메뉴 건너뛰기




Volumn 8, Issue 1, 2005, Pages 92-98

Bacterial interactions with the eukaryotic secretory pathway

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; LIPID;

EID: 13444280123     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2004.12.007     Document Type: Review
Times cited : (56)

References (70)
  • 1
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • E.A. Miller, T.H. Beilharz, P.N. Malkus, M.C. Lee, S. Hamamoto, L. Orci, and R. Schekman Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles Cell 114 2003 497 509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 2
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • E. Mossessova, L.C. Bickford, and J. Goldberg SNARE selectivity of the COPII coat Cell 114 2003 483 495
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 3
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • R. Garcia-Mata, T. Szul, C. Alvarez, and E. Sztul ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1 Mol Biol Cell 14 2003 2250 2261
    • (2003) Mol Biol Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 5
    • 0031464540 scopus 로고    scopus 로고
    • The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1
    • T. Aoe, E. Cukierman, A. Lee, D. Cassel, P.J. Peters, and V.W. Hsu The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1 EMBO J 16 1997 7305 7316
    • (1997) EMBO J , vol.16 , pp. 7305-7316
    • Aoe, T.1    Cukierman, E.2    Lee, A.3    Cassel, D.4    Peters, P.J.5    Hsu, V.W.6
  • 6
    • 2442717709 scopus 로고    scopus 로고
    • Domains of the TGN: Coats, tethers and G proteins
    • P.A. Gleeson, J.G. Lock, M.R. Luke, and J.L. Stow Domains of the TGN: coats, tethers and G proteins Traffic 5 2004 315 326
    • (2004) Traffic , vol.5 , pp. 315-326
    • Gleeson, P.A.1    Lock, J.G.2    Luke, M.R.3    Stow, J.L.4
  • 8
    • 0025012987 scopus 로고
    • Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity
    • V.K. Chaudhary, Y. Jinno, D. FitzGerald, and I. Pastan Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity Proc Natl Acad Sci USA 87 1990 308 312
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 308-312
    • Chaudhary, V.K.1    Jinno, Y.2    Fitzgerald, D.3    Pastan, I.4
  • 10
    • 0032969203 scopus 로고    scopus 로고
    • The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum
    • M.E. Jackson, J.C. Simpson, A. Girod, R. Pepperkok, L.M. Roberts, and J.M. Lord The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum J Cell Sci 112 1999 467 475
    • (1999) J Cell Sci , vol.112 , pp. 467-475
    • Jackson, M.E.1    Simpson, J.C.2    Girod, A.3    Pepperkok, R.4    Roberts, L.M.5    Lord, J.M.6
  • 12
    • 4344571004 scopus 로고    scopus 로고
    • Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells
    • Y. Feng, A.P. Jadhav, C. Rodighiero, Y. Fujinaga, T. Kirchhausen, and W.I. Lencer Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells EMBO Rep 5 2004 596 601
    • (2004) EMBO Rep , vol.5 , pp. 596-601
    • Feng, Y.1    Jadhav, A.P.2    Rodighiero, C.3    Fujinaga, Y.4    Kirchhausen, T.5    Lencer, W.I.6
  • 15
    • 0036887054 scopus 로고    scopus 로고
    • Intracellular localization modulates targeting of ExoS, a type III cytotoxin, to eukaryotic signalling proteins
    • K.J. Pederson, R. Krall, M.J. Riese, and J.T. Barbieri Intracellular localization modulates targeting of ExoS, a type III cytotoxin, to eukaryotic signalling proteins Mol Microbiol 46 2002 1381 1390
    • (2002) Mol Microbiol , vol.46 , pp. 1381-1390
    • Pederson, K.J.1    Krall, R.2    Riese, M.J.3    Barbieri, J.T.4
  • 16
    • 12144290330 scopus 로고    scopus 로고
    • Identification and characterization of NleA, a non-LEE-encoded type III translocated virulence factor of enterohaemorrhagic Escherichia coli O157:H7
    • S. Gruenheid, I. Sekirov, N.A. Thomas, W. Deng, P. O'Donnell, D. Goode, Y. Li, E.A. Frey, N.F. Brown, and P. Metalnikov Identification and characterization of NleA, a non-LEE-encoded type III translocated virulence factor of enterohaemorrhagic Escherichia coli O157:H7 Mol Microbiol 51 2004 1233 1249 The authors identify a new effector of the TTSS of enterohaemorrhagic E. coli and Citrobacter, which, after translocation into host epithelial cells, targets the Golgi network.
    • (2004) Mol Microbiol , vol.51 , pp. 1233-1249
    • Gruenheid, S.1    Sekirov, I.2    Thomas, N.A.3    Deng, W.4    O'Donnell, P.5    Goode, D.6    Li, Y.7    Frey, E.A.8    Brown, N.F.9    Metalnikov, P.10
  • 17
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • E. Gagnon, S. Duclos, C. Rondeau, E. Chevet, P.H. Cameron, O. Steele-Mortimer, J. Paiement, J.J. Bergeron, and M. Desjardins Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages Cell 110 2002 119 131 The study demonstrates the presence of ER membranes during the formation of macrophage phagosomes after uptake of either latex beads or different pathogens.
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, E.1    Duclos, S.2    Rondeau, C.3    Chevet, E.4    Cameron, P.H.5    Steele-Mortimer, O.6    Paiement, J.7    Bergeron, J.J.8    Desjardins, M.9
  • 18
    • 0035691622 scopus 로고    scopus 로고
    • How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: Implications for conversion of plasma membrane to the ER membrane
    • L.G. Tilney, O.S. Harb, P.S. Connelly, C.G. Robinson, and C.R. Roy How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane J Cell Sci 114 2001 4637 4650
    • (2001) J Cell Sci , vol.114 , pp. 4637-4650
    • Tilney, L.G.1    Harb, O.S.2    Connelly, P.S.3    Robinson, C.G.4    Roy, C.R.5
  • 19
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • J.C. Kagan, and C.R. Roy Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites Nat Cell Biol 4 2002 945 954
    • (2002) Nat Cell Biol , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 20
    • 0031971194 scopus 로고    scopus 로고
    • Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake
    • C.R. Roy, K.H. Berger, and R.R. Isberg Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake Mol Microbiol 28 1998 663 674
    • (1998) Mol Microbiol , vol.28 , pp. 663-674
    • Roy, C.R.1    Berger, K.H.2    Isberg, R.R.3
  • 21
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • H. Nagai, J.C. Kagan, X. Zhu, R.A. Kahn, and C.R. Roy A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes Science 295 2002 679 682 The authors show that RalF, a Legionella effector protein translocated by the Dot/Icm type IV secretion system acts as an exchange factor for Arf1, which is recruited to the Legionella-containing vacuole.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 22
    • 0038349211 scopus 로고    scopus 로고
    • The Legionella pneumophila LidA protein: A translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity
    • G.M. Conover, I. Derre, J.P. Vogel, and R.R. Isberg The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity Mol Microbiol 48 2003 305 321
    • (2003) Mol Microbiol , vol.48 , pp. 305-321
    • Conover, G.M.1    Derre, I.2    Vogel, J.P.3    Isberg, R.R.4
  • 24
    • 1642514882 scopus 로고    scopus 로고
    • Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer
    • Z.Q. Luo, and R.R. Isberg Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer Proc Natl Acad Sci USA 101 2004 841 846 The authors describe an elegant screen for candidate effectors secreted by the Legionella Dot/Icm type IV secretion system.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 841-846
    • Luo, Z.Q.1    Isberg, R.R.2
  • 25
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle
    • J.C. Kagan, M.P. Stein, M. Pypaert, and C.R. Roy Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle J Exp Med 199 2004 1201 1211 This work shows that the recruitment of Rab1 and the host SNARE Sec22 to Legionella-containing vacuoles is necessary for the establishment of the ER-derived replicative organelle.
    • (2004) J Exp Med , vol.199 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 26
    • 0022449073 scopus 로고
    • Ultrastructural morphometric analysis of Brucella abortus-infected trophoblasts in experimental placentitis. Bacterial replication occurs in rough endoplasmic reticulum
    • T.D. Anderson, and N.F. Cheville Ultrastructural morphometric analysis of Brucella abortus-infected trophoblasts in experimental placentitis. Bacterial replication occurs in rough endoplasmic reticulum Am J Pathol 124 1986 226 237
    • (1986) Am J Pathol , vol.124 , pp. 226-237
    • Anderson, T.D.1    Cheville, N.F.2
  • 27
    • 0025352188 scopus 로고
    • Penetration and intracellular growth of Brucella abortus in nonphagocytic cells in vitro
    • P.G. Detilleux, B.L. Deyoe, and N.F. Cheville Penetration and intracellular growth of Brucella abortus in nonphagocytic cells in vitro Infect Immun 58 1990 2320 2328
    • (1990) Infect Immun , vol.58 , pp. 2320-2328
    • Detilleux, P.G.1    Deyoe, B.L.2    Cheville, N.F.3
  • 31
    • 0041920932 scopus 로고    scopus 로고
    • Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum
    • J. Celli, C. de Chastellier, D.M. Franchini, J. Pizarro-Cerda, E. Moreno, and J.P. Gorvel Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum J Exp Med 198 2003 545 556 This study characterises the nature of the Brucella-containing vacuole in primary macrophages and demonstrates a role for the VirB type IV secretion system for establishment of an ER-derived organelle.
    • (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
  • 32
    • 0035079679 scopus 로고    scopus 로고
    • Essential role of the VirB machinery in the maturation of the Brucella abortus-containing vacuole
    • D.J. Comerci, M.J. Martinez-Lorenzo, R. Sieira, J.P. Gorvel, and R.A. Ugalde Essential role of the VirB machinery in the maturation of the Brucella abortus-containing vacuole Cell Microbiol 3 2001 159 168
    • (2001) Cell Microbiol , vol.3 , pp. 159-168
    • Comerci, D.J.1    Martinez-Lorenzo, M.J.2    Sieira, R.3    Gorvel, J.P.4    Ugalde, R.A.5
  • 33
    • 0029807058 scopus 로고    scopus 로고
    • Vesicular interactions of the Chlamydia trachomatis inclusion are determined by chlamydial early protein synthesis rather than route of entry
    • M.A. Scidmore, D.D. Rockey, E.R. Fischer, R.A. Heinzen, and T. Hackstadt Vesicular interactions of the Chlamydia trachomatis inclusion are determined by chlamydial early protein synthesis rather than route of entry Infect Immun 64 1996 5366 5372
    • (1996) Infect Immun , vol.64 , pp. 5366-5372
    • Scidmore, M.A.1    Rockey, D.D.2    Fischer, E.R.3    Heinzen, R.A.4    Hackstadt, T.5
  • 34
    • 0037305123 scopus 로고    scopus 로고
    • Restricted fusion of Chlamydia trachomatis vesicles with endocytic compartments during the initial stages of infection
    • M.A. Scidmore, E.R. Fischer, and T. Hackstadt Restricted fusion of Chlamydia trachomatis vesicles with endocytic compartments during the initial stages of infection Infect Immun 71 2003 973 984
    • (2003) Infect Immun , vol.71 , pp. 973-984
    • Scidmore, M.A.1    Fischer, E.R.2    Hackstadt, T.3
  • 35
    • 0029034043 scopus 로고
    • Lipid metabolism in Chlamydia trachomatis-infected cells: Directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion
    • T. Hackstadt, M.A. Scidmore, and D.D. Rockey Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion Proc Natl Acad Sci USA 92 1995 4877 4881
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4877-4881
    • Hackstadt, T.1    Scidmore, M.A.2    Rockey, D.D.3
  • 36
    • 0035079677 scopus 로고    scopus 로고
    • Sphingomyelin trafficking in Chlamydia pneumoniae-infected cells
    • K. Wolf, and T. Hackstadt Sphingomyelin trafficking in Chlamydia pneumoniae-infected cells Cell Microbiol 3 2001 145 152
    • (2001) Cell Microbiol , vol.3 , pp. 145-152
    • Wolf, K.1    Hackstadt, T.2
  • 37
    • 0034526766 scopus 로고    scopus 로고
    • Host cell-derived sphingolipids are required for the intracellular growth of Chlamydia trachomatis
    • C. van Ooij, L. Kalman, I. van, M. Nishijima, K. Hanada, K. Mostov, and J.N. Engel Host cell-derived sphingolipids are required for the intracellular growth of Chlamydia trachomatis Cell Microbiol 2 2000 627 637
    • (2000) Cell Microbiol , vol.2 , pp. 627-637
    • Van Ooij, C.1    Kalman, L.2    Van, I.3    Nishijima, M.4    Hanada, K.5    Mostov, K.6    Engel, J.N.7
  • 38
    • 0037974695 scopus 로고    scopus 로고
    • Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion
    • R.A. Carabeo, D.J. Mead, and T. Hackstadt Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion Proc Natl Acad Sci USA 100 2003 6771 6776 This paper provides evidence that Chlamydia inclusions acquire cholesterol directly from the Golgi network through a bacterially driven process.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6771-6776
    • Carabeo, R.A.1    Mead, D.J.2    Hackstadt, T.3
  • 39
    • 0141613752 scopus 로고    scopus 로고
    • Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process
    • S.S. Grieshaber, N.A. Grieshaber, and T. Hackstadt Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process J Cell Sci 116 2003 3793 3802 Molecular motors are shown to be involved in the movement of a bacterial inclusion to the perinuclear region.
    • (2003) J Cell Sci , vol.116 , pp. 3793-3802
    • Grieshaber, S.S.1    Grieshaber, N.A.2    Hackstadt, T.3
  • 41
    • 0035131373 scopus 로고    scopus 로고
    • Secretion of predicted Inc proteins of Chlamydia pneumoniae by a heterologous type III machinery
    • A. Subtil, C. Parsot, and A. Dautry-Varsat 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
  • 42
    • 0038011417 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion: Evidence for a functional apparatus during early-cycle development
    • K.A. Fields, D.J. Mead, C.A. Dooley, and T. Hackstadt 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
  • 43
    • 0141669008 scopus 로고    scopus 로고
    • Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner
    • K.A. Rzomp, L.D. Scholtes, B.J. Briggs, G.R. Whittaker, and M.A. Scidmore 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
  • 44
    • 0035675043 scopus 로고    scopus 로고
    • Salmonella entry into host cells: The work in concert of type III-secreted effector proteins
    • D. Zhou, and J. Galán Salmonella entry into host cells: the work in concert of type III-secreted effector proteins Microbes Infect 3 2001 1293 1298
    • (2001) Microbes Infect , vol.3 , pp. 1293-1298
    • Zhou, D.1    Galán, J.2
  • 45
    • 0036161224 scopus 로고    scopus 로고
    • The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells
    • O. Steele-Mortimer, J.H. Brumell, L.A. Knodler, S. Meresse, A. Lopez, and B.B. Finlay The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells Cell Microbiol 4 2002 43 54
    • (2002) Cell Microbiol , vol.4 , pp. 43-54
    • Steele-Mortimer, O.1    Brumell, J.H.2    Knodler, L.A.3    Meresse, S.4    Lopez, A.5    Finlay, B.B.6
  • 46
    • 0036112327 scopus 로고    scopus 로고
    • Trafficking of the Salmonella vacuole in macrophages
    • D.W. Holden Trafficking of the Salmonella vacuole in macrophages Traffic 3 2002 161 169
    • (2002) Traffic , vol.3 , pp. 161-169
    • Holden, D.W.1
  • 47
    • 0042357064 scopus 로고    scopus 로고
    • Taking possession: Biogenesis of the Salmonella-containing vacuole
    • L.A. Knodler, and O. Steele-Mortimer Taking possession: biogenesis of the Salmonella-containing vacuole Traffic 4 2003 587 599
    • (2003) Traffic , vol.4 , pp. 587-599
    • Knodler, L.A.1    Steele-Mortimer, O.2
  • 48
    • 0242485924 scopus 로고    scopus 로고
    • The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells
    • S. Méresse, O. Steele-Mortimer, B.B. Finlay, and J.P. Gorvel The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells EMBO J 18 1999 4394 4403
    • (1999) EMBO J , vol.18 , pp. 4394-4403
    • Méresse, S.1    Steele-Mortimer, O.2    Finlay, B.B.3    Gorvel, J.P.4
  • 49
    • 0033157323 scopus 로고    scopus 로고
    • Biogenesis of Salmonella typhimurium-containing vacuoles in epithelial cells involves interactions with the early endocytic pathway
    • O. Steele-Mortimer, S. Meresse, J.P. Gorvel, B.H. Toh, and B.B. Finlay Biogenesis of Salmonella typhimurium-containing vacuoles in epithelial cells involves interactions with the early endocytic pathway Cell Microbiol 1 1999 33 49
    • (1999) Cell Microbiol , vol.1 , pp. 33-49
    • Steele-Mortimer, O.1    Meresse, S.2    Gorvel, J.P.3    Toh, B.H.4    Finlay, B.B.5
  • 50
    • 0028941255 scopus 로고
    • Targeting of Salmonella typhimurium to vesicles containing lysosomal membrane glycoproteins bypasses compartments with mannose 6-phosphate receptors
    • F. Garcia-del Portillo, and B.B. Finlay Targeting of Salmonella typhimurium to vesicles containing lysosomal membrane glycoproteins bypasses compartments with mannose 6-phosphate receptors J Cell Biol 129 1995 81 97
    • (1995) J Cell Biol , vol.129 , pp. 81-97
    • Garcia-Del Portillo, F.1    Finlay, B.B.2
  • 51
    • 0030911922 scopus 로고    scopus 로고
    • The unique trafficking pattern of Salmonella typhimurium-containing phagosomes in murine macrophages is independent of the mechanism of bacterial entry
    • M. Rathman, L.P. Barker, and S. Falkow The unique trafficking pattern of Salmonella typhimurium-containing phagosomes in murine macrophages is independent of the mechanism of bacterial entry Infect Immun 65 1997 1475 1485
    • (1997) Infect Immun , vol.65 , pp. 1475-1485
    • Rathman, M.1    Barker, L.P.2    Falkow, S.3
  • 52
    • 0037066701 scopus 로고    scopus 로고
    • Role of 3-phosphoinositides in the maturation of Salmonella-containing vacuoles within host cells
    • C.C. Scott, P. Cuellar-Mata, T. Matsuo, H.W. Davidson, and S. Grinstein Role of 3-phosphoinositides in the maturation of Salmonella-containing vacuoles within host cells J Biol Chem 277 2002 12770 12776
    • (2002) J Biol Chem , vol.277 , pp. 12770-12776
    • Scott, C.C.1    Cuellar-Mata, P.2    Matsuo, T.3    Davidson, H.W.4    Grinstein, S.5
  • 53
    • 0035166577 scopus 로고    scopus 로고
    • A role for the PhoP/Q regulon in inhibition of fusion between lysosomes and Salmonella-containing vacuoles in macrophages
    • S.G. Garvis, C.R. Beuzón, and D.W. Holden A role for the PhoP/Q regulon in inhibition of fusion between lysosomes and Salmonella-containing vacuoles in macrophages Cell Microbiol 3 2001 731 744
    • (2001) Cell Microbiol , vol.3 , pp. 731-744
    • Garvis, S.G.1    Beuzón, C.R.2    Holden, D.W.3
  • 54
    • 0141642027 scopus 로고    scopus 로고
    • SseG, a virulence protein that targets Salmonella to the Golgi network
    • S.P. Salcedo, and D.W. Holden SseG, a virulence protein that targets Salmonella to the Golgi network EMBO J 22 2003 5003 5014 The study provides evidence that Salmonella interacts with the Golgi network in epithelial cells, and identifies an effector responsible for intracellular positioning of the bacterial microcolony.
    • (2003) EMBO J , vol.22 , pp. 5003-5014
    • Salcedo, S.P.1    Holden, D.W.2
  • 56
    • 2542480782 scopus 로고    scopus 로고
    • Dynein-mediated vesicle transport controls intracellular Salmonella replication
    • M. Marsman, I. Jordens, C. Kuijl, L. Janssen, and J. Neefjes Dynein-mediated vesicle transport controls intracellular Salmonella replication Mol Biol Cell 15 2004 2954 2964
    • (2004) Mol Biol Cell , vol.15 , pp. 2954-2964
    • Marsman, M.1    Jordens, I.2    Kuijl, C.3    Janssen, L.4    Neefjes, J.5
  • 57
    • 1842584706 scopus 로고    scopus 로고
    • Microtubule motors control membrane dynamics of Salmonella-containing vacuoles
    • J. Guignot, E. Caron, C. Beuzon, C. Bucci, J. Kagan, C. Roy, and D.W. Holden Microtubule motors control membrane dynamics of Salmonella-containing vacuoles J Cell Sci 117 2004 1033 1045
    • (2004) J Cell Sci , vol.117 , pp. 1033-1045
    • Guignot, J.1    Caron, E.2    Beuzon, C.3    Bucci, C.4    Kagan, J.5    Roy, C.6    Holden, D.W.7
  • 58
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • G. Cantalupo, P. Alifano, V. Roberti, C.B. Bruni, and C. Bucci Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes EMBO J 20 2001 683 693
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 60
    • 0036915515 scopus 로고    scopus 로고
    • SseF and SseG are translocated effectors of the type III secretion system of Salmonella pathogenicity island 2 that modulate aggregation of endosomal compartments
    • V. Kuhle, and M. Hensel SseF and SseG are translocated effectors of the type III secretion system of Salmonella pathogenicity island 2 that modulate aggregation of endosomal compartments Cell Microbiol 4 2002 813 824
    • (2002) Cell Microbiol , vol.4 , pp. 813-824
    • Kuhle, V.1    Hensel, M.2
  • 61
    • 0027485163 scopus 로고
    • Role of acid tolerance response genes in Salmonella typhimurium virulence
    • F. Garcia-del Portillo, J.W. Foster, and B.B. Finlay Role of acid tolerance response genes in Salmonella typhimurium virulence Infect Immun 61 1993 4489 4492
    • (1993) Infect Immun , vol.61 , pp. 4489-4492
    • Garcia-Del Portillo, F.1    Foster, J.W.2    Finlay, B.B.3
  • 62
    • 0041903802 scopus 로고    scopus 로고
    • Salmonella type III effectors PipB and PipB2 are targeted to detergent-resistant microdomains on internal host cell membranes
    • L.A. Knodler, B.A. Vallance, M. Hensel, D. Jackel, B.B. Finlay, and O. Steele-Mortimer Salmonella type III effectors PipB and PipB2 are targeted to detergent-resistant microdomains on internal host cell membranes Mol Microbiol 49 2003 685 704
    • (2003) Mol Microbiol , vol.49 , pp. 685-704
    • Knodler, L.A.1    Vallance, B.A.2    Hensel, M.3    Jackel, D.4    Finlay, B.B.5    Steele-Mortimer, O.6
  • 63
    • 0036303831 scopus 로고    scopus 로고
    • The Salmonella-containing vacuole is a major site of intracellular cholesterol accumulation and recruits the GPI-anchored protein CD55
    • D.M. Catron, M.D. Sylvester, Y. Lange, M. Kadekoppala, B.D. Jones, D.M. Monack, S. Falkow, and K. Haldar The Salmonella-containing vacuole is a major site of intracellular cholesterol accumulation and recruits the GPI-anchored protein CD55 Cell Microbiol 4 2002 315 328
    • (2002) Cell Microbiol , vol.4 , pp. 315-328
    • Catron, D.M.1    Sylvester, M.D.2    Lange, Y.3    Kadekoppala, M.4    Jones, B.D.5    Monack, D.M.6    Falkow, S.7    Haldar, K.8
  • 64
    • 0036201964 scopus 로고    scopus 로고
    • The Salmonella pathogenicity island 1 secretion system directs cellular cholesterol redistribution during mammalian cell entry and intracellular trafficking
    • M.J. Garner, R.D. Hayward, and V. Koronakis The Salmonella pathogenicity island 1 secretion system directs cellular cholesterol redistribution during mammalian cell entry and intracellular trafficking Cell Microbiol 4 2002 153 165
    • (2002) Cell Microbiol , vol.4 , pp. 153-165
    • Garner, M.J.1    Hayward, R.D.2    Koronakis, V.3
  • 65
    • 0842283056 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium requires nonsterol precursors of the cholesterol biosynthetic pathway for intracellular proliferation
    • D.M. Catron, Y. Lange, J. Borensztajn, M.D. Sylvester, B.D. Jones, and K. Haldar Salmonella enterica serovar Typhimurium requires nonsterol precursors of the cholesterol biosynthetic pathway for intracellular proliferation Infect Immun 72 2004 1036 1042
    • (2004) Infect Immun , vol.72 , pp. 1036-1042
    • Catron, D.M.1    Lange, Y.2    Borensztajn, J.3    Sylvester, M.D.4    Jones, B.D.5    Haldar, K.6
  • 66
    • 8744275514 scopus 로고    scopus 로고
    • Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae
    • C. Delevoye, M. Nilges, A. Dautry-Varsat, and A. Subtil Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae 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
  • 67
    • 85030829554 scopus 로고    scopus 로고
    • The structure of RalF, an Arf guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site
    • In Press, published online ahead of print.
    • Amor JC, Swails J, Roy CR, Nagai H, Ingmundson A, Cheng X and Kahn RA: The structure of RalF, an Arf guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site. J Biol Chem 2004, In Press, published online ahead of print.
    • (2004) J Biol Chem
    • Amor, J.C.1    Swails, J.2    Roy, C.R.3    Nagai, H.4    Ingmundson, A.5    Cheng, X.6    Kahn, R.A.7
  • 68
    • 0031899678 scopus 로고    scopus 로고
    • Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments
    • J. Pizarro-Cerda, E. Moreno, V. Sanguedolce, J.L. Mege, and J.P. Gorvel Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments Infect Immun 66 1998 2387 2392
    • (1998) Infect Immun , vol.66 , pp. 2387-2392
    • Pizarro-Cerda, J.1    Moreno, E.2    Sanguedolce, V.3    Mege, J.L.4    Gorvel, J.P.5
  • 69
    • 0029155737 scopus 로고
    • Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    • M.S. Swanson, and R.R. Isberg Association of Legionella pneumophila with the macrophage endoplasmic reticulum Infect Immun 63 1995 3609 3620
    • (1995) Infect Immun , vol.63 , pp. 3609-3620
    • Swanson, M.S.1    Isberg, R.R.2
  • 70
    • 0347595335 scopus 로고    scopus 로고
    • Macroautophagy is dispensable for intracellular replication of Legionella pneumophila in Dictyostelium discoideum
    • G.P. Otto, M.Y. Wu, M. Clarke, H. Lu, O.R. Anderson, H. Hilbi, H.A. Shuman, and R.H. Kessin Macroautophagy is dispensable for intracellular replication of Legionella pneumophila in Dictyostelium discoideum Mol Microbiol 51 2004 63 72
    • (2004) Mol Microbiol , vol.51 , pp. 63-72
    • Otto, G.P.1    Wu, M.Y.2    Clarke, M.3    Lu, H.4    Anderson, O.R.5    Hilbi, H.6    Shuman, H.A.7    Kessin, R.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.