland, A.1    Sixt, B.S.2    Horn, M.3    Hackstadt, T.4
  • 15
    • 82155175628 scopus 로고    scopus 로고
    • Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms
    • Saka, H. A. et al. Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms. Mol. Microbiol. 82, 1185-1203 (2011).
    • (2011) Mol. Microbiol. , vol.82 , pp. 1185-1203
    • Saka, H.A.1
  • 18
    • 84887927789 scopus 로고    scopus 로고
    • Modulation of host signaling and cellular responses by Chlamydia
    • Mehlitz, A. & Rudel, T. Modulation of host signaling and cellular responses by Chlamydia. Cell Commun. Signal. 11, 90 (2013).
    • (2013) Cell Commun. Signal. , vol.11 , pp. 90
    • Mehlitz, A.1    Rudel, T.2
  • 19
    • 84930981309 scopus 로고    scopus 로고
    • (eds Tan, M. & Bavoil, P. M.) ASM press
    • Tan, M. in Intracellular Pathogens 1: Chlamydiales Vol. 1 (eds Tan, M. & Bavoil, P. M.)149-169 (ASM press, 2012).
    • (2012) Intracellular Pathogens 1: Chlamydiales , vol.1 , pp. 149-169
    • Tan, M.1
  • 20
    • 84924838610 scopus 로고    scopus 로고
    • Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: An expanded role for Inc proteins
    • Moore, E. R. & Ouellette, S. P. Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: an expanded role for Inc proteins. Front. Cell. Infect. Microbiol. 4, 157 (2014).
    • (2014) Front. Cell. Infect. Microbiol. , vol.4 , pp. 157
    • Moore, E.R.1    Ouellette, S.P.2
  • 21
    • 84862539845 scopus 로고    scopus 로고
    • Lipid acquisition by intracellular Chlamydiae
    • Elwell, C. A. & Engel, J. N. Lipid acquisition by intracellular Chlamydiae. Cell. Microbiol. 14, 1010-1018 (2012).
    • (2012) Cell. Microbiol. , vol.14 , pp. 1010-1018
    • Elwell, C.A.1    Engel, J.N.2
  • 22
    • 84898603182 scopus 로고    scopus 로고
    • Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding
    • Barta, M. L. et al. Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding. PLoS ONE 9, e91760 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e91760
    • Barta, M.L.1
  • 23
    • 84930982118 scopus 로고    scopus 로고
    • The transcriptional repressor EUO regulates both subsets of Chlamydia late genes
    • Rosario, C. J., Hanson, B. R. & Tan, M. The transcriptional repressor EUO regulates both subsets of Chlamydia late genes. Mol. Microbiol. 94, 888-897 (2014).
    • (2014) Mol. Microbiol. , vol.94 , pp. 888-897
    • Rosario, C.J.1    Hanson, B.R.2    Tan, M.3
  • 24
    • 84957107109 scopus 로고    scopus 로고
    • 54 (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis
    • 54 (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis. Protein Sci. 24, 1617-1632 (2015).
    • (2015) Protein Sci. , vol.24 , pp. 1617-1632
    • Barta, M.L.1    Battaile, K.P.2    Lovell, S.3    Hefty, P.S.4
  • 25
    • 84944610231 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion proteins regulate transcription
    • Hanson, B. R., Slepenkin, A., Peterson, E. M. & Tan, M. Chlamydia trachomatis type III secretion proteins regulate transcription. J. Bacteriol. 197, 3238-3244 (2015).
    • (2015) J. Bacteriol. , vol.197 , pp. 3238-3244
    • Hanson, B.R.1    Slepenkin, A.2    Peterson, E.M.3    Tan, M.4
  • 26
    • 84947708703 scopus 로고    scopus 로고
    • Multipart chaperone-effector recognition in the type III secretion system of Chlamydia trachomatis
    • Shen, L. et al. Multipart chaperone-effector recognition in the type III secretion system of Chlamydia trachomatis. J. Biol. Chem. 290, 28141-28155 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 28141-28155
    • Shen, L.1
  • 28
    • 84881555972 scopus 로고    scopus 로고
    • Endosulfatases SULF1 and SULF2 limit Chlamydia muridarum infection
    • Kim, J. H. et al. Endosulfatases SULF1 and SULF2 limit Chlamydia muridarum infection. Cell. Microbiol. 15, 1560-1571 (2013).
    • (2013) Cell. Microbiol. , vol.15 , pp. 1560-1571
    • Kim, J.H.1
  • 29
    • 84862564468 scopus 로고    scopus 로고
    • Attachment of Chlamydia trachomatis L2 to host cells requires sulfation
    • Rosmarin, D. M. et al. Attachment of Chlamydia trachomatis L2 to host cells requires sulfation. Proc. Natl Acad. Sci. USA 109, 10059-10064 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 10059-10064
    • Rosmarin, D.M.1
  • 30
    • 77955073254 scopus 로고    scopus 로고
    • CFTR is required for cellular entry and internalization of Chlamydia trachomatis
    • Ajonuma, L. C. et al. CFTR is required for cellular entry and internalization of Chlamydia trachomatis. Cell Biol. Int. 34, 593-600 (2010).
    • (2010) Cell Biol. Int. , vol.34 , pp. 593-600
    • Ajonuma, L.C.1
  • 31
    • 84955063764 scopus 로고    scopus 로고
    • The Chlamydia trachomatis Ctad1 invasin exploits the human integrin β1 receptor for host cell entry
    • Stallmann, S. & Hegemann, J. H. The Chlamydia trachomatis Ctad1 invasin exploits the human integrin β1 receptor for host cell entry. Cell. Microbiol. http://dx.doi.org/10.1111/cmi.12549 (2015).
    • (2015) Cell. Microbiol
    • Stallmann, S.1    Hegemann, J.H.2
  • 32
    • 84906092332 scopus 로고    scopus 로고
    • All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species-specific function
    • Becker, E. & Hegemann, J. H. All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species-specific function. Microbiologyopen 3, 544-556 (2014).
    • (2014) Microbiologyopen , vol.3 , pp. 544-556
    • Becker, E.1    Hegemann, J.H.2
  • 33
    • 84876850984 scopus 로고    scopus 로고
    • The Chlamydia pneumoniae invasin protein Pmp21 recruits the EGF receptor for host cell entry
    • Molleken, K., Becker, E. & Hegemann, J. H. The Chlamydia pneumoniae invasin protein Pmp21 recruits the EGF receptor for host cell entry. PLoS Pathog. 9, e1003325 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003325
    • Molleken, K.1    Becker, E.2    Hegemann, J.H.3
  • 34
    • 42949086499 scopus 로고    scopus 로고
    • RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry
    • Elwell, C. A., Ceesay, A., Kim, J. H., Kalman, D. & Engel, J. N. RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. PLoS Pathog. 4, e1000021 (2008).
    • (2008) PLoS Pathog. , vol.4 , pp. e1000021
    • Elwell, C.A.1    Ceesay, A.2    Kim, J.H.3    Kalman, D.4    Engel, J.N.5
  • 35
    • 80055088874 scopus 로고    scopus 로고
    • Chlamydia trachomatis co-opts the FGF2 signaling pathway to enhance infection
    • Kim, J. H., Jiang, S., Elwell, C. A. & Engel, J. N. Chlamydia trachomatis co-opts the FGF2 signaling pathway to enhance infection. PLoS Pathog. 7, e1002285 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1002285
    • Kim, J.H.1    Jiang, S.2    Elwell, C.A.3    Engel, J.N.4
  • 36
    • 84929485971 scopus 로고    scopus 로고
    • EphrinA2 receptor (EphA2) is an invasion and intracellular signaling receptor for Chlamydia trachomatis
    • Subbarayal, P. et al. EphrinA2 receptor (EphA2) is an invasion and intracellular signaling receptor for Chlamydia trachomatis. PLoS Pathog. 11, e1004846 (2015).
    • (2015) PLoS Pathog. , vol.11 , pp. e1004846
    • Subbarayal, P.1
  • 37
    • 40749128778 scopus 로고    scopus 로고
    • Apolipoprotein E4 enhances attachment of Chlamydophila (Chlamydia) pneumoniae elementary bodies to host cells
    • Gerard, H. C., Fomicheva, E., Whittum-Hudson, J. A. & Hudson, A. P. Apolipoprotein E4 enhances attachment of Chlamydophila (Chlamydia) pneumoniae elementary bodies to host cells. Microb. Pathog. 44, 279-285 (2008).
    • (2008) Microb. Pathog. , vol.44 , pp. 279-285
    • Gerard, H.C.1    Fomicheva, E.2    Whittum-Hudson, J.A.3    Hudson, A.P.4
  • 38
    • 84957843455 scopus 로고    scopus 로고
    • A working model for the type III secretion mechanism in Chlamydia
    • Ferrell, J. C. & Fields, K. A. A working model for the type III secretion mechanism in Chlamydia. Microbes Infect. 18, 84-92 (2015).
    • (2015) Microbes Infect. , vol.18 , pp. 84-92
    • Ferrell, J.C.1    Fields, K.A.2
  • 39
    • 84908060953 scopus 로고    scopus 로고
    • Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography
    • Nans, A., Saibil, H. R. & Hayward, R. D. Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography. Cell. Microbiol. 16, 1457-1472 (2014).
    • (2014) Cell. Microbiol. , vol.16 , pp. 1457-1472
    • Nans, A.1    Saibil, H.R.2    Hayward, R.D.3
  • 40
    • 84908543848 scopus 로고    scopus 로고
    • Making connections: Snapshots of chlamydial type III secretion systems in contact with host membranes
    • Dumoux, M., Nans, A., Saibil, H. R. & Hayward, R. D. Making connections: snapshots of chlamydial type III secretion systems in contact with host membranes. Curr. Opin. Microbiol. 23, 1-7 (2015).
    • (2015) Curr. Opin. Microbiol. , vol.23 , pp. 1-7
    • Dumoux, M.1    Nans, A.2    Saibil, H.R.3    Hayward, R.D.4
  • 41
    • 84856237323 scopus 로고    scopus 로고
    • Chlamydia pneumoniae entry into epithelial cells by clathrin-independent endocytosis
    • Korhonen, J. T. et al. Chlamydia pneumoniae entry into epithelial cells by clathrin-independent endocytosis. Microb. Pathog. 52, 157-164 (2012).
    • (2012) Microb. Pathog. , vol.52 , pp. 157-164
    • Korhonen, J.T.1
  • 42
    • 84911472000 scopus 로고    scopus 로고
    • Conserved type III secretion system exerts important roles in Chlamydia trachomatis
    • Dai, W. & Li, Z. Conserved type III secretion system exerts important roles in Chlamydia trachomatis. Int. J. Clin. Exp. Pathol. 7, 5404-5414 (2014).
    • (2014) Int. J. Clin. Exp. Pathol. , vol.7 , pp. 5404-5414
    • Dai, W.1    Li, Z.2
  • 43
    • 84873535013 scopus 로고    scopus 로고
    • Chlamydia trachomatis TarP harbors distinct G and F actin binding domains that bundle actin filaments
    • Jiwani, S. et al. Chlamydia trachomatis TarP harbors distinct G and F actin binding domains that bundle actin filaments. J. Bacteriol. 195, 708-716 (2013).
    • (2013) J. Bacteriol. , vol.195 , pp. 708-716
    • Jiwani, S.1
  • 44
    • 84908592806 scopus 로고    scopus 로고
    • The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion
    • Thwaites, T. et al. The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion. J. Biol. Chem. 289, 30426-30442 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 30426-30442
    • Thwaites, T.1
  • 45
    • 84897692384 scopus 로고    scopus 로고
    • The Chlamydia trachomatis type III secretion chaperone Slc1 engages multiple early effectors, including TepP, a tyrosine-phosphorylated protein required for the recruitment of CrkI-II to nascent inclusions and innate immune signaling
    • Chen, Y. S. et al. The Chlamydia trachomatis type III secretion chaperone Slc1 engages multiple early effectors, including TepP, a tyrosine-phosphorylated protein required for the recruitment of CrkI-II to nascent inclusions and innate immune signaling. PLoS Pathog. 10, e1003954 (2014).
    • (2014) PLoS Pathog. , vol.10 , pp. e1003954
    • Chen, Y.S.1
  • 46
    • 84874196853 scopus 로고    scopus 로고
    • Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis
    • Pais, S. V., Milho, C., Almeida, F. & Mota, L. J. Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis. PLoS ONE 8, e56292 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e56292
    • Pais, S.V.1    Milho, C.2    Almeida, F.3    Mota, L.J.4
  • 47
    • 84865015973 scopus 로고    scopus 로고
    • Domain analyses reveal that Chlamydia trachomatis CT694 protein belongs to the membrane-localized family of type III effector proteins
    • Bullock, H. D., Hower, S. & Fields, K. A. Domain analyses reveal that Chlamydia trachomatis CT694 protein belongs to the membrane-localized family of type III effector proteins. J. Biol. Chem. 287, 28078-28086 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 28078-28086
    • Bullock, H.D.1    Hower, S.2    Fields, K.A.3
  • 48
    • 84929392923 scopus 로고    scopus 로고
    • SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
    • Mojica, S. A. et al. SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors. Mol. Biol. Cell 26, 1918-1934 (2015).
    • (2015) Mol. Biol. Cell , vol.26 , pp. 1918-1934
    • Mojica, S.A.1
  • 50
    • 84881035019 scopus 로고    scopus 로고
    • Chlamydia trachomatis homotypic inclusion fusion is promoted by host microtubule trafficking
    • Richards, T. S., Knowlton, A. E. & Grieshaber, S. S. Chlamydia trachomatis homotypic inclusion fusion is promoted by host microtubule trafficking. BMC Microbiol. 13, 185 (2013).
    • (2013) BMC Microbiol. , vol.13 , pp. 185
    • Richards, T.S.1    Knowlton, A.E.2    Grieshaber, S.S.3
  • 51
    • 84930196697 scopus 로고    scopus 로고
    • Chlamydia trachomatis inclusion membrane protein CT850 interacts with the dynein light chain DYNLT1 (Tctex1)
    • Mital, J., Lutter, E. I., Barger, A. C., Dooley, C. A. & Hackstadt, T. Chlamydia trachomatis inclusion membrane protein CT850 interacts with the dynein light chain DYNLT1 (Tctex1). Biochem. Biophys. Res. Commun. 462, 165-170 (2015).
    • (2015) Biochem. Biophys. Res. Commun. , vol.462 , pp. 165-170
    • Mital, J.1    Lutter, E.I.2    Barger, A.C.3    Dooley, C.A.4    Hackstadt, T.5
  • 52
    • 84903817950 scopus 로고    scopus 로고
    • Chlamydia psittaci inclusion membrane protein IncB associates with host protein Snapin
    • Bocker, S. et al. Chlamydia psittaci inclusion membrane protein IncB associates with host protein Snapin. Int. J. Med. Microbiol. 304, 542-553 (2014).
    • (2014) Int. J. Med. Microbiol. , vol.304 , pp. 542-553
    • Bocker, S.1
  • 53
    • 84906790612 scopus 로고    scopus 로고
    • Targeting eukaryotic Rab proteins: A smart strategy for chlamydial survival and replication
    • Damiani, M. T., Gambarte Tudela, J. & Capmany, A. Targeting eukaryotic Rab proteins: a smart strategy for chlamydial survival and replication. Cell. Microbiol. 16, 1329-1338 (2014).
    • (2014) Cell. Microbiol. , vol.16 , pp. 1329-1338
    • Damiani, M.T.1    Gambarte Tudela, J.2    Capmany, A.3
  • 54
    • 84939474868 scopus 로고    scopus 로고
    • The late endocytic Rab39a GTPase regulates multivesicular bodies-chlamydial inclusion interaction and bacterial growth
    • Gambarte Tudela, J. et al. The late endocytic Rab39a GTPase regulates multivesicular bodies-chlamydial inclusion interaction and bacterial growth. J. Cell Sci. 128, 3068-3081 (2015).
    • (2015) J. Cell Sci. , vol.128 , pp. 3068-3081
    • Gambarte Tudela, J.1
  • 55
    • 84871051175 scopus 로고    scopus 로고
    • Rab11-family of interacting protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
    • Leiva, N., Capmany, A. & Damiani, M. T. Rab11-family of interacting protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication. Cell. Microbiol. 15, 114-129 (2013).
    • (2013) Cell. Microbiol. , vol.15 , pp. 114-129
    • Leiva, N.1    Capmany, A.2    Damiani, M.T.3
  • 56
    • 84922537676 scopus 로고    scopus 로고
    • Bicaudal D family adaptor proteins control the velocity of Dynein-based movements
    • Schlager, M. A. et al. Bicaudal D family adaptor proteins control the velocity of Dynein-based movements. Cell Rep. 8, 1248-1256 (2014).
    • (2014) Cell Rep. , vol.8 , pp. 1248-1256
    • Schlager, M.A.1
  • 57
    • 77951231154 scopus 로고    scopus 로고
    • Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion
    • Moorhead, A. M., Jung, J. Y., Smirnov, A., Kaufer, S. & Scidmore, M. A. Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion. Infect. Immun. 78, 1990-2007 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 1990-2007
    • Moorhead, A.M.1    Jung, J.Y.2    Smirnov, A.3    Kaufer, S.4    Scidmore, M.A.5
  • 58
    • 79952261147 scopus 로고    scopus 로고
    • The trans-Golgi SNARE syntaxin 6 is recruited to the chlamydial inclusion membrane
    • Moore, E. R., Mead, D. J., Dooley, C. A., Sager, J. & Hackstadt, T. The trans-Golgi SNARE syntaxin 6 is recruited to the chlamydial inclusion membrane. Microbiology 157, 830-838 (2011).
    • (2011) Microbiology , vol.157 , pp. 830-838
    • Moore, E.R.1    Mead, D.J.2    Dooley, C.A.3    Sager, J.4    Hackstadt, T.5
  • 61
    • 84884217866 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 4 and syntaxin 6 interactions at the chlamydial inclusion
    • Kabeiseman, E. J., Cichos, K., Hackstadt, T., Lucas, A. & Moore, E. R. Vesicle-associated membrane protein 4 and syntaxin 6 interactions at the chlamydial inclusion. Infect. Immun. 81, 3326-3337 (2013).
    • (2013) Infect. Immun. , vol.81 , pp. 3326-3337
    • Kabeiseman, E.J.1    Cichos, K.2    Hackstadt, T.3    Lucas, A.4    Moore, E.R.5
  • 62
    • 84859892605 scopus 로고    scopus 로고
    • Chlamydia trachomatis hijacks intra-Golgi COG complex-dependent vesicle trafficking pathway
    • Pokrovskaya, I. D. et al. Chlamydia trachomatis hijacks intra-Golgi COG complex-dependent vesicle trafficking pathway. Cell. Microbiol. 14, 656-668 (2012).
    • (2012) Cell. Microbiol. , vol.14 , pp. 656-668
    • Pokrovskaya, I.D.1
  • 63
    • 84880718252 scopus 로고    scopus 로고
    • Tw o coiled-coil domains of Chlamydia trachomatis IncA affect membrane fusion events during infection
    • Ronzone, E. & Paumet, F. Tw o coiled-coil domains of Chlamydia trachomatis IncA affect membrane fusion events during infection. PLoS ONE 8, e69769 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e69769
    • Ronzone, E.1    Paumet, F.2
  • 64
    • 84912133953 scopus 로고    scopus 로고
    • An α-helical core encodes the dual functions of the chlamydial protein IncA
    • Ronzone, E. et al. An α-helical core encodes the dual functions of the chlamydial protein IncA. J. Biol. Chem. 289, 33469-33480 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 33469-33480
    • Ronzone, E.1
  • 65
    • 84965189434 scopus 로고    scopus 로고
    • Characterization of interactions between inclusion membrane proteins from Chlamydia trachomatis
    • Gauliard, E., Ouellette, S. P., Rueden, K. J. & Ladant, D. Characterization of interactions between inclusion membrane proteins from Chlamydia trachomatis. Front. Cell. Infect. Microbiol. 5, 13 (2015).
    • (2015) Front. Cell. Infect. Microbiol. , vol.5 , pp. 13
    • Gauliard, E.1    Ouellette, S.P.2    Rueden, K.J.3    Ladant, D.4
  • 66
    • 0035479046 scopus 로고    scopus 로고
    • Epidemiology and clinical manifestations of unique Chlamydia trachomatis isolates that occupy nonfusogenic inclusions
    • Geisler, W. M., Suchland, R. J., Rockey, D. D. & Stamm, W. E. Epidemiology and clinical manifestations of unique Chlamydia trachomatis isolates that occupy nonfusogenic inclusions. J. Infect. Dis. 184, 879-884 (2001).
    • (2001) J. Infect. Dis. , vol.184 , pp. 879-884
    • Geisler, W.M.1    Suchland, R.J.2    Rockey, D.D.3    Stamm, W.E.4
  • 67
    • 84943186180 scopus 로고    scopus 로고
    • Global mapping of the Inc-human interactome reveals that retromer restricts Chlamydia infection
    • Mirrashidi, K. M. et al. Global mapping of the Inc-human interactome reveals that retromer restricts Chlamydia infection. Cell Host Microbe 18, 109-121 (2015).
    • (2015) Cell Host Microbe , vol.18 , pp. 109-121
    • Mirrashidi, K.M.1
  • 68
    • 84936753193 scopus 로고    scopus 로고
    • The proteome of the isolated Chlamydia trachomatis containing vacuole reveals a complex trafficking platform enriched for retromer components
    • Aeberhard, L. et al. The proteome of the isolated Chlamydia trachomatis containing vacuole reveals a complex trafficking platform enriched for retromer components. PLoS Pathog. 11, e1004883 (2015).
    • (2015) PLoS Pathog. , vol.11 , pp. e1004883
    • Aeberhard, L.1
  • 69
    • 84872183810 scopus 로고    scopus 로고
    • The retromer complex-endosomal protein recycling and beyond
    • Seaman, M. N. The retromer complex-endosomal protein recycling and beyond. J. Cell Sci. 125, 4693-4702 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 4693-4702
    • Seaman, M.N.1
  • 70
    • 84880657924 scopus 로고    scopus 로고
    • Chlamydia trachomatis transports NAD via the Npt1 ATP/ADP translocase
    • Fisher, D. J., Fernandez, R. E. & Maurelli, A. T. Chlamydia trachomatis transports NAD via the Npt1 ATP/ADP translocase. J. Bacteriol. 195, 3381-3386 (2013).
    • (2013) J. Bacteriol. , vol.195 , pp. 3381-3386
    • Fisher, D.J.1    Fernandez, R.E.2    Maurelli, A.T.3
  • 71
    • 84907853391 scopus 로고    scopus 로고
    • Dynamin-mediated lipid acquisition is essential for Chlamydia trachomatis development
    • Gurumurthy, R. K. et al. Dynamin-mediated lipid acquisition is essential for Chlamydia trachomatis development. Mol. Microbiol. 94, 186-201 (2014).
    • (2014) Mol. Microbiol. , vol.94 , pp. 186-201
    • Gurumurthy, R.K.1
  • 72
    • 84893349228 scopus 로고    scopus 로고
    • A CREB3-ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens
    • Reiling, J. H. et al. A CREB3-ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens. Nat. Cell Biol. 15, 1473-1485 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1473-1485
    • Reiling, J.H.1
  • 73
    • 80053446744 scopus 로고    scopus 로고
    • Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development
    • Elwell, C. A. et al. Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development. PLoS Pathog. 7, e1002198 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1002198
    • Elwell, C.A.1
  • 74
    • 79959845500 scopus 로고    scopus 로고
    • The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sites
    • Derre, I., Swiss, R. & Agaisse, H. The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sites. PLoS Pathog. 7, e1002092 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1002092
    • Derre, I.1    Swiss, R.2    Agaisse, H.3
  • 75
    • 84898892202 scopus 로고    scopus 로고
    • Expression of the effector protein IncD in Chlamydia trachomatis mediates recruitment of the lipid transfer protein CERT and the endoplasmic reticulum-resident protein VAPB to the inclusion membrane
    • Agaisse, H. & Derre, I. Expression of the effector protein IncD in Chlamydia trachomatis mediates recruitment of the lipid transfer protein CERT and the endoplasmic reticulum-resident protein VAPB to the inclusion membrane. Infect. Immun. 82, 2037-2047 (2014).
    • (2014) Infect. Immun. , vol.82 , pp. 2037-2047
    • Agaisse, H.1    Derre, I.2
  • 76
    • 84866329972 scopus 로고    scopus 로고
    • Host HDL biogenesis machinery is recruited to the inclusion of Chlamydia trachomatis-infected cells and regulates chlamydial growth
    • Cox, J. V., Naher, N., Abdelrahman, Y. M. & Belland, R. J. Host HDL biogenesis machinery is recruited to the inclusion of Chlamydia trachomatis-infected cells and regulates chlamydial growth. Cell. Microbiol. 14, 1497-1512 (2012).
    • (2012) Cell. Microbiol. , vol.14 , pp. 1497-1512
    • Cox, J.V.1    Naher, N.2    Abdelrahman, Y.M.3    Belland, R.J.4
  • 77
    • 84941312992 scopus 로고    scopus 로고
    • Chlamydia trachomatis scavenges host fatty acids for phospholipid synthesis via an acyl-acyl carrier protein synthetase
    • Yao, J., Dodson, V. J., Frank, M. W. & Rock, C. O. Chlamydia trachomatis scavenges host fatty acids for phospholipid synthesis via an acyl-acyl carrier protein synthetase. J. Biol. Chem. 290, 22163-22173 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 22163-22173
    • Yao, J.1    Dodson, V.J.2    Frank, M.W.3    Rock, C.O.4
  • 78
    • 84940499894 scopus 로고    scopus 로고
    • Chlamydia trachomatis relies on autonomous phospholipid synthesis for membrane biogenesis
    • Yao, J., Cherian, P. T., Frank, M. W. & Rock, C. O. Chlamydia trachomatis relies on autonomous phospholipid synthesis for membrane biogenesis. J. Biol. Chem. 290, 18874-18888 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 18874-18888
    • Yao, J.1    Cherian, P.T.2    Frank, M.W.3    Rock, C.O.4
  • 79
    • 84905851436 scopus 로고    scopus 로고
    • Type II fatty acid synthesis is essential for the replication of Chlamydia trachomatis
    • Yao, J. et al. Type II fatty acid synthesis is essential for the replication of Chlamydia trachomatis. J. Biol. Chem. 289, 22365-22376 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 22365-22376
    • Yao, J.1
  • 80
    • 59649092835 scopus 로고    scopus 로고
    • Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction
    • Heuer, D. et al. Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction. Nature 457, 731-735 (2009).
    • (2009) Nature , vol.457 , pp. 731-735
    • Heuer, D.1
  • 81
    • 84929510811 scopus 로고    scopus 로고
    • Integrating chemical mutagenesis and whole-genome sequencing as a platform for forward and reverse genetic analysis of Chlamydia
    • Kokes, M. et al. Integrating chemical mutagenesis and whole-genome sequencing as a platform for forward and reverse genetic analysis of Chlamydia. Cell Host Microbe 17, 716-725 (2015).
    • (2015) Cell Host Microbe , vol.17 , pp. 716-725
    • Kokes, M.1
  • 82
    • 84911407936 scopus 로고    scopus 로고
    • Chlamydia trachomatis remodels stable microtubules to coordinate Golgi stack recruitment to the chlamydial inclusion surface
    • Al-Zeer, M. A. et al. Chlamydia trachomatis remodels stable microtubules to coordinate Golgi stack recruitment to the chlamydial inclusion surface. Mol. Microbiol. 94, 1285-1297 (2014).
    • (2014) Mol. Microbiol. , vol.94 , pp. 1285-1297
    • Al-Zeer, M.A.1
  • 83
    • 84947263167 scopus 로고    scopus 로고
    • Differential translocation of host cellular materials into the Chlamydia trachomatis inclusion lumen during chemical fixation
    • Kokes, M. & Valdivia, R. H. Differential translocation of host cellular materials into the Chlamydia trachomatis inclusion lumen during chemical fixation. PLoS ONE 10, e0139153 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0139153
    • Kokes, M.1    Valdivia, R.H.2
  • 84
    • 84899842142 scopus 로고    scopus 로고
    • The intracellular bacteria Chlamydia hijack peroxisomes and utilize their enzymatic capacity to produce bacteria-specific phospholipids
    • Boncompain, G. et al. The intracellular bacteria Chlamydia hijack peroxisomes and utilize their enzymatic capacity to produce bacteria-specific phospholipids. PLoS ONE 9, e86196 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e86196
    • Boncompain, G.1
  • 85
    • 84929991908 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection leads to defined alterations to the lipid droplet proteome in epithelial cells
    • Saka, H. A. et al. Chlamydia trachomatis infection leads to defined alterations to the lipid droplet proteome in epithelial cells. PLoS ONE 10, e0124630 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0124630
    • Saka, H.A.1
  • 86
    • 84860713687 scopus 로고    scopus 로고
    • Eukaryotic protein recruitment into the Chlamydia inclusion: Implications for survival and growth
    • Soupene, E., Rothschild, J., Kuypers, F. A. & Dean, D. Eukaryotic protein recruitment into the Chlamydia inclusion: implications for survival and growth. PLoS ONE 7, e36843 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e36843
    • Soupene, E.1    Rothschild, J.2    Kuypers, F.A.3    Dean, D.4
  • 87
    • 84926421028 scopus 로고    scopus 로고
    • Remodeling of host phosphatidylcholine by Chlamydia acyltransferase is regulated by acyl-CoA binding protein ACBD6 associated with lipid droplets
    • Soupene, E., Wang, D. & Kuypers, F. A. Remodeling of host phosphatidylcholine by Chlamydia acyltransferase is regulated by acyl-CoA binding protein ACBD6 associated with lipid droplets. Microbiologyopen 4, 235-251 (2015).
    • (2015) Microbiologyopen , vol.4 , pp. 235-251
    • Soupene, E.1    Wang, D.2    Kuypers, F.A.3
  • 88
    • 84931566276 scopus 로고    scopus 로고
    • Chlamydiae interaction with the endoplasmic reticulum: Contact, function and consequences
    • Derre, I. Chlamydiae interaction with the endoplasmic reticulum: contact, function and consequences. Cell. Microbiol. 17, 959-966 (2015).
    • (2015) Cell. Microbiol. , vol.17 , pp. 959-966
    • Derre, I.1
  • 89
    • 84928565638 scopus 로고    scopus 로고
    • STIM1 is a novel component of ER-Chlamydia trachomatis inclusion membrane contact sites
    • Agaisse, H. & Derre, I. STIM1 is a novel component of ER-Chlamydia trachomatis inclusion membrane contact sites. PLoS ONE 10, e0125671 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0125671
    • Agaisse, H.1    Derre, I.2
  • 90
    • 84878616469 scopus 로고    scopus 로고
    • STING-dependent recognition of cyclic di-AMP mediates type i interferon responses during Chlamydia trachomatis infection
    • Barker, J. R. et al. STING-dependent recognition of cyclic di-AMP mediates type I interferon responses during Chlamydia trachomatis infection. mBio 4, e00018-13 (2013).
    • (2013) MBio , vol.4 , pp. e00018-13
    • Barker, J.R.1
  • 91
    • 84931572331 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum-related BiP/GRP78 in interferon-γ-induced persistent Chlamydia pneumoniae infection
    • Shima, K. et al. The role of endoplasmic reticulum-related BiP/GRP78 in interferon-γ-induced persistent Chlamydia pneumoniae infection. Cell. Microbiol. 17, 923-934 (2015).
    • (2015) Cell. Microbiol. , vol.17 , pp. 923-934
    • Shima, K.1
  • 92
    • 84905049631 scopus 로고    scopus 로고
    • The chlamydial organism Simkania negevensis forms ER vacuole contact sites and inhibits ER-stress
    • Mehlitz, A. et al. The chlamydial organism Simkania negevensis forms ER vacuole contact sites and inhibits ER-stress. Cell. Microbiol. 16, 1224-1243 (2014).
    • (2014) Cell. Microbiol. , vol.16 , pp. 1224-1243
    • Mehlitz, A.1
  • 93
    • 84873253603 scopus 로고    scopus 로고
    • Chlamydiae assemble a pathogen synapse to hijack the host endoplasmic reticulum
    • Dumoux, M., Clare, D. K., Saibil, H. R. & Hayward, R. D. Chlamydiae assemble a pathogen synapse to hijack the host endoplasmic reticulum. Traffic 13, 1612-1627 (2012).
    • (2012) Traffic , vol.13 , pp. 1612-1627
    • Dumoux, M.1    Clare, D.K.2    Saibil, H.R.3    Hayward, R.D.4
  • 94
    • 84908441266 scopus 로고    scopus 로고
    • Septins arrange F-actin-containing fibers on the Chlamydia trachomatis inclusion and are required for normal release of the inclusion by extrusion
    • Volceanov, L. et al. Septins arrange F-actin-containing fibers on the Chlamydia trachomatis inclusion and are required for normal release of the inclusion by extrusion. mBio 5, e01802-14 (2014).
    • (2014) MBio , vol.5 , pp. e01802-e01814
    • Volceanov, L.1
  • 95
    • 84924199277 scopus 로고    scopus 로고
    • Activation of epidermal growth factor receptor is required for Chlamydia trachomatis development
    • Patel, A. L. et al. Activation of epidermal growth factor receptor is required for Chlamydia trachomatis development. BMC Microbiol. 14, 277 (2014).
    • (2014) BMC Microbiol. , vol.14 , pp. 277
    • Patel, A.L.1
  • 96
    • 84946061503 scopus 로고    scopus 로고
    • A Chlamydia effector recruits CEP170 to reprogram host microtubule organization
    • Dumoux, M., Menny, A., Delacour, D. & Hayward, R. D. A Chlamydia effector recruits CEP170 to reprogram host microtubule organization. J. Cell Sci. 128, 3420-3434 (2015).
    • (2015) J. Cell Sci. , vol.128 , pp. 3420-3434
    • Dumoux, M.1    Menny, A.2    Delacour, D.3    Hayward, R.D.4
  • 97
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske, K. & Stephens, R. S. Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc. Natl Acad. Sci. USA 104, 11430-11435 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.S.2
  • 98
    • 84904867513 scopus 로고    scopus 로고
    • Reassessing the role of the secreted protease CPAF in Chlamydia trachomatis infection through genetic approaches
    • Snavely, E. A. et al. Reassessing the role of the secreted protease CPAF in Chlamydia trachomatis infection through genetic approaches. Pathog. Dis. 71, 336-351 (2014).
    • (2014) Pathog. Dis. , vol.71 , pp. 336-351
    • Snavely, E.A.1
  • 99
    • 84929485224 scopus 로고    scopus 로고
    • Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection
    • Yang, Z., Tang, L., Sun, X., Chai, J. & Zhong, G. Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection. Infect. Immun. 83, 2234-2241 (2015).
    • (2015) Infect. Immun. , vol.83 , pp. 2234-2241
    • Yang, Z.1    Tang, L.2    Sun, X.3    Chai, J.4    Zhong, G.5
  • 100
    • 84879795143 scopus 로고    scopus 로고
    • Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms
    • Lutter, E. I., Barger, A. C., Nair, V. & Hackstadt, T. Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms. Cell Rep. 3, 1921-1931 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1921-1931
    • Lutter, E.I.1    Barger, A.C.2    Nair, V.3    Hackstadt, T.4
  • 101
    • 84867421419 scopus 로고    scopus 로고
    • Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors
    • Chin, E., Kirker, K., Zuck, M., James, G. & Hybiske, K. Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors. PLoS ONE 7, e46949 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e46949
    • Chin, E.1    Kirker, K.2    Zuck, M.3    James, G.4    Hybiske, K.5
  • 102
    • 84947017752 scopus 로고    scopus 로고
    • Chlamydia-infected cells shed Gp96 to prevent chlamydial re-infection
    • Karunakaran, K., Subbarayal, P., Vollmuth, N. & Rudel, T. Chlamydia-infected cells shed Gp96 to prevent chlamydial re-infection. Mol. Microbiol. 98, 694-711 (2015).
    • (2015) Mol. Microbiol. , vol.98 , pp. 694-711
    • Karunakaran, K.1    Subbarayal, P.2    Vollmuth, N.3    Rudel, T.4
  • 103
    • 84930643382 scopus 로고    scopus 로고
    • The Chlamydia pneumoniae inclusion membrane protein Cpn1027 interacts with host cell Wnt signaling pathway regulator cytoplasmic activation/proliferation-associated protein 2 (Caprin2)
    • Flores, R. & Zhong, G. The Chlamydia pneumoniae inclusion membrane protein Cpn1027 interacts with host cell Wnt signaling pathway regulator cytoplasmic activation/proliferation-associated protein 2 (Caprin2). PLoS ONE 10, e0127909 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0127909
    • Flores, R.1    Zhong, G.2
  • 104
    • 60049088257 scopus 로고    scopus 로고
    • Apoptosis resistance in Chlamydia-infected cells: A fate worse than death?
    • Sharma, M. & Rudel, T. Apoptosis resistance in Chlamydia-infected cells: a fate worse than death? FEMS Immunol. Med. Microbiol. 55, 154-161 (2009).
    • (2009) FEMS Immunol. Med. Microbiol. , vol.55 , pp. 154-161
    • Sharma, M.1    Rudel, T.2
  • 105
    • 84928771542 scopus 로고    scopus 로고
    • Chlamydia infection depends on a functional MDM2-p53 axis
    • Gonzalez, E. et al. Chlamydia infection depends on a functional MDM2-p53 axis. Nat. Commun. 5, 5201 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 5201
    • Gonzalez, E.1
  • 106
    • 84919771811 scopus 로고    scopus 로고
    • Tumor suppressor p53 alters host cell metabolism to limit Chlamydia trachomatis infection
    • Siegl, C., Prusty, B. K., Karunakaran, K., Wischhusen, J. & Rudel, T. Tumor suppressor p53 alters host cell metabolism to limit Chlamydia trachomatis infection. Cell Rep. 9, 918-929 (2014).
    • (2014) Cell Rep. , vol.9 , pp. 918-929
    • Siegl, C.1    Prusty, B.K.2    Karunakaran, K.3    Wischhusen, J.4    Rudel, T.5
  • 107
    • 84881474061 scopus 로고    scopus 로고
    • Chlamydia inhibit host cell apoptosis by inducing Bag-1 via the MAPK/ERK survival pathway
    • Kun, D., Xiang-Lin, C., Ming, Z. & Qi, L. Chlamydia inhibit host cell apoptosis by inducing Bag-1 via the MAPK/ERK survival pathway. Apoptosis 18, 1083-1092 (2013).
    • (2013) Apoptosis , vol.18 , pp. 1083-1092
    • Kun, D.1    Xiang-Lin, C.2    Ming, Z.3    Qi, L.4
  • 108
    • 77957120464 scopus 로고    scopus 로고
    • Chlamydia trachomatis-infected host cells resist dsRNA-induced apoptosis
    • Bohme, L., Albrecht, M., Riede, O. & Rudel, T. Chlamydia trachomatis-infected host cells resist dsRNA-induced apoptosis. Cell. Microbiol. 12, 1340-1351 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 1340-1351
    • Bohme, L.1    Albrecht, M.2    Riede, O.3    Rudel, T.4
  • 109
    • 84866172218 scopus 로고    scopus 로고
    • CPAF: A chlamydial protease in search of an authentic substrate
    • Chen, A. L., Johnson, K. A., Lee, J. K., Sutterlin, C. & Tan, M. CPAF: a chlamydial protease in search of an authentic substrate. PLoS Pathog. 8, e1002842 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002842
    • Chen, A.L.1    Johnson, K.A.2    Lee, J.K.3    Sutterlin, C.4    Tan, M.5
  • 110
    • 84923129480 scopus 로고    scopus 로고
    • DXD motif-dependent and-independent effects of the Chlamydia trachomatis cytotoxin CT166
    • Bothe, M., Dutow, P., Pich, A., Genth, H. & Klos, A. DXD motif-dependent and-independent effects of the Chlamydia trachomatis cytotoxin CT166. Toxins (Basel) 7, 621-637 (2015).
    • (2015) Toxins (Basel) , vol.7 , pp. 621-637
    • Bothe, M.1    Dutow, P.2    Pich, A.3    Genth, H.4    Klos, A.5
  • 111
    • 84903550840 scopus 로고    scopus 로고
    • Multinucleation during C. Trachomatis infections is caused by the contribution of two effector pathways
    • Brown, H. M. et al. Multinucleation during C. trachomatis infections is caused by the contribution of two effector pathways. PLoS ONE 9, e100763 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e100763
    • Brown, H.M.1
  • 112
    • 55549138715 scopus 로고    scopus 로고
    • The essential role of the CopN protein in Chlamydia pneumoniae intracellular growth
    • Huang, J., Lesser, C. F. & Lory, S. The essential role of the CopN protein in Chlamydia pneumoniae intracellular growth. Nature 456, 112-115 (2008).
    • (2008) Nature , vol.456 , pp. 112-115
    • Huang, J.1    Lesser, C.F.2    Lory, S.3
  • 113
    • 84906974130 scopus 로고    scopus 로고
    • Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae
    • Nawrotek, A. et al. Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae. J. Biol. Chem. 289, 25199-25210 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 25199-25210
    • Nawrotek, A.1
  • 114
    • 84957308868 scopus 로고    scopus 로고
    • Chlamydia trachomatis inclusion disrupts host cell cytokinesis to enhance its growth in multinuclear cells
    • Sun, H. S., Sin, A. T., Poirier, M. & Harrison, R. E. Chlamydia trachomatis inclusion disrupts host cell cytokinesis to enhance its growth in multinuclear cells. J. Cell Biochem. 117, 132-143 (2015).
    • (2015) J. Cell Biochem. , vol.117 , pp. 132-143
    • Sun, H.S.1    Sin, A.T.2    Poirier, M.3    Harrison, R.E.4
  • 115
    • 79958768096 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection causes mitotic spindle pole defects independently from its effects on centrosome amplification
    • Knowlton, A. E. et al. Chlamydia trachomatis infection causes mitotic spindle pole defects independently from its effects on centrosome amplification. Traffic 12, 854-866 (2011).
    • (2011) Traffic , vol.12 , pp. 854-866
    • Knowlton, A.E.1
  • 116
    • 77957127488 scopus 로고    scopus 로고
    • Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network
    • Mital, J., Miller, N. J., Fischer, E. R. & Hackstadt, T. Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network. Cell. Microbiol. 12, 1235-1249 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 1235-1249
    • Mital, J.1    Miller, N.J.2    Fischer, E.R.3    Hackstadt, T.4
  • 117
    • 84879113042 scopus 로고    scopus 로고
    • Chlamydia infection promotes host DNA damage and proliferation but impairs the DNA damage response
    • Chumduri, C., Gurumurthy, R. K., Zadora, P. K., Mi, Y. & Meyer, T. F. Chlamydia infection promotes host DNA damage and proliferation but impairs the DNA damage response. Cell Host Microbe 13, 746-758 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 746-758
    • Chumduri, C.1    Gurumurthy, R.K.2    Zadora, P.K.3    Mi, Y.4    Meyer, T.F.5
  • 118
  • 119
    • 84872017157 scopus 로고    scopus 로고
    • Chlamydia induces anchorage independence in 3T3 cells and detrimental cytological defects in an infection model
    • Knowlton, A. E., Fowler, L. J., Patel, R. K., Wallet, S. M. & Grieshaber, S. S. Chlamydia induces anchorage independence in 3T3 cells and detrimental cytological defects in an infection model. PLoS ONE 8, e54022 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e54022
    • Knowlton, A.E.1    Fowler, L.J.2    Patel, R.K.3    Wallet, S.M.4    Grieshaber, S.S.5
  • 120
    • 84887611781 scopus 로고    scopus 로고
    • Chlamydia trachomatis inhibits telomeric DNA damage signaling via transient hTERT upregulation
    • Padberg, I., Janssen, S. & Meyer, T. F. Chlamydia trachomatis inhibits telomeric DNA damage signaling via transient hTERT upregulation. Int. J. Med. Microbiol. 303, 463-474 (2013).
    • (2013) Int. J. Med. Microbiol. , vol.303 , pp. 463-474
    • Padberg, I.1    Janssen, S.2    Meyer, T.F.3
  • 123
    • 84870250210 scopus 로고    scopus 로고
    • Innate immune responses to Chlamydia pneumoniae infection: Role of TLRs NLRs and the inflammasome
    • Shimada, K., Crother, T. R. & Arditi, M. Innate immune responses to Chlamydia pneumoniae infection: role of TLRs, NLRs, and the inflammasome. Microbes Infect. 14, 1301-1307 (2012).
    • (2012) Microbes Infect. , vol.14 , pp. 1301-1307
    • Shimada, K.1    Crother, T.R.2    Arditi, M.3
  • 125
    • 84907025040 scopus 로고    scopus 로고
    • The DNA sensor, cyclic GMP-AMP synthase, is essential for induction of IFN-β during Chlamydia trachomatis infection
    • Zhang, Y. et al. The DNA sensor, cyclic GMP-AMP synthase, is essential for induction of IFN-β during Chlamydia trachomatis infection. J. Immunol. 193, 2394-2404 (2014).
    • (2014) J. Immunol. , vol.193 , pp. 2394-2404
    • Zhang, Y.1
  • 126
    • 78650630756 scopus 로고    scopus 로고
    • Enhancement of reactive oxygen species production and chlamydial infection by the mitochondrial Nod-like family member NLRX1
    • Abdul-Sater, A. A. et al. Enhancement of reactive oxygen species production and chlamydial infection by the mitochondrial Nod-like family member NLRX1. J. Biol. Chem. 285, 41637-41645 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 41637-41645
    • Abdul-Sater, A.A.1
  • 127
    • 84907482558 scopus 로고    scopus 로고
    • Chlamydia pneumoniae harness host NLRP3 inflammasome-mediated caspase-1 activation for optimal intracellular growth in murine macrophages
    • Itoh, R. et al. Chlamydia pneumoniae harness host NLRP3 inflammasome-mediated caspase-1 activation for optimal intracellular growth in murine macrophages. Biochem. Biophys. Res. Commun. 452, 689-694 (2014).
    • (2014) Biochem. Biophys. Res. Commun. , vol.452 , pp. 689-694
    • Itoh, R.1
  • 128
    • 84873559158 scopus 로고    scopus 로고
    • Chlamydia pneumoniae impairs the innate immune response in infected epithelial cells by targeting TRAF3
    • Wolf, K. & Fields, K. A. Chlamydia pneumoniae impairs the innate immune response in infected epithelial cells by targeting TRAF3. J. Immunol. 190, 1695-1701 (2013).
    • (2013) J. Immunol. , vol.190 , pp. 1695-1701
    • Wolf, K.1    Fields, K.A.2
  • 129
    • 84907083338 scopus 로고    scopus 로고
    • Chlamydia trachomatis inhibits inducible NO synthase in human mesenchymal stem cells by stimulating polyamine synthesis
    • Abu-Lubad, M., Meyer, T. F. & Al-Zeer, M. A. Chlamydia trachomatis inhibits inducible NO synthase in human mesenchymal stem cells by stimulating polyamine synthesis. J. Immunol. 193, 2941-2951 (2014).
    • (2014) J. Immunol. , vol.193 , pp. 2941-2951
    • Abu-Lubad, M.1    Meyer, T.F.2    Al-Zeer, M.A.3
  • 130
    • 84872194128 scopus 로고    scopus 로고
    • Autophagy restricts Chlamydia trachomatis growth in human macrophages via IFNγ-inducible guanylate binding proteins
    • Al-Zeer, M. A., Al-Younes, H. M., Lauster, D., Abu Lubad, M. & Meyer, T. F. Autophagy restricts Chlamydia trachomatis growth in human macrophages via IFNγ-inducible guanylate binding proteins. Autophagy 9, 50-62 (2013).
    • (2013) Autophagy , vol.9 , pp. 50-62
    • Al-Zeer, M.A.1    Al-Younes, H.M.2    Lauster, D.3    Abu Lubad, M.4    Meyer, T.F.5
  • 131
    • 84944242576 scopus 로고    scopus 로고
    • Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins
    • Haldar, A. K. et al. Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins. Proc. Natl Acad. Sci. USA 112, E5628-E5637 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E5628-E5637
    • Haldar, A.K.1
  • 132
    • 84898471391 scopus 로고    scopus 로고
    • The E2-like conjugation enzyme Atg3 promotes binding of IRG and Gbp proteins to Chlamydia-and Toxoplasma-containing vacuoles and host resistance
    • Haldar, A. K., Piro, A. S., Pilla, D. M., Yamamoto, M. & Coers, J. The E2-like conjugation enzyme Atg3 promotes binding of IRG and Gbp proteins to Chlamydia-and Toxoplasma-containing vacuoles and host resistance. PLoS ONE 9, e86684 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e86684
    • Haldar, A.K.1    Piro, A.S.2    Pilla, D.M.3    Yamamoto, M.4    Coers, J.5
  • 133
    • 84949652170 scopus 로고    scopus 로고
    • Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages
    • Finethy, R. et al. Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages. Infect. Immun. 83, 4740-4749 (2015).
    • (2015) Infect. Immun. , vol.83 , pp. 4740-4749
    • Finethy, R.1
  • 134
    • 84879547102 scopus 로고    scopus 로고
    • IRG and GBP host resistance factors target aberrant "non-self" vacuoles characterized by the missing of "self" IRGM proteins
    • Haldar, A. K. et al. IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins. PLoS Pathog. 9, e1003414 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003414
    • Haldar, A.K.1
  • 135
    • 64049095824 scopus 로고    scopus 로고
    • A protein secreted by the respiratory pathogen Chlamydia pneumoniae impairs IL-17 signalling via interaction with human Act1
    • Wolf, K., Plano, G. V. & Fields, K. A. A protein secreted by the respiratory pathogen Chlamydia pneumoniae impairs IL-17 signalling via interaction with human Act1. Cell. Microbiol. 11, 769-779 (2009).
    • (2009) Cell. Microbiol. , vol.11 , pp. 769-779
    • Wolf, K.1    Plano, G.V.2    Fields, K.A.3
  • 136
    • 83455258112 scopus 로고    scopus 로고
    • Chlamydia trachomatis disturbs epithelial tissue homeostasis in fallopian tubes via paracrine Wnt signaling
    • Kessler, M. et al. Chlamydia trachomatis disturbs epithelial tissue homeostasis in fallopian tubes via paracrine Wnt signaling. Am. J. Pathol. 180, 186-198 (2012).
    • (2012) Am. J. Pathol. , vol.180 , pp. 186-198
    • Kessler, M.1
  • 137
    • 77955637905 scopus 로고    scopus 로고
    • Histone methylation by NUE, a novel nuclear effector of the intracellular pathogen Chlamydia trachomatis
    • Pennini, M. E., Perrinet, S., Dautry-Varsat, A. & Subtil, A. Histone methylation by NUE, a novel nuclear effector of the intracellular pathogen Chlamydia trachomatis. PLoS Pathog. 6, e1000995 (2010).
    • (2010) PLoS Pathog. , vol.6 , pp. e1000995
    • Pennini, M.E.1    Perrinet, S.2    Dautry-Varsat, A.3    Subtil, A.4
  • 138
    • 84892566227 scopus 로고    scopus 로고
    • Chlamydia trachomatis-induced alterations in the host cell proteome are required for intracellular growth
    • Olive, A. J. et al. Chlamydia trachomatis-induced alterations in the host cell proteome are required for intracellular growth. Cell Host Microbe 15, 113-124 (2014).
    • (2014) Cell Host Microbe , vol.15 , pp. 113-124
    • Olive, A.J.1
  • 139
    • 84887606445 scopus 로고    scopus 로고
    • The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
    • Furtado, A. R. et al. The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52. Cell. Microbiol. 15, 2064-2079 (2013).
    • (2013) Cell. Microbiol. , vol.15 , pp. 2064-2079
    • Furtado, A.R.1
  • 140
    • 33745186215 scopus 로고    scopus 로고
    • Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection
    • Misaghi, S. et al. Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection. Mol. Microbiol. 61, 142-150 (2006).
    • (2006) Mol. Microbiol. , vol.61 , pp. 142-150
    • Misaghi, S.1
  • 141
    • 84873429590 scopus 로고    scopus 로고
    • Catch-and-release probes applied to semi-intact cells reveal ubiquitin-specific protease expression in Chlamydia trachomatis infection
    • Claessen, J. H. et al. Catch-and-release probes applied to semi-intact cells reveal ubiquitin-specific protease expression in Chlamydia trachomatis infection. Chembiochem 14, 343-352 (2013).
    • (2013) Chembiochem , vol.14 , pp. 343-352
    • Claessen, J.H.1
  • 142
    • 84889094466 scopus 로고    scopus 로고
    • A path forward for the chlamydial virulence factor CPAF
    • Conrad, T., Yang, Z., Ojcius, D. & Zhong, G. A path forward for the chlamydial virulence factor CPAF. Microbes Infect. 15, 1026-1032 (2013).
    • (2013) Microbes Infect. , vol.15 , pp. 1026-1032
    • Conrad, T.1    Yang, Z.2    Ojcius, D.3    Zhong, G.4
  • 143
    • 84943608694 scopus 로고    scopus 로고
    • Induction and inhibition of CPAF activity during analysis of Chlamydia-infected cells
    • Johnson, K. A., Lee, J. K., Chen, A. L., Tan, M. & Sutterlin, C. Induction and inhibition of CPAF activity during analysis of Chlamydia-infected cells. Pathog. Dis. 73, 1-8 (2015).
    • (2015) Pathog. Dis. , vol.73 , pp. 1-8
    • Johnson, K.A.1    Lee, J.K.2    Chen, A.L.3    Tan, M.4    Sutterlin, C.5
  • 144
    • 84908203944 scopus 로고    scopus 로고
    • The Chlamydia protease CPAF: Caution, precautions and function
    • Tan, M. & Sutterlin, C. The Chlamydia protease CPAF: caution, precautions and function. Pathog. Dis. 72, 7-9 (2014).
    • (2014) Pathog. Dis. , vol.72 , pp. 7-9
    • Tan, M.1    Sutterlin, C.2
  • 145
    • 84904906405 scopus 로고    scopus 로고
    • Golgi fragmentation and sphingomyelin transport to Chlamydia trachomatis during penicillin-induced persistence do not depend on the cytosolic presence of the chlamydial protease CPAF
    • Dille, S. et al. Golgi fragmentation and sphingomyelin transport to Chlamydia trachomatis during penicillin-induced persistence do not depend on the cytosolic presence of the chlamydial protease CPAF. PLoS ONE 9, e103220 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e103220
    • Dille, S.1
  • 146
    • 84962197484 scopus 로고    scopus 로고
    • A coming of age story: Chlamydia in the post-genetic era
    • Hooppaw, A. J. & Fisher, D. J. A coming of age story: Chlamydia in the post-genetic era. Infect. Immun. 84, 612-621 (2015).
    • (2015) Infect. Immun. , vol.84 , pp. 612-621
    • Hooppaw, A.J.1    Fisher, D.J.2
  • 147
    • 81555198357 scopus 로고    scopus 로고
    • Innate immune mediator profiles and their regulation in a novel polarized immortalized epithelial cell model derived from human endocervix
    • Buckner, L. R. et al. Innate immune mediator profiles and their regulation in a novel polarized immortalized epithelial cell model derived from human endocervix. J. Reprod. Immunol. 92, 8-20 (2011).
    • (2011) J. Reprod. Immunol. , vol.92 , pp. 8-20
    • Buckner, L.R.1
  • 148
    • 79960386252 scopus 로고    scopus 로고
    • The multifaceted role of oestrogen in enhancing Chlamydia trachomatis infection in polarized human endometrial epithelial cells
    • Hall, J. V. et al. The multifaceted role of oestrogen in enhancing Chlamydia trachomatis infection in polarized human endometrial epithelial cells. Cell. Microbiol. 13, 1183-1199 (2011).
    • (2011) Cell. Microbiol. , vol.13 , pp. 1183-1199
    • Hall, J.V.1
  • 149
    • 84962564337 scopus 로고    scopus 로고
    • Progesterone antagonizes the positive influence of estrogen on Chlamydia trachomatis serovar e in an Ishikawa/SHT-290 co-culture model
    • Kintner, J., Schoborg, R. V., Wyrick, P. B. & Hall, J. V. Progesterone antagonizes the positive influence of estrogen on Chlamydia trachomatis serovar E in an Ishikawa/SHT-290 co-culture model. Pathog. Dis. 73, ftv015 (2015).
    • (2015) Pathog. Dis. , vol.73 , pp. ftv015
    • Kintner, J.1    Schoborg, R.V.2    Wyrick, P.B.3    Hall, J.V.4
  • 150
    • 84890841831 scopus 로고    scopus 로고
    • New frontiers in type III secretion biology: The Chlamydia perspective
    • Mueller, K. E., Plano, G. V. & Fields, K. A. New frontiers in type III secretion biology: the Chlamydia perspective. Infect. Immun. 82, 2-9 (2014).
    • (2014) Infect. Immun. , vol.82 , pp. 2-9
    • Mueller, K.E.1    Plano, G.V.2    Fields, K.A.3
  • 151
    • 79951553486 scopus 로고    scopus 로고
    • Multi-genome identification and characterization of Chlamydiae-specific type III secretion substrates: The Inc proteins
    • Dehoux, P., Flores, R., Dauga, C., Zhong, G. & Subtil, A. Multi-genome identification and characterization of Chlamydiae-specific type III secretion substrates: the Inc proteins. BMC Genomics 12, 109 (2011).
    • (2011) BMC Genomics , vol.12 , pp. 109
    • Dehoux, P.1    Flores, R.2    Dauga, C.3    Zhong, G.4    Subtil, A.5
  • 152
    • 84858113031 scopus 로고    scopus 로고
    • Evolution and conservation of predicted inclusion membrane proteins in Chlamydiae
    • Lutter, E. I., Martens, C. & Hackstadt, T. Evolution and conservation of predicted inclusion membrane proteins in Chlamydiae. Comp. Funct. Genomics 2012, 362104 (2012).
    • (2012) Comp. Funct. Genomics 2012 , pp. 362104
    • Lutter, E.I.1    Martens, C.2    Hackstadt, T.3
  • 153
    • 84877866393 scopus 로고    scopus 로고
    • Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis
    • Mital, J., Miller, N. J., Dorward, D. W., Dooley, C. A. & Hackstadt, T. Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. PLoS ONE 8, e63426 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e63426
    • Mital, J.1    Miller, N.J.2    Dorward, D.W.3    Dooley, C.A.4    Hackstadt, T.5
  • 155
    • 0028021272 scopus 로고
    • Expression of recombinant DNA introduced into Chlamydia trachomatis by electroporation
    • Tam, J. E., Davis, C. H. & Wyrick, P. B. Expression of recombinant DNA introduced into Chlamydia trachomatis by electroporation. Can. J. Microbiol. 40, 583-591 (1994).
    • (1994) Can. J. Microbiol. , vol.40 , pp. 583-591
    • Tam, J.E.1    Davis, C.H.2    Wyrick, P.B.3
  • 156
    • 58549091374 scopus 로고    scopus 로고
    • Transformation and isolation of allelic exchange mutants of Chlamydia psittaci using recombinant DNA introduced by electroporation
    • Binet, R. & Maurelli, A. T. Transformation and isolation of allelic exchange mutants of Chlamydia psittaci using recombinant DNA introduced by electroporation. Proc. Natl Acad. Sci. USA 106, 292-297 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 292-297
    • Binet, R.1    Maurelli, A.T.2
  • 157
    • 80053440375 scopus 로고    scopus 로고
    • Development of a transformation system for Chlamydia trachomatis: Restoration of glycogen biosynthesis by acquisition of a plasmid shuttle vector
    • Wang, Y. et al. Development of a transformation system for Chlamydia trachomatis: restoration of glycogen biosynthesis by acquisition of a plasmid shuttle vector. PLoS Pathog. 7, e1002258 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1002258
    • Wang, Y.1
  • 158
    • 84885053267 scopus 로고    scopus 로고
    • Conditional gene expression in Chlamydia trachomatis using the tet system
    • Wickstrum, J., Sammons, L. R., Restivo, K. N. & Hefty, P. S. Conditional gene expression in Chlamydia trachomatis using the tet system. PLoS ONE 8, e76743 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e76743
    • Wickstrum, J.1    Sammons, L.R.2    Restivo, K.N.3    Hefty, P.S.4
  • 159
    • 84874132591 scopus 로고    scopus 로고
    • C. Trachomatis cloning vector and the generation of C. Trachomatis strains expressing fluorescent proteins under the control of a C. Trachomatis promoter
    • Agaisse, H. & Derre, I. A. C. trachomatis cloning vector and the generation of C. trachomatis strains expressing fluorescent proteins under the control of a C. trachomatis promoter. PLoS ONE 8, e57090 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e57090
    • Agaisse, H.1    Derre, I.A.2
  • 160
    • 84895733039 scopus 로고    scopus 로고
    • Expression and targeting of secreted proteins from Chlamydia trachomatis
    • Bauler, L. D. & Hackstadt, T. Expression and targeting of secreted proteins from Chlamydia trachomatis. J. Bacteriol. 196, 1325-1334 (2014).
    • (2014) J. Bacteriol. , vol.196 , pp. 1325-1334
    • Bauler, L.D.1    Hackstadt, T.2
  • 161
    • 84949638685 scopus 로고    scopus 로고
    • Expression and localization of predicted inclusion membrane proteins in Chlamydia trachomatis
    • Weber, M. M., Bauler, L. D., Lam, J. & Hackstadt, T. Expression and localization of predicted inclusion membrane proteins in Chlamydia trachomatis. Infect. Immun. 83, 4710-4718 (2015).
    • (2015) Infect. Immun. , vol.83 , pp. 4710-4718
    • Weber, M.M.1    Bauler, L.D.2    Lam, J.3    Hackstadt, T.4
  • 162
    • 84942626926 scopus 로고    scopus 로고
    • Application of β-lactamase reporter fusions as an indicator of effector protein secretion during infections with the obligate intracellular pathogen Chlamydia trachomatis
    • Mueller, K. E. & Fields, K. A. Application of β-lactamase reporter fusions as an indicator of effector protein secretion during infections with the obligate intracellular pathogen Chlamydia trachomatis. PLoS ONE 10, e0135295 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0135295
    • Mueller, K.E.1    Fields, K.A.2
  • 163
    • 84856372043 scopus 로고    scopus 로고
    • Virulence determinants in the obligate intracellular pathogen Chlamydia trachomatis revealed by forward genetic approaches
    • Nguyen, B. D. & Valdivia, R. H. Virulence determinants in the obligate intracellular pathogen Chlamydia trachomatis revealed by forward genetic approaches. Proc. Natl Acad. Sci. USA 109, 1263-1268 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 1263-1268
    • Nguyen, B.D.1    Valdivia, R.H.2
  • 164
    • 33846592804 scopus 로고    scopus 로고
    • Lateral gene transfer in vitro in the intracellular pathogen Chlamydia trachomatis
    • Demars, R., Weinfurter, J., Guex, E., Lin, J. & Potucek, Y. Lateral gene transfer in vitro in the intracellular pathogen Chlamydia trachomatis. J. Bacteriol. 189, 991-1003 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 991-1003
    • Demars, R.1    Weinfurter, J.2    Guex, E.3    Lin, J.4    Potucek, Y.5
  • 165
    • 84930989055 scopus 로고    scopus 로고
    • Mutational analysis of the Chlamydia muridarum plasticity zone
    • Rajaram, K. et al. Mutational analysis of the Chlamydia muridarum plasticity zone. Infect. Immun. 83, 2870-2881 (2015).
    • (2015) Infect. Immun. , vol.83 , pp. 2870-2881
    • Rajaram, K.1
  • 166
    • 84896728925 scopus 로고    scopus 로고
    • Site-specific insertional inactivation of incA in Chlamydia trachomatis using a group II intron
    • Johnson, C. M. & Fisher, D. J. Site-specific, insertional inactivation of incA in Chlamydia trachomatis using a group II intron. PLoS ONE 8, e83989 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e83989
    • Johnson, C.M.1    Fisher, D.J.2
  • 167
    • 79955570483 scopus 로고    scopus 로고
    • Generation of targeted Chlamydia trachomatis null mutants
    • Kari, L. et al. Generation of targeted Chlamydia trachomatis null mutants. Proc. Natl Acad. Sci. USA 108, 7189-7193 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7189-7193
    • Kari, L.1
  • 168
    • 84928215881 scopus 로고    scopus 로고
    • The role of peptidoglycan in chlamydial cell division: Towards resolving the chlamydial anomaly
    • Jacquier, N., Viollier, P. H. & Greub, G. The role of peptidoglycan in chlamydial cell division: towards resolving the chlamydial anomaly. FEMS Microbiol. Rev. 39, 262-275 (2015).
    • (2015) FEMS Microbiol. Rev. , vol.39 , pp. 262-275
    • Jacquier, N.1    Viollier, P.H.2    Greub, G.3
  • 169
    • 84890205605 scopus 로고    scopus 로고
    • Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ
    • Pilhofer, M. et al. Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ. Nat. Commun. 4, 2856 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2856
    • Pilhofer, M.1
  • 170
    • 84896708374 scopus 로고    scopus 로고
    • A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis
    • Liechti, G. W. et al. A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis. Nature 506, 507-510 (2014).
    • (2014) Nature , vol.506 , pp. 507-510
    • Liechti, G.W.1
  • 171
    • 84905189777 scopus 로고    scopus 로고
    • Analysis of MreB interactors in Chlamydia reveals a RodZ homolog but fails to detect an interaction with MraY
    • Ouellette, S. P. et al. Analysis of MreB interactors in Chlamydia reveals a RodZ homolog but fails to detect an interaction with MraY. Front. Microbiol. 5, 279 (2014).
    • (2014) Front. Microbiol. , vol.5 , pp. 279
    • Ouellette, S.P.1
  • 172
    • 84924719513 scopus 로고    scopus 로고
    • Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB
    • Kemege, K. E. et al. Chlamydia trachomatis protein CT009 is a structural and functional homolog to the key morphogenesis component RodZ and interacts with division septal plane localized MreB. Mol. Microbiol. 95, 365-382 (2015).
    • (2015) Mol. Microbiol. , vol.95 , pp. 365-382
    • Kemege, K.E.1
  • 173
    • 84903220304 scopus 로고    scopus 로고
    • Cell wall precursors are required to organize the chlamydial division septum
    • Jacquier, N., Frandi, A., Pillonel, T., Viollier, P. H. & Greub, G. Cell wall precursors are required to organize the chlamydial division septum. Nat. Commun. 5, 3578 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 3578
    • Jacquier, N.1    Frandi, A.2    Pillonel, T.3    Viollier, P.H.4    Greub, G.5
  • 174
    • 84941696043 scopus 로고    scopus 로고
    • Structural characterization of muropeptides from Chlamydia trachomatis peptidoglycan by mass spectrometry resolves "chlamydial anomaly"
    • Packiam, M., Weinrick, B., Jacobs, W. R. & Maurelli, A. T. Structural characterization of muropeptides from Chlamydia trachomatis peptidoglycan by mass spectrometry resolves "chlamydial anomaly". Proc. Nat. Acad. Sci. USA 112, 11660-11665 (2015).
    • (2015) Proc. Nat. Acad. Sci. USA , vol.112 , pp. 11660-11665
    • Packiam, M.1    Weinrick, B.2    Jacobs, W.R.3    Maurelli, A.T.4
  • 175
    • 84903127194 scopus 로고    scopus 로고
    • AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae
    • Klockner, A. et al. AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae. Nat. Commun. 5, 4201 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4201
    • Klockner, A.1
  • 176
    • 84903216873 scopus 로고    scopus 로고
    • FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens
    • Frandi, A., Jacquier, N., Theraulaz, L., Greub, G. & Viollier, P. H. FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens. Nat. Commun. 5, 4200 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4200
    • Frandi, A.1    Jacquier, N.2    Theraulaz, L.3    Greub, G.4    Viollier, P.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.