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Volumn 71, Issue 6, 2003, Pages 3310-3319

Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; PROTEIN ESCC; PROTEIN ESCN; PROTEIN ESCV; SECRETIN; UNCLASSIFIED DRUG;

EID: 0038187635     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.6.3310-3319.2003     Document Type: Article
Times cited : (132)

References (71)
  • 1
  • 2
    • 0037053426 scopus 로고    scopus 로고
    • Intrinsic membrane targeting of the flagellar export ATPase FliI: Interaction with acidic phospholipids and FliH
    • Auvray, F., A. J. Ozin, L. Claret, and C. Hughes. 2002. Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH. J. Mol. Biol. 318:941-950.
    • (2002) J. Mol. Biol. , vol.318 , pp. 941-950
    • Auvray, F.1    Ozin, A.J.2    Claret, L.3    Hughes, C.4
  • 4
    • 0030924763 scopus 로고    scopus 로고
    • Altered localization of HrpZ in Pseudomonas syringae pv. syringae hrp mutants suggests that different components of the type III secretion pathway control protein translocation across the inner and outer membranes of gram-negative bacteria
    • Charkowski, A. O., H. C. Huang, and A. Collmer. 1997. Altered localization of HrpZ in Pseudomonas syringae pv. syringae hrp mutants suggests that different components of the type III secretion pathway control protein translocation across the inner and outer membranes of gram-negative bacteria. J. Bacteriol. 179:3866-3874.
    • (1997) J. Bacteriol. , vol.179 , pp. 3866-3874
    • Charkowski, A.O.1    Huang, H.C.2    Collmer, A.3
  • 5
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago, A. M., and V. Koronakis. 1998. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30:47-56.
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 6
    • 0031777144 scopus 로고    scopus 로고
    • The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG
    • Daefler, S., and M. Russel. 1998. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol. Microbiol. 28:1367-1380.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1367-1380
    • Daefler, S.1    Russel, M.2
  • 9
    • 0034819364 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli infection induces expression of the early growth response factor by activating mitogen-activated protein kinase cascades in epithelial cells
    • de Grado, M., C. M. Rosenberger, A. Gauthier, B. A. Vallance, and B. B. Finlay. 2001. Enteropathogenic Escherichia coli infection induces expression of the early growth response factor by activating mitogen-activated protein kinase cascades in epithelial cells. Infect. Immun. 69:6217-6224.
    • (2001) Infect. Immun. , vol.69 , pp. 6217-6224
    • De Grado, M.1    Rosenberger, C.M.2    Gauthier, A.3    Vallance, B.A.4    Finlay, B.B.5
  • 10
    • 0031960239 scopus 로고    scopus 로고
    • EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein
    • Deibel, C., S. Kramer, T. Chakraborty, and F. Ebel. 1998. EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein. Mol. Microbiol. 28:463-474.
    • (1998) Mol. Microbiol. , vol.28 , pp. 463-474
    • Deibel, C.1    Kramer, S.2    Chakraborty, T.3    Ebel, F.4
  • 12
    • 0032936313 scopus 로고    scopus 로고
    • Cellular locations of Pseudomonas syringae pv. syringae HrcC and HrcJ proteins, required for harpin secretion via the type III pathway
    • Deng, W. L., and H. C. Huang. 1999. Cellular locations of Pseudomonas syringae pv. syringae HrcC and HrcJ proteins, required for harpin secretion via the type III pathway. J. Bacteriol. 181:2298-2301.
    • (1999) J. Bacteriol. , vol.181 , pp. 2298-2301
    • Deng, W.L.1    Huang, H.C.2
  • 13
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg, M. S., and J. B. Kaper. 1991. Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect. Immun. 59:4310-4317.
    • (1991) Infect. Immun. , vol.59 , pp. 4310-4317
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 14
    • 0031696843 scopus 로고    scopus 로고
    • Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages
    • Ebel, F., T. Podzadel, M. Rohde, A. U. Kresse, S. Kramer, C. Deibel, C. A. Guzman, and T. Chakraborty. 1998. Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages. Mol. Microbiol. 30:147-161.
    • (1998) Mol. Microbiol. , vol.30 , pp. 147-161
    • Ebel, F.1    Podzadel, T.2    Rohde, M.3    Kresse, A.U.4    Kramer, S.5    Deibel, C.6    Guzman, C.A.7    Chakraborty, T.8
  • 16
    • 0029730706 scopus 로고    scopus 로고
    • Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhmurium
    • Fan, F., and R. M. Macnab. 1996. Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhmurium. J. Biol. Chem. 271:31981-31988.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31981-31988
    • Fan, F.1    Macnab, R.M.2
  • 17
    • 0015854977 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodiumlauryl sarcosinate
    • Filip, C., G. Fletcher, J. L. Wulff, and C. F. Earhart. 1973. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodiumlauryl sarcosinate. J. Bacteriol. 115:717-722.
    • (1973) J. Bacteriol. , vol.115 , pp. 717-722
    • Filip, C.1    Fletcher, G.2    Wulff, J.L.3    Earhart, C.F.4
  • 18
    • 0033917851 scopus 로고    scopus 로고
    • Mechanical fractionation reveals structural requirements for enteropathogenic Escherichia coli Tir insertion into host membranes
    • Gauthier, A., M. de Grado, and B. B. Finlay. 2000. Mechanical fractionation reveals structural requirements for enteropathogenic Escherichia coli Tir insertion into host membranes. Infect. Immun. 68:4344-4348.
    • (2000) Infect. Immun. , vol.68 , pp. 4344-4348
    • Gauthier, A.1    De Grado, M.2    Finlay, B.B.3
  • 19
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S., and C. A. Boucher. 1994. A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol. Gen. Genet. 243:112-118.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 20
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • Guilvout, I., K. R. Hardie, N. Sauvonnet, and A. P. Pugsley. 1999. Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J. Bacteriol. 181:7212-7220.
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 21
    • 0018074492 scopus 로고
    • Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier
    • Hancock, R. E., and H. Nikaido. 1978. Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J. Bacteriol. 136:381-390.
    • (1978) J. Bacteriol. , vol.136 , pp. 381-390
    • Hancock, R.E.1    Nikaido, H.2
  • 22
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K. R., S. Lory, and A. P. Pugsley. 1996. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15:978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 23
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: Separation of proteolytic protection and piloting functions
    • Hardie, K. R., A. Seydel, I. Guilvout, and A. P. Pugsley. 1996. The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol. Microbiol. 22:967-976.
    • (1996) Mol. Microbiol. , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsley, A.P.4
  • 25
    • 0035860359 scopus 로고    scopus 로고
    • The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase
    • Hirano, T., T. Minamino, and R. M. Macnab. 2001. The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase. J. Mol. Biol. 312:359-369.
    • (2001) J. Mol. Biol. , vol.312 , pp. 359-369
    • Hirano, T.1    Minamino, T.2    Macnab, R.M.3
  • 26
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C. J. 1998. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62:379-433.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 27
    • 0034775390 scopus 로고    scopus 로고
    • Characterization of translocation pores inserted into plasma membranes by type III-secreted Esp proteins of enteropathogenic Escherichia coli
    • Ide, T., S. Laarmann, L. Greune, H. Schillers, H. Oberleithner, and M. A. Schmidt. 2001. Characterization of translocation pores inserted into plasma membranes by type III-secreted Esp proteins of enteropathogenic Escherichia coli. Cell. Microbiol. 3:669-679.
    • (2001) Cell. Microbiol. , vol.3 , pp. 669-679
    • Ide, T.1    Laarmann, S.2    Greune, L.3    Schillers, H.4    Oberleithner, H.5    Schmidt, M.A.6
  • 28
    • 0033564208 scopus 로고    scopus 로고
    • Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide
    • Ilan, O., Y. Bloch, G. Frankel, H. Ullrich, K. Geider, and I. Rosenshine. 1999. Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide. EMBO J. 18:3241-3248.
    • (1999) EMBO J. , vol.18 , pp. 3241-3248
    • Ilan, O.1    Bloch, Y.2    Frankel, G.3    Ullrich, H.4    Geider, K.5    Rosenshine, I.6
  • 29
    • 0025840513 scopus 로고
    • The eae gene of enteropathogenic Escherichia coli encodes a 94-kilodalton membrane protein, the expression of which is influenced by the EAF plasmid
    • Jerse, A. E., and J. B. Kaper. 1991. The eae gene of enteropathogenic Escherichia coli encodes a 94-kilodalton membrane protein, the expression of which is influenced by the EAF plasmid. Infect. Immun. 59:4302-4309.
    • (1991) Infect. Immun. , vol.59 , pp. 4302-4309
    • Jerse, A.E.1    Kaper, J.B.2
  • 30
    • 0016151381 scopus 로고
    • Active transport of maltose in Escherichia coli K12: Involvement of "periplasmic" maltose binding protein
    • Kellermann, O., and S. Szmelcman. 1974. Active transport of maltose in Escherichia coli K12: involvement of "periplasmic" maltose binding protein. Eur. J. Biochem. 47:139-149.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 139-149
    • Kellermann, O.1    Szmelcman, S.2
  • 31
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., R. DeVinney, M. Stein, D. J. Reinscheid, E. A. Frey, and B. B. Finlay. 1997. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91:511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 32
    • 0036165971 scopus 로고    scopus 로고
    • Assembly of the type III secretion needle complex of Salmonella typhimurium
    • Kimbrough, T. G., and S. I. Miller. 2002. Assembly of the type III secretion needle complex of Salmonella typhimurium. Microbes Infect. 4:75-82.
    • (2002) Microbes Infect. , vol.4 , pp. 75-82
    • Kimbrough, T.G.1    Miller, S.I.2
  • 33
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type III secretion components to needle complex formation
    • Kimbrough, T. G., and S. I. Miller. 2000. Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc. Natl. Acad. Sci. USA 97:11008-11013.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 34
    • 0032522344 scopus 로고    scopus 로고
    • A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells
    • Knutton, S., I. Rosenshine, M. J. Pallen, I. Nisan, B. C. Neves, C. Bain, C. Wolff, G. Dougan, and G. Frankel. 1998. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 17:2166-2176.
    • (1998) EMBO J. , vol.17 , pp. 2166-2176
    • Knutton, S.1    Rosenshine, I.2    Pallen, M.J.3    Nisan, I.4    Neves, B.C.5    Bain, C.6    Wolff, C.7    Dougan, G.8    Frankel, G.9
  • 35
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component. YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster, M., W. Bitter, H. de Cock, A. Allaoui, G. R. Cornelis, and J. Tommassen. 1997. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26:789-797.
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    De Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 36
    • 0032774771 scopus 로고    scopus 로고
    • The EspD protein of enterohemorrhagic Escherichia coli is required for the formation of bacterial surface appendages and is incorporated in the cytoplasmic membranes of target cells
    • Kresse, A. U., M. Rohde, and C. A. Guzman. 1999. The EspD protein of enterohemorrhagic Escherichia coli is required for the formation of bacterial surface appendages and is incorporated in the cytoplasmic membranes of target cells. Infect. Immun. 67:4834-4842.
    • (1999) Infect. Immun. , vol.67 , pp. 4834-4842
    • Kresse, A.U.1    Rohde, M.2    Guzman, C.A.3
  • 38
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., N. Shimamoto, K. Yamaguchi, K. Namba, and S.-I. Aizawa. 1992. Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol. 226:433-446.
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, K.3    Namba, K.4    Aizawa, S.-I.5
  • 39
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
    • Kubori, T., A. Sukhan, S. I. Aizawa, and J. E. Galan. 2000. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc. Natl. Acad. Sci. USA 97:10225-10230.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 40
    • 0012749458 scopus 로고
    • Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication
    • Liberek, K., C. Georgopoulos, and M. Zylicz. 1988. Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication. Proc. Natl. Acad. Sci. USA 85:6632-6636.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6632-6636
    • Liberek, K.1    Georgopoulos, C.2    Zylicz, M.3
  • 41
    • 0032698478 scopus 로고    scopus 로고
    • The bacterial flagellum: Reversible rotary propellor and type III export apparatus
    • Macnab, R. M. 1999. The bacterial flagellum: reversible rotary propellor and type III export apparatus. J. Bacteriol. 181:7149-7153.
    • (1999) J. Bacteriol. , vol.181 , pp. 7149-7153
    • Macnab, R.M.1
  • 42
    • 0027235766 scopus 로고
    • Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa
    • Martin, P. R., M. Hobbs, P. D. Free, Y. Jeske, and J. S. Mattick. 1993. Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa. Mol. Microbiol. 9:857-868.
    • (1993) Mol. Microbiol. , vol.9 , pp. 857-868
    • Martin, P.R.1    Hobbs, M.2    Free, P.D.3    Jeske, Y.4    Mattick, J.S.5
  • 44
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino, T., and R. M. Macnab. 1999. Components of the Salmonella flagellar export apparatus and classification of export substrates. J. Bacteriol. 181:1388-1394.
    • (1999) J. Bacteriol. , vol.181 , pp. 1388-1394
    • Minamino, T.1    Macnab, R.M.2
  • 45
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T., and R. M. Macnab. 2000. Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35:1052-1064.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    Macnab, R.M.2
  • 46
    • 0031984684 scopus 로고    scopus 로고
    • Diarrheagenic Escherichia coli
    • Nataro, J., and J. Kaper. 1998. Diarrheagenic Escherichia coli. Clin. Microbiol. Rev. 11:142-201.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 142-201
    • Nataro, J.1    Kaper, J.2
  • 47
    • 0028298380 scopus 로고
    • Isolation of outer membranes
    • Nikaido, H. 1994. Isolation of outer membranes. Methods Enzymol. 235:225-235.
    • (1994) Methods Enzymol. , vol.235 , pp. 225-235
    • Nikaido, H.1
  • 49
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen, N., H. Stahlberg, A. P. Pugsley, and A. Engel. 2000. Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 19:2229-2236.
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 50
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N., and A. Geissler. 2001. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell. Biol. 2:339-349.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 51
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersiniapestis low-calcium response
    • Plano, G. V., S. S. Barve, and S. C. Straley. 1991. LcrD, a membrane-bound regulator of the Yersiniapestis low-calcium response. J. Bacteriol. 173:7293-7303.
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 52
    • 0035029021 scopus 로고    scopus 로고
    • Type III export: New uses for an old pathway
    • Plano, G. V., J. B. Day, and F. Ferracci. 2001. Type III export: new uses for an old pathway. Mol. Microbiol. 40:284-293.
    • (2001) Mol. Microbiol. , vol.40 , pp. 284-293
    • Plano, G.V.1    Day, J.B.2    Ferracci, F.3
  • 53
    • 0027297680 scopus 로고
    • Multiple effects of lcrD mutations in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1993. Multiple effects of lcrD mutations in Yersinia pestis. J. Bacteriol. 175:3536-3545.
    • (1993) J. Bacteriol. , vol.175 , pp. 3536-3545
    • Plano, G.V.1    Straley, S.C.2
  • 54
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1995. Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis. J. Bacteriol. 177:3843-3854.
    • (1995) J. Bacteriol. , vol.177 , pp. 3843-3854
    • Plano, G.V.1    Straley, S.C.2
  • 55
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 56
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist, M. 2001. Type II secretion and pathogenesis. Infect. Immun. 69:3523-3535.
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 57
    • 0035213076 scopus 로고    scopus 로고
    • MxiM and MxiJ, base elements of the Mxi-Spa type III secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope
    • Schuch, R., and A. T. Maurelli. 2001. MxiM and MxiJ, base elements of the Mxi-Spa type III secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope. J. Bacteriol. 183:6991-6998.
    • (2001) J. Bacteriol. , vol.183 , pp. 6991-6998
    • Schuch, R.1    Maurelli, A.T.2
  • 58
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya, K., M. Ohishi, T. Ogino, K. Tamano, C. Sasakawa, and A. Abe. 2001. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. USA 98:11638-11643.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 59
    • 0032957679 scopus 로고    scopus 로고
    • Interaction of FliI, a component of the flagellar export apparatus, with flagellin and hook protein
    • Silva-Herzog, E., and G. Dreyfus. 1999. Interaction of FliI, a component of the flagellar export apparatus, with flagellin and hook protein. Biochim. Biophys. Acta 1431:374-383.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 374-383
    • Silva-Herzog, E.1    Dreyfus, G.2
  • 60
    • 0030886946 scopus 로고    scopus 로고
    • Identification of the fliI and fliJ components of the Caulobacter flagellar type III protein secretion system
    • Stephens, C., C. Mohr, C. Boyd, J. Maddock, J. Gober, and L. Shapiro. 1997. Identification of the fliI and fliJ components of the Caulobacter flagellar type III protein secretion system. J. Bacteriol. 179:5355-5365.
    • (1997) J. Bacteriol. , vol.179 , pp. 5355-5365
    • Stephens, C.1    Mohr, C.2    Boyd, C.3    Maddock, J.4    Gober, J.5    Shapiro, L.6
  • 61
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex
    • Sukhan, A., T. Kubori, J. Wilson, and J. E. Galan. 2001. Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J. Bacteriol. 183:1159-1167.
    • (2001) J. Bacteriol. , vol.183 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 62
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors
    • Tamano, K., S. Aizawa, E. Katayama, T. Nonaka, S. Imajoh-Ohmi, A. Kuwae, S. Nagai, and C. Sasakawa. 2000. Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors. EMBO J. 19:3876-3887.
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.2    Katayama, E.3    Nonaka, T.4    Imajoh-Ohmi, S.5    Kuwae, A.6    Nagai, S.7    Sasakawa, C.8
  • 63
    • 0032443226 scopus 로고    scopus 로고
    • The EspB protein of enteropathogenic Escherichia coli is targeted to the cytoplasm of infected HeLa cells
    • Taylor, K. A., C. B. O'Connell, P. W. Luther, and M. S. Donnenberg. 1998. The EspB protein of enteropathogenic Escherichia coli is targeted to the cytoplasm of infected HeLa cells. Infect. Immun. 66:5501-5507.
    • (1998) Infect. Immun. , vol.66 , pp. 5501-5507
    • Taylor, K.A.1    O'Connell, C.B.2    Luther, P.W.3    Donnenberg, M.S.4
  • 64
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi, D. G., and S. J. Hultgren. 2000. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12:420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 65
    • 0034255122 scopus 로고    scopus 로고
    • Exploitation of host cells by enteropathogenic Escherichia coli
    • Vallance, B. A., and B. B. Finlay. 2000. Exploitation of host cells by enteropathogenic Escherichia coli. Proc. Natl. Acad. Sci. USA 97:8799-8806.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8799-8806
    • Vallance, B.A.1    Finlay, B.B.2
  • 66
    • 0030587961 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Nrampl encodes a membrane phosphoglycoprotein absent in macrophages from susceptible (Nramp1 D169) mouse strains
    • Vidal, S. M., E. Pinner, P. Lepage, S. Gauthier, and P. Gros. 1996. Natural resistance to intracellular infections: Nrampl encodes a membrane phosphoglycoprotein absent in macrophages from susceptible (Nramp1 D169) mouse strains. J. Immunol. 157:3559-3568.
    • (1996) J. Immunol. , vol.157 , pp. 3559-3568
    • Vidal, S.M.1    Pinner, E.2    Lepage, P.3    Gauthier, S.4    Gros, P.5
  • 67
    • 0032992390 scopus 로고    scopus 로고
    • Insertion of EspD into epithelial target cell membranes by infecting enteropathogenic Escherichia coli
    • Wachter, C., C. Beinke, M. Mattes, and M. A. Schmidt. 1999. Insertion of EspD into epithelial target cell membranes by infecting enteropathogenic Escherichia coli. Mol. Microbiol. 31:1695-1707.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1695-1707
    • Wachter, C.1    Beinke, C.2    Mattes, M.3    Schmidt, M.A.4
  • 68
    • 0032868135 scopus 로고    scopus 로고
    • Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli
    • Warawa, J., B. B. Finlay, and B. Kenny. 1999. Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli. Infect. Immun. 67:5538-5540.
    • (1999) Infect. Immun. , vol.67 , pp. 5538-5540
    • Warawa, J.1    Finlay, B.B.2    Kenny, B.3
  • 69
    • 0035167256 scopus 로고    scopus 로고
    • Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli
    • Wilson, R. K., R. K. Shaw, S. Daniell, S. Knutton, and G. Frankel. 2001. Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli. Cell. Microbiol. 3:753-762.
    • (2001) Cell. Microbiol. , vol.3 , pp. 753-762
    • Wilson, R.K.1    Shaw, R.K.2    Daniell, S.3    Knutton, S.4    Frankel, G.5
  • 70
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., A. Allaoui, P. Wattiau, and G. R. Cornelis. 1994. YscN, the putative energizer of the Yersinia Yop secretion machinery. J. Bacteriol. 176:1561-1569.
    • (1994) J. Bacteriol. , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 71
    • 0031922691 scopus 로고    scopus 로고
    • Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli
    • Wolff, C., I. Nisan, E. Hanski, G. Frankel, and I. Rosenshine. 1998. Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli. Mol. Microbiol. 28:143-155.
    • (1998) Mol. Microbiol. , vol.28 , pp. 143-155
    • Wolff, C.1    Nisan, I.2    Hanski, E.3    Frankel, G.4    Rosenshine, I.5


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