메뉴 건너뛰기




Volumn 81, Issue 3, 2011, Pages 734-750

The N-terminal amphipathic region of the Escherichia coli type III secretion system protein EspD is required for membrane insertion and function

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ESPD PROTEIN; PHOSPHATIDYLSERINE; UNCLASSIFIED DRUG;

EID: 79960728151     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07727.x     Document Type: Article
Times cited : (9)

References (67)
  • 1
    • 33644857975 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli Tir translocation and pedestal formation requires membrane cholesterol in the absence of bundle-forming pili
    • Allen-Vercoe, E., Waddell, B., Livingstone, S., Deans, J., and DeVinney, R. (2006) Enteropathogenic Escherichia coli Tir translocation and pedestal formation requires membrane cholesterol in the absence of bundle-forming pili. Cell Microbiol 8: 613-624.
    • (2006) Cell Microbiol , vol.8 , pp. 613-624
    • Allen-Vercoe, E.1    Waddell, B.2    Livingstone, S.3    Deans, J.4    DeVinney, R.5
  • 2
    • 0032728507 scopus 로고    scopus 로고
    • Phosphatidylethanolamine recognition promotes enteropathogenic E. coli and enterohemorrhagic E. coli host cell attachment
    • Barnett Foster, D., Philpott, D., Abul-Milh, M., Huesca, M., Sherman, P.M., and Lingwood, C.A. (1999) Phosphatidylethanolamine recognition promotes enteropathogenic E. coli and enterohemorrhagic E. coli host cell attachment. Microb Pathog 27: 289-301.
    • (1999) Microb Pathog , vol.27 , pp. 289-301
    • Barnett Foster, D.1    Philpott, D.2    Abul-Milh, M.3    Huesca, M.4    Sherman, P.M.5    Lingwood, C.A.6
  • 3
    • 0001123420 scopus 로고    scopus 로고
    • Enterohemorrhagic Escherichia coli induces apoptosis which augments bacterial binding and phosphatidylethanolamine exposure on the plasma membrane outer leaflet
    • Barnett Foster, D., Abul-Milh, M., Huesca, M., and Lingwood, C.A. (2000) Enterohemorrhagic Escherichia coli induces apoptosis which augments bacterial binding and phosphatidylethanolamine exposure on the plasma membrane outer leaflet. Infect Immun 68: 3108-3115.
    • (2000) Infect Immun , vol.68 , pp. 3108-3115
    • Barnett Foster, D.1    Abul-Milh, M.2    Huesca, M.3    Lingwood, C.A.4
  • 4
    • 33846985974 scopus 로고    scopus 로고
    • Increased adherence and actin pedestal formation by dam-deficient enterohaemorrhagic Escherichia coli O157:H7
    • Campellone, K.G., Roe, A.J., Løbner-Olesen, A., Murphy, K.C., Magoun, L., Brady, M.J., etal. (2007) Increased adherence and actin pedestal formation by dam-deficient enterohaemorrhagic Escherichia coli O157:H7. Mol Microbiol 63: 1468-1481.
    • (2007) Mol Microbiol , vol.63 , pp. 1468-1481
    • Campellone, K.G.1    Roe, A.J.2    Løbner-Olesen, A.3    Murphy, K.C.4    Magoun, L.5    Brady, M.J.6
  • 5
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell, R.B., and Taneva, S.G. (2006) Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr Protein Pept Sci 7: 539-552.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 6
    • 0032925379 scopus 로고    scopus 로고
    • Host cell death due to enteropathogenic Escherichia coli has features of apoptosis
    • Crane, J.K., Majumdar, S., and Pickhardt, D.F., III (1999) Host cell death due to enteropathogenic Escherichia coli has features of apoptosis. Infect Immun 67: 2575-2584.
    • (1999) Infect Immun , vol.67 , pp. 2575-2584
    • Crane, J.K.1    Majumdar, S.2    Pickhardt III, D.F.3
  • 7
    • 0034997929 scopus 로고    scopus 로고
    • Coiled-coil domain of enteropathogenic Escherichia coli type III secreted protein EspD is involved in EspA filament-mediated cell attachment and hemolysis
    • Daniell, S.J., Delahay, R.M., Shaw, R.K., Hartland, E.L., Pallen, M.J., Booy, F., etal. (2001) Coiled-coil domain of enteropathogenic Escherichia coli type III secreted protein EspD is involved in EspA filament-mediated cell attachment and hemolysis. Infect Immun 69: 4055-4064.
    • (2001) Infect Immun , vol.69 , pp. 4055-4064
    • Daniell, S.J.1    Delahay, R.M.2    Shaw, R.K.3    Hartland, E.L.4    Pallen, M.J.5    Booy, F.6
  • 8
    • 0036041792 scopus 로고    scopus 로고
    • Coiled-coil proteins associated with type III secretion systems: a versatile domain revisited
    • Delahay, R.M., and Frankel, G. (2002) Coiled-coil proteins associated with type III secretion systems: a versatile domain revisited. Mol Microbiol 45: 905-916.
    • (2002) Mol Microbiol , vol.45 , pp. 905-916
    • Delahay, R.M.1    Frankel, G.2
  • 10
    • 34948876257 scopus 로고    scopus 로고
    • Rapid site-directed domain scanning mutagenesis of enteropathogenic Escherichia coli espD
    • Deng, Q., Luo, W., and Donnenberg, M.S. (2007) Rapid site-directed domain scanning mutagenesis of enteropathogenic Escherichia coli espD. Biol Proced Online 9: 18-26.
    • (2007) Biol Proced Online , vol.9 , pp. 18-26
    • Deng, Q.1    Luo, W.2    Donnenberg, M.S.3
  • 11
    • 0029833954 scopus 로고    scopus 로고
    • Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase
    • Dunne, S.J., Cornell, R.B., Johnson, J.E., Glover, N.R., and Tracey, A.S. (1996) Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry 35: 11975-11984.
    • (1996) Biochemistry , vol.35 , pp. 11975-11984
    • Dunne, S.J.1    Cornell, R.B.2    Johnson, J.E.3    Glover, N.R.4    Tracey, A.S.5
  • 12
    • 0018789682 scopus 로고
    • Adsorption of monovalent cations to bilayer membranes containing negative phospholipids
    • Eisenberg, M., Gresalfi, T., Riccio, T., and McLaughlin, S. (1979) Adsorption of monovalent cations to bilayer membranes containing negative phospholipids. Biochemistry 18: 5213-5223.
    • (1979) Biochemistry , vol.18 , pp. 5213-5223
    • Eisenberg, M.1    Gresalfi, T.2    Riccio, T.3    McLaughlin, S.4
  • 13
    • 33745615443 scopus 로고    scopus 로고
    • Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa
    • Faudry, E., Vernier, G., Neumann, E., Forge, V., and Attree, I. (2006) Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa. Biochemistry 45: 8117-8123.
    • (2006) Biochemistry , vol.45 , pp. 8117-8123
    • Faudry, E.1    Vernier, G.2    Neumann, E.3    Forge, V.4    Attree, I.5
  • 15
    • 0141794280 scopus 로고    scopus 로고
    • Cellular apoptosis is associated with increased caveolin-1 expression in macrophages
    • Gargalovic, P., and Dory, L. (2003) Cellular apoptosis is associated with increased caveolin-1 expression in macrophages. J Lipid Res 44: 1622-1632.
    • (2003) J Lipid Res , vol.44 , pp. 1622-1632
    • Gargalovic, P.1    Dory, L.2
  • 16
    • 17644382700 scopus 로고    scopus 로고
    • Enteropathogenic and enterohemorrhagic Escherichia coli infections: translocation, translocation, translocation
    • Garmendia, J., Frankel, G., and Crepin, V.F. (2005) Enteropathogenic and enterohemorrhagic Escherichia coli infections: translocation, translocation, translocation. Infect Immun 73: 2573-2585.
    • (2005) Infect Immun , vol.73 , pp. 2573-2585
    • Garmendia, J.1    Frankel, G.2    Crepin, V.F.3
  • 17
    • 4344690860 scopus 로고    scopus 로고
    • Targeting of Helicobacter pylori vacuolating toxin to lipid raft membrane domains analysed by atomic force microscopy
    • Geisse, N.A., Cover, T.L., Henderson, R.M., and Edwardson, J.M. (2004) Targeting of Helicobacter pylori vacuolating toxin to lipid raft membrane domains analysed by atomic force microscopy. Biochem J 381: 911-917.
    • (2004) Biochem J , vol.381 , pp. 911-917
    • Geisse, N.A.1    Cover, T.L.2    Henderson, R.M.3    Edwardson, J.M.4
  • 18
    • 0034659385 scopus 로고    scopus 로고
    • Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin
    • Goosney, D.L., DeVinney, R., Pfuetzner, R.A., Frey, E.A., Strynadka, N.C., and Finlay, B.B. (2000) Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin. Curr Biol 10: 735-738.
    • (2000) Curr Biol , vol.10 , pp. 735-738
    • Goosney, D.L.1    DeVinney, R.2    Pfuetzner, R.A.3    Frey, E.A.4    Strynadka, N.C.5    Finlay, B.B.6
  • 19
    • 0037425743 scopus 로고    scopus 로고
    • Gut flora in health and disease
    • Guarner, F., and Malagelada, J.R. (2003) Gut flora in health and disease. Lancet 361: 512-519.
    • (2003) Lancet , vol.361 , pp. 512-519
    • Guarner, F.1    Malagelada, J.R.2
  • 20
    • 0033852317 scopus 로고    scopus 로고
    • Membrane fusion activity of purified SipB, a Salmonella surface protein essential for mammalian cell invasion
    • Hayward, R.D., McGhie, E.J., and Koronakis, V. (2000) Membrane fusion activity of purified SipB, a Salmonella surface protein essential for mammalian cell invasion. Mol Microbiol 37: 727-739.
    • (2000) Mol Microbiol , vol.37 , pp. 727-739
    • Hayward, R.D.1    McGhie, E.J.2    Koronakis, V.3
  • 21
    • 17644366419 scopus 로고    scopus 로고
    • Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells
    • Hayward, R.D., Cain, R.J., McGhie, E.J., Phillips, N., Garner, M.J., and Koronakis, V. (2005) Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells. Mol Microbiol 56: 590-603.
    • (2005) Mol Microbiol , vol.56 , pp. 590-603
    • Hayward, R.D.1    Cain, R.J.2    McGhie, E.J.3    Phillips, N.4    Garner, M.J.5    Koronakis, V.6
  • 22
    • 0038501071 scopus 로고    scopus 로고
    • The purified Shigella IpaB and Salomella SipB translocators share biochemical properties and membrane topology
    • Hume, P.J., McGhie, E.J., Hayward, R.D., and Koronakis, V. (2003) The purified Shigella IpaB and Salomella SipB translocators share biochemical properties and membrane topology. Mol Microbiol 49: 425-439.
    • (2003) Mol Microbiol , vol.49 , pp. 425-439
    • Hume, P.J.1    McGhie, E.J.2    Hayward, R.D.3    Koronakis, V.4
  • 23
    • 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., Laarmann, S., Greune, L., Schillers, H., Oberleithner, H., and Schmidt, M.A. (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
  • 24
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation
    • Jarvis, K.G., Girón, J.A., Jerse, A.E., McDaniel, T.K., Donnenberg, M.S., and Kaper, J.B. (1995) Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc Natl Acad Sci USA 92: 7996-8000.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7996-8000
    • Jarvis, K.G.1    Girón, J.A.2    Jerse, A.E.3    McDaniel, T.K.4    Donnenberg, M.S.5    Kaper, J.B.6
  • 25
    • 0142248438 scopus 로고    scopus 로고
    • Synergistic roles for the Map and Tir effector molecules in mediating uptake of enteropathogenic Escherichia coli (EPEC) into non-phagocytic cells
    • Jepson, M.A., Pellegrin, S., Peto, L., Banbury, D.N., Leard, A.D., Mellor, H., and Kenny, B. (2003) Synergistic roles for the Map and Tir effector molecules in mediating uptake of enteropathogenic Escherichia coli (EPEC) into non-phagocytic cells. Cell Microbiol 5: 773-783.
    • (2003) Cell Microbiol , vol.5 , pp. 773-783
    • Jepson, M.A.1    Pellegrin, S.2    Peto, L.3    Banbury, D.N.4    Leard, A.D.5    Mellor, H.6    Kenny, B.7
  • 26
    • 0037414807 scopus 로고    scopus 로고
    • Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes
    • Johnson, J.E., Xie, M., Singh, L.M.R., Edge, R., and Cornell, R.B. (2003) Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes. J Biol Chem 278: 514-522.
    • (2003) J Biol Chem , vol.278 , pp. 514-522
    • Johnson, J.E.1    Xie, M.2    Singh, L.M.R.3    Edge, R.4    Cornell, R.B.5
  • 27
    • 58449115816 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli modulates host intestinal cell membrane asymmetry and metabolic activity
    • Johnson, A.M., Kaushik, R.S., Rotella, N.J., and Hardwidge, P.R. (2009) Enterotoxigenic Escherichia coli modulates host intestinal cell membrane asymmetry and metabolic activity. Infect Immun 77: 341-347.
    • (2009) Infect Immun , vol.77 , pp. 341-347
    • Johnson, A.M.1    Kaushik, R.S.2    Rotella, N.J.3    Hardwidge, P.R.4
  • 29
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., DeVinney, R., Stein, M., Reinscheid, D.J., Frey, E.A., and Finlay, B.B. (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
  • 30
    • 0023073670 scopus 로고
    • Adhesion of enteropathogenic Escherichia coli to human intestinal enterocytes and cultured human intestinal mucosa
    • Knutton, S., Lloyd, D.R., and McNeish, A. (1987) Adhesion of enteropathogenic Escherichia coli to human intestinal enterocytes and cultured human intestinal mucosa. Infect Immun 55: 69-77.
    • (1987) Infect Immun , vol.55 , pp. 69-77
    • Knutton, S.1    Lloyd, D.R.2    McNeish, A.3
  • 31
    • 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., Rohde, M., and Guzmán, C.A. (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    Guzmán, C.A.3
  • 32
    • 17844381899 scopus 로고    scopus 로고
    • Bacterial invasion via lipid rafts
    • Lafont, F., and van der Goot, F.G. (2005) Bacterial invasion via lipid rafts. Cell Microbiol 7: 613-620.
    • (2005) Cell Microbiol , vol.7 , pp. 613-620
    • Lafont, F.1    van der Goot, F.G.2
  • 33
    • 0031009562 scopus 로고    scopus 로고
    • A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells
    • Lai, L.C., Wainwright, L.A., Stone, K.D., and Donnenberg, M.S. (1997) A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells. Infect Immun 65: 2211-2217.
    • (1997) Infect Immun , vol.65 , pp. 2211-2217
    • Lai, L.C.1    Wainwright, L.A.2    Stone, K.D.3    Donnenberg, M.S.4
  • 34
    • 0029154652 scopus 로고
    • Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide
    • Leenhouts, J.M., van den Wijngaard, P.W.J., de Kroon, A.I.P.M., and de Kruijff, B. (1995) Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide. FEBS Lett 370: 189-192.
    • (1995) FEBS Lett , vol.370 , pp. 189-192
    • Leenhouts, J.M.1    van den Wijngaard, P.W.J.2    de Kroon, A.I.P.M.3    de Kruijff, B.4
  • 35
    • 31844450592 scopus 로고    scopus 로고
    • Analysis of the function of enteropathogenic Escherichia coli EspB by random mutagenesis
    • Luo, W., and Donnenberg, M.S. (2006) Analysis of the function of enteropathogenic Escherichia coli EspB by random mutagenesis. Infect Immun 74: 810-820.
    • (2006) Infect Immun , vol.74 , pp. 810-820
    • Luo, W.1    Donnenberg, M.S.2
  • 36
    • 79958022702 scopus 로고    scopus 로고
    • Interactions and predicted host membrane topology of enteropathogenic Escherichia coli translocator protein EspB
    • 2972-2980 JB00153-00111
    • Luo, W., and Donnenberg, M.S. (2011) Interactions and predicted host membrane topology of enteropathogenic Escherichia coli translocator protein EspB. J Bacteriol 193: 2972-2980. JB.00153-00111.
    • (2011) J Bacteriol , vol.193
    • Luo, W.1    Donnenberg, M.S.2
  • 37
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., and Stock, J. (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 38
    • 0028945803 scopus 로고
    • A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens
    • McDaniel, T.K., Jarvis, K.G., Donnenberg, M.S., and Kaper, J.B. (1995) A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proc Natl Acad Sci USA 92: 1664-1668.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1664-1668
    • McDaniel, T.K.1    Jarvis, K.G.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 39
    • 0036015644 scopus 로고    scopus 로고
    • Topology of the Salmonella invasion protein SipB in a model bilayer
    • McGhie, E.J., Hume, P.J., Hayward, R.D., Torres, J., and Koronakis, V. (2002) Topology of the Salmonella invasion protein SipB in a model bilayer. Mol Microbiol 45: 1309-1321.
    • (2002) Mol Microbiol , vol.45 , pp. 1309-1321
    • McGhie, E.J.1    Hume, P.J.2    Hayward, R.D.3    Torres, J.4    Koronakis, V.5
  • 41
    • 25444439530 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli type III effectors EspG and EspG2 alter epithelial paracellular permeability
    • Matsuzawa, T., Kuwae, A., and Abe, A. (2005) Enteropathogenic Escherichia coli type III effectors EspG and EspG2 alter epithelial paracellular permeability. Infect Immun 73: 6283-6289.
    • (2005) Infect Immun , vol.73 , pp. 6283-6289
    • Matsuzawa, T.1    Kuwae, A.2    Abe, A.3
  • 42
    • 34548502503 scopus 로고    scopus 로고
    • Enteropathogenic and enterohemorrhagic Escherichia coli virulence gene regulation
    • Mellies, J.L., Barron, A.M., and Carmona, A.M. (2007) Enteropathogenic and enterohemorrhagic Escherichia coli virulence gene regulation. Infect Immun 75: 4199-4210.
    • (2007) Infect Immun , vol.75 , pp. 4199-4210
    • Mellies, J.L.1    Barron, A.M.2    Carmona, A.M.3
  • 43
    • 21344453525 scopus 로고    scopus 로고
    • The bacterial injection kit: type III secretion systems
    • Mota, L.J., and Cornelis, G.R. (2005) The bacterial injection kit: type III secretion systems. Ann Med 37: 234-249.
    • (2005) Ann Med , vol.37 , pp. 234-249
    • Mota, L.J.1    Cornelis, G.R.2
  • 44
    • 0037379441 scopus 로고    scopus 로고
    • CesD2 of enteropathogenic Escherichia coli is a second chaperone for the type III secretion translocator protein EspD
    • Neves, B.C., Mundy, R., Petrovska, L., Dougan, G., Knutton, S., and Frankel, G. (2003) CesD2 of enteropathogenic Escherichia coli is a second chaperone for the type III secretion translocator protein EspD. Infect Immun 71: 2130-2141.
    • (2003) Infect Immun , vol.71 , pp. 2130-2141
    • Neves, B.C.1    Mundy, R.2    Petrovska, L.3    Dougan, G.4    Knutton, S.5    Frankel, G.6
  • 45
    • 0038339444 scopus 로고    scopus 로고
    • Adhesion of enteropathogenic Escherichia coli to host cells
    • Nougayrede, J.P., Fernandes, P.J., and Donnenberg, M.S. (2003) Adhesion of enteropathogenic Escherichia coli to host cells. Cell Microbiol 5: 359-372.
    • (2003) Cell Microbiol , vol.5 , pp. 359-372
    • Nougayrede, J.P.1    Fernandes, P.J.2    Donnenberg, M.S.3
  • 46
    • 0030811577 scopus 로고    scopus 로고
    • Coiled-coil domains in proteins secreted by type III secretion systems
    • Pallen, M.J., Dougan, G., and Frankel, G. (1997) Coiled-coil domains in proteins secreted by type III secretion systems. Mol Microbiol 25: 423-425.
    • (1997) Mol Microbiol , vol.25 , pp. 423-425
    • Pallen, M.J.1    Dougan, G.2    Frankel, G.3
  • 47
    • 18944390249 scopus 로고    scopus 로고
    • Bioinformatics analysis of the locus for enterocyte effacement provides novel insights into type-III secretion
    • Pallen, M.J., Beatson, S.A., and Bailey, C.M. (2005) Bioinformatics analysis of the locus for enterocyte effacement provides novel insights into type-III secretion. BMC Microbiol 5: 9-30.
    • (2005) BMC Microbiol , vol.5 , pp. 9-30
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 49
    • 33646363801 scopus 로고    scopus 로고
    • Insertion of the enteropathogenic Escherichia coli Tir virulence protein into membranes in vitro
    • Race, P.R., Lakey, J.H., and Banfield, M.J. (2006) Insertion of the enteropathogenic Escherichia coli Tir virulence protein into membranes in vitro. J Biol Chem 281: 7842-7849.
    • (2006) J Biol Chem , vol.281 , pp. 7842-7849
    • Race, P.R.1    Lakey, J.H.2    Banfield, M.J.3
  • 50
    • 27744584137 scopus 로고    scopus 로고
    • Cholesterol-enriched membrane microdomains are required for inducing host cell cytoskeleton rearrangements in response to attaching-effacing Escherichia coli
    • Riff, J.D., Callahan, J.W., and Sherman, P.M. (2005) Cholesterol-enriched membrane microdomains are required for inducing host cell cytoskeleton rearrangements in response to attaching-effacing Escherichia coli. Infect Immun 73: 7113-7125.
    • (2005) Infect Immun , vol.73 , pp. 7113-7125
    • Riff, J.D.1    Callahan, J.W.2    Sherman, P.M.3
  • 51
    • 0034676288 scopus 로고    scopus 로고
    • Microbial pathogenesis: lipid rafts as pathogen portals
    • Rosenberger, C.M., Brumell, J.H., and Finlay, B.B. (2000) Microbial pathogenesis: lipid rafts as pathogen portals. Curr Biol 10: R823-R825.
    • (2000) Curr Biol , vol.10
    • Rosenberger, C.M.1    Brumell, J.H.2    Finlay, B.B.3
  • 52
    • 0038076041 scopus 로고    scopus 로고
    • Medical and economic impact of extraintestinal infections due to Escherichia coli: focus on an increasingly important endemic problem
    • Russo, T.A., and Johnson, J.R. (2003) Medical and economic impact of extraintestinal infections due to Escherichia coli: focus on an increasingly important endemic problem. Microbes Infect 5: 449-456.
    • (2003) Microbes Infect , vol.5 , pp. 449-456
    • Russo, T.A.1    Johnson, J.R.2
  • 53
    • 33748881180 scopus 로고    scopus 로고
    • Prediction of in-plane membrane anchors in monotopic proteins using a SVM classifier
    • Sapay, N., Guermeur, Y., and Deleage, G. (2006) Prediction of in-plane membrane anchors in monotopic proteins using a SVM classifier. BMC Bioinformatics 7: 255-266.
    • (2006) BMC Bioinformatics , vol.7 , pp. 255-266
    • Sapay, N.1    Guermeur, Y.2    Deleage, G.3
  • 54
    • 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., Ohishi, M., Ogino, T., Tamano, K., Sasakawa, C., and Abe, A. (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
  • 55
    • 0036267259 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli translocate Tir and form an intimin-Tir intimate attachment to red blood cell membranes
    • Shaw, R.K., Daniell, S., Frankel, G., and Knutton, S. (2002) Enteropathogenic Escherichia coli translocate Tir and form an intimin-Tir intimate attachment to red blood cell membranes. Microbiology 148: 1355-1365.
    • (2002) Microbiology , vol.148 , pp. 1355-1365
    • Shaw, R.K.1    Daniell, S.2    Frankel, G.3    Knutton, S.4
  • 56
    • 12844281912 scopus 로고    scopus 로고
    • Interaction of enteropathogenic Escherichia coli with human intestinal mucosa: role of effector proteins in brush border remodeling and formation of attaching and effacing lesions
    • Shaw, R.K., Cleary, J., Murphy, M.S., Frankel, G., and Knutton, S. (2005) Interaction of enteropathogenic Escherichia coli with human intestinal mucosa: role of effector proteins in brush border remodeling and formation of attaching and effacing lesions. Infect Immun 73: 1243-1251.
    • (2005) Infect Immun , vol.73 , pp. 1243-1251
    • Shaw, R.K.1    Cleary, J.2    Murphy, M.S.3    Frankel, G.4    Knutton, S.5
  • 57
    • 25144442798 scopus 로고    scopus 로고
    • Enteropathogenic E. coli disrupts tight junction barrier function and structure in vivo
    • Shifflett, D.E., Clayburgh, D.R., Koutsouris, A., Turner, J.R., and Hecht, G.A. (2005) Enteropathogenic E. coli disrupts tight junction barrier function and structure in vivo. Lab Invest 85: 1308-1324.
    • (2005) Lab Invest , vol.85 , pp. 1308-1324
    • Shifflett, D.E.1    Clayburgh, D.R.2    Koutsouris, A.3    Turner, J.R.4    Hecht, G.A.5
  • 58
    • 0034737268 scopus 로고    scopus 로고
    • Membrane-induced conformational change of proteins
    • Sui, S.-F. (2000) Membrane-induced conformational change of proteins. Adv Colloid Interface Sci 85: 257-267.
    • (2000) Adv Colloid Interface Sci , vol.85 , pp. 257-267
    • Sui, S.-F.1
  • 59
    • 0036161373 scopus 로고    scopus 로고
    • Species-specific cell adhesion of enteropathogenic Escherichia coli is mediated by type IV bundle-forming pili
    • Tobe, T., and Sasakawa, C. (2002) Species-specific cell adhesion of enteropathogenic Escherichia coli is mediated by type IV bundle-forming pili. Cell Microbiol 4: 29-42.
    • (2002) Cell Microbiol , vol.4 , pp. 29-42
    • Tobe, T.1    Sasakawa, C.2
  • 60
    • 0037238121 scopus 로고    scopus 로고
    • EspH, a new cytoskeleton-modulating effector of enterohaemorrhagic and enteropathogenic Escherichia coli
    • Tu, X., Nisan, I., Yona, C., Hanski, E., and Rosenshine, I. (2003) EspH, a new cytoskeleton-modulating effector of enterohaemorrhagic and enteropathogenic Escherichia coli. Mol Microbiol 47: 595-606.
    • (2003) Mol Microbiol , vol.47 , pp. 595-606
    • Tu, X.1    Nisan, I.2    Yona, C.3    Hanski, E.4    Rosenshine, I.5
  • 61
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky, V.N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11: 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 62
    • 0032992390 scopus 로고    scopus 로고
    • Insertion of EspD into epithelial target cell membranes by infecting enteropathogenic Escherichia coli
    • Wachter, C., Beinke, C., Mattes, M., and Schmidt, M.A. (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
  • 63
    • 0031931363 scopus 로고    scopus 로고
    • EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli
    • Wainwright, L.A., and Kaper, J.B. (1998) EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli. Mol Microbiol 27: 1247-1260.
    • (1998) Mol Microbiol , vol.27 , pp. 1247-1260
    • Wainwright, L.A.1    Kaper, J.B.2
  • 64
    • 0031922691 scopus 로고    scopus 로고
    • Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli
    • Wolff, C., Nisan, I., Hanski, E., Frankel, G., and Rosenshine, I. (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
  • 65
    • 0028295796 scopus 로고
    • Resonance energy transfer: methods and applications
    • Wu, P.G., and Brand, L. (1994) Resonance energy transfer: methods and applications. Anal Biochem 218: 1-13.
    • (1994) Anal Biochem , vol.218 , pp. 1-13
    • Wu, P.G.1    Brand, L.2
  • 66
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.-M., Wimley, W.C., Gawrisch, K., and White, S.H. (1998) The preference of tryptophan for membrane interfaces. Biochemistry 37: 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 67
    • 62049084949 scopus 로고    scopus 로고
    • Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling
    • Zech, T., Ejsing, C.S., Gaus, K., de Wet, B., Shevchenko, A., Simons, K., and Harder, T. (2009) Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling. EMBO J 28: 466-476.
    • (2009) EMBO J , vol.28 , pp. 466-476
    • Zech, T.1    Ejsing, C.S.2    Gaus, K.3    de Wet, B.4    Shevchenko, A.5    Simons, K.6    Harder, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.