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Volumn 12, Issue 9, 2010, Pages 1308-1321

The bacterial effectors EspG and EspG2 induce a destructive calpain activity that is kept in check by the co-delivered Tir effector

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CALPAIN; CALPASTATIN; CYSTEINE PROTEINASE; ESPG PROTEIN; ESPG2 PROTEIN; INTIMIN; LIGAND; UNCLASSIFIED DRUG;

EID: 77957147180     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2010.01469.x     Document Type: Article
Times cited : (23)

References (55)
  • 1
    • 34748911856 scopus 로고    scopus 로고
    • The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways
    • Alto NM, Weflen AW, Rardin MJ, Yarar D, Lazar CS, Tonikian R. The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways. J Cell Biol 2007, 178:1265-1278.
    • (2007) J Cell Biol , vol.178 , pp. 1265-1278
    • Alto, N.M.1    Weflen, A.W.2    Rardin, M.J.3    Yarar, D.4    Lazar, C.S.5    Tonikian, R.6    et al7
  • 3
    • 43049090506 scopus 로고    scopus 로고
    • Deciphering interplay between Salmonella invasion effectors
    • Cain RJ, Hayward RD, Koronakis V. Deciphering interplay between Salmonella invasion effectors. PLoS Pathog 2008, 4:e1000037.
    • (2008) PLoS Pathog , vol.4
    • Cain, R.J.1    Hayward, R.D.2    Koronakis, V.3
  • 4
    • 0027302362 scopus 로고
    • Enteropathogenic Escherichia coli decreases the transepithelial electrical resistance of polarized epithelial monolayers
    • Canil C, Rosenshine I, Ruschkowski S, Donnenberg MS, Kaper JB, Finlay BB. Enteropathogenic Escherichia coli decreases the transepithelial electrical resistance of polarized epithelial monolayers. Infect Immun 1993, 61:2755-2762.
    • (1993) Infect Immun , vol.61 , pp. 2755-2762
    • Canil, C.1    Rosenshine, I.2    Ruschkowski, S.3    Donnenberg, M.S.4    Kaper, J.B.5    Finlay, B.B.6
  • 5
    • 0027979552 scopus 로고
    • Differential expression of sucrase-isomaltase in clones isolated from early and late passages of the cell line Caco-2: evidence for glucose-dependent negative regulation
    • Chantret I, Rodolosse A, Barbat A, Dussaulx E, Brot-Laroche E, Zweibaum A, Rousset M. Differential expression of sucrase-isomaltase in clones isolated from early and late passages of the cell line Caco-2: evidence for glucose-dependent negative regulation. J Cell Sci 1994, 107:213-225.
    • (1994) J Cell Sci , vol.107 , pp. 213-225
    • Chantret, I.1    Rodolosse, A.2    Barbat, A.3    Dussaulx, E.4    Brot-Laroche, E.5    Zweibaum, A.6    Rousset, M.7
  • 6
    • 12144279606 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli: unravelling pathogenesis
    • Chen HD, Frankel G. Enteropathogenic Escherichia coli: unravelling pathogenesis. FEMS Microbiol Rev 2005, 29:83-98.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 83-98
    • Chen, H.D.1    Frankel, G.2
  • 7
    • 50049086091 scopus 로고    scopus 로고
    • Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U)
    • Cheng HC, Skehan BM, Campellone KG, Leong JM, Rosen MK. Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U). Nature 2008, 454:1009-1013.
    • (2008) Nature , vol.454 , pp. 1009-1013
    • Cheng, H.C.1    Skehan, B.M.2    Campellone, K.G.3    Leong, J.M.4    Rosen, M.K.5
  • 8
    • 58249092789 scopus 로고    scopus 로고
    • TLR2-induced calpain cleavage of epithelial junctional proteins facilitates leukocyte transmigration
    • Chun J, Prince A. TLR2-induced calpain cleavage of epithelial junctional proteins facilitates leukocyte transmigration. Cell Host Microbe 2009, 5:47-58.
    • (2009) Cell Host Microbe , vol.5 , pp. 47-58
    • Chun, J.1    Prince, A.2
  • 9
    • 56749097786 scopus 로고    scopus 로고
    • Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri
    • Davis J, Wang J, Tropea JE, Zhang D, Dauter Z, Waugh DS, Wlodawer A. Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri. Protein Sci 2008, 17:2167-2173.
    • (2008) Protein Sci , vol.17 , pp. 2167-2173
    • Davis, J.1    Wang, J.2    Tropea, J.E.3    Zhang, D.4    Dauter, Z.5    Waugh, D.S.6    Wlodawer, A.7
  • 10
    • 7644225138 scopus 로고    scopus 로고
    • Intestinal barrier dysfunction by enteropathogenic Escherichia coli is mediated by two effector molecules and a bacterial surface protein
    • Dean P, Kenny B. Intestinal barrier dysfunction by enteropathogenic Escherichia coli is mediated by two effector molecules and a bacterial surface protein. Mol Microbiol 2004, 54:665-675.
    • (2004) Mol Microbiol , vol.54 , pp. 665-675
    • Dean, P.1    Kenny, B.2
  • 11
    • 59849113939 scopus 로고    scopus 로고
    • The effector repertoire of enteropathogenic E. coli: ganging up on the host cell
    • Dean P, Kenny B. The effector repertoire of enteropathogenic E. coli: ganging up on the host cell. Curr Opin Microbiol 2009, 12:101-109.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 101-109
    • Dean, P.1    Kenny, B.2
  • 12
    • 32444434444 scopus 로고    scopus 로고
    • Potent diarrheagenic mechanism mediated by the cooperative action of three enteropathogenic Escherichia coli-injected effector proteins
    • Dean P, Maresca M, Schuller S, Phillips AD, Kenny B. Potent diarrheagenic mechanism mediated by the cooperative action of three enteropathogenic Escherichia coli-injected effector proteins. Proc Natl Acad Sci USA 2006, 103:1876-1881.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1876-1881
    • Dean, P.1    Maresca, M.2    Schuller, S.3    Phillips, A.D.4    Kenny, B.5
  • 13
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg MS, Kaper JB. Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect Immun 1991, 59:4310-4317.
    • (1991) Infect Immun , vol.59 , pp. 4310-4317
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 14
    • 0025285812 scopus 로고
    • Construction and analysis of TnphoA mutants of enteropathogenic Escherichia coli unable to invade HEp-2 cells
    • Donnenberg MS, Calderwood SB, Donohue-Rolfe A, Keusch GT, Kaper JB. Construction and analysis of TnphoA mutants of enteropathogenic Escherichia coli unable to invade HEp-2 cells. Infect Immun 1990, 58:1565-1571.
    • (1990) Infect Immun , vol.58 , pp. 1565-1571
    • Donnenberg, M.S.1    Calderwood, S.B.2    Donohue-Rolfe, A.3    Keusch, G.T.4    Kaper, J.B.5
  • 15
    • 0035024818 scopus 로고    scopus 로고
    • EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella flexneri
    • Elliott SJ, Krejany EO, Mellies JL, Robins-Browne RM, Sasakawa C, Kaper JB. EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella flexneri. Infect Immun 2001, 69:4027-4033.
    • (2001) Infect Immun , vol.69 , pp. 4027-4033
    • Elliott, S.J.1    Krejany, E.O.2    Mellies, J.L.3    Robins-Browne, R.M.4    Sasakawa, C.5    Kaper, J.B.6
  • 16
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: calpains make the cut
    • Franco SJ, Huttenlocher A. Regulating cell migration: calpains make the cut. J Cell Sci 2005, 118:3829-3838.
    • (2005) J Cell Sci , vol.118 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 17
    • 0033575956 scopus 로고    scopus 로고
    • A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y, Galan JE. A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999, 401:293-297.
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 18
    • 33846810181 scopus 로고    scopus 로고
    • Mechanism underlying inhibition of intestinal apical Cl/OH exchange following infection with enteropathogenic E. coli
    • Gill RK, Borthakur A, Hodges K, Turner JR, Clayburgh DR, Saksena S. Mechanism underlying inhibition of intestinal apical Cl/OH exchange following infection with enteropathogenic E. coli. J Clin Invest 2007, 117:428-437.
    • (2007) J Clin Invest , vol.117 , pp. 428-437
    • Gill, R.K.1    Borthakur, A.2    Hodges, K.3    Turner, J.R.4    Clayburgh, D.R.5    Saksena, S.6    et al7
  • 19
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: calpain proteases in cell motility
    • Glading A, Lauffenburger DA, Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 2002, 12:46-54.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 20
    • 63249098521 scopus 로고    scopus 로고
    • Tight junctions as targets of infectious agents
    • Guttman JA, Finlay BB. Tight junctions as targets of infectious agents. Biochim Biophys Acta 2009, 1788:832-841.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 832-841
    • Guttman, J.A.1    Finlay, B.B.2
  • 23
    • 58149498183 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69
    • Iguchi A, Thomson NR, Ogura Y, Saunders D, Ooka T, Henderson IR. Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69. J Bacteriol 2009, 191:347-354.
    • (2009) J Bacteriol , vol.191 , pp. 347-354
    • Iguchi, A.1    Thomson, N.R.2    Ogura, Y.3    Saunders, D.4    Ooka, T.5    Henderson, I.R.6    et al7
  • 24
    • 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 MA, Pellegrin S, Peto L, Banbury DN, Leard AD, Mellor H, Kenny B. Synergistic roles for the Map and Tir effector molecules in mediating uptake of enteropathogenic Escherichia coli (EPEC) into non-phagocytic cells. Cell Microbiol 2003, 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
  • 25
    • 0034872761 scopus 로고    scopus 로고
    • The enterohaemorrhagic Escherichia coli (serotype O157:H7) Tir molecule is not functionally interchangeable for its enteropathogenic E. coli (serotype O127:H6) homologue
    • Kenny B. The enterohaemorrhagic Escherichia coli (serotype O157:H7) Tir molecule is not functionally interchangeable for its enteropathogenic E. coli (serotype O127:H6) homologue. Cell Microbiol 2001, 3:499-510.
    • (2001) Cell Microbiol , vol.3 , pp. 499-510
    • Kenny, B.1
  • 26
    • 0034518855 scopus 로고    scopus 로고
    • Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria
    • Kenny B, Jepson M. Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria. Cell Microbiol 2000, 2:579-590.
    • (2000) Cell Microbiol , vol.2 , pp. 579-590
    • Kenny, B.1    Jepson, M.2
  • 27
    • 0029972684 scopus 로고    scopus 로고
    • EspA, a protein secreted by enteropathogenic Escherichia coli, is required to induce signals in epithelial cells
    • Kenny B, Lai LC, Finlay BB, Donnenberg MS. EspA, a protein secreted by enteropathogenic Escherichia coli, is required to induce signals in epithelial cells. Mol Microbiol 1996, 20:313-323.
    • (1996) Mol Microbiol , vol.20 , pp. 313-323
    • Kenny, B.1    Lai, L.C.2    Finlay, B.B.3    Donnenberg, M.S.4
  • 28
    • 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 DJ, Frey EA, Finlay BB. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 1997, 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
  • 29
    • 0036096793 scopus 로고    scopus 로고
    • Co-ordinate regulation of distinct host cell signalling pathways by multifunctional enteropathogenic Escherichia coli effector molecules
    • Kenny B, Ellis S, Leard AD, Warawa J, Mellor H, Jepson MA. Co-ordinate regulation of distinct host cell signalling pathways by multifunctional enteropathogenic Escherichia coli effector molecules. Mol Microbiol 2002, 44:1095-1107.
    • (2002) Mol Microbiol , vol.44 , pp. 1095-1107
    • Kenny, B.1    Ellis, S.2    Leard, A.D.3    Warawa, J.4    Mellor, H.5    Jepson, M.A.6
  • 30
    • 25444461419 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes
    • Kim DW, Lenzen G, Page AL, Legrain P, Sansonetti PJ, Parsot C. The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proc Natl Acad Sci USA 2005, 102:14046-14051.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14046-14051
    • Kim, D.W.1    Lenzen, G.2    Page, A.L.3    Legrain, P.4    Sansonetti, P.J.5    Parsot, C.6
  • 31
    • 33746155723 scopus 로고    scopus 로고
    • Calpain involvement in the remodeling of cytoskeletal anchorage complexes
    • Lebart MC, Benyamin Y. Calpain involvement in the remodeling of cytoskeletal anchorage complexes. FEBS J 2006, 273:3415-3426.
    • (2006) FEBS J , vol.273 , pp. 3415-3426
    • Lebart, M.C.1    Benyamin, Y.2
  • 32
    • 0021825282 scopus 로고
    • The diarrheal response of humans to some classic serotypes of enteropathogenic Escherichia coli is dependent on a plasmid encoding an enteroadhesiveness factor
    • Levine MM, Nataro JP, Karch H, Baldini MM, Kaper JB, Black RE. The diarrheal response of humans to some classic serotypes of enteropathogenic Escherichia coli is dependent on a plasmid encoding an enteroadhesiveness factor. J Infect Dis 1985, 152:550-559.
    • (1985) J Infect Dis , vol.152 , pp. 550-559
    • Levine, M.M.1    Nataro, J.P.2    Karch, H.3    Baldini, M.M.4    Kaper, J.B.5    Black, R.E.6    et al7
  • 33
    • 0035341210 scopus 로고    scopus 로고
    • Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin
    • McGhie EJ, Hayward RD, Koronakis V. Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin. EMBO J 2001, 20:2131-2139.
    • (2001) EMBO J , vol.20 , pp. 2131-2139
    • McGhie, E.J.1    Hayward, R.D.2    Koronakis, V.3
  • 35
    • 0034018023 scopus 로고    scopus 로고
    • Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2
    • Marches O, Nougayrede JP, Boullier S, Mainil J, Charlier G, Raymond I. Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2. Infect Immun 2000, 68:2171-2182.
    • (2000) Infect Immun , vol.68 , pp. 2171-2182
    • Marches, O.1    Nougayrede, J.P.2    Boullier, S.3    Mainil, J.4    Charlier, G.5    Raymond, I.6    et al7
  • 36
    • 10744230521 scopus 로고    scopus 로고
    • Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition
    • Marches O, Ledger TN, Boury M, Ohara M, Tu X, Goffaux F. Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition. Mol Microbiol 2003, 50:1553-1567.
    • (2003) Mol Microbiol , vol.50 , pp. 1553-1567
    • Marches, O.1    Ledger, T.N.2    Boury, M.3    Ohara, M.4    Tu, X.5    Goffaux, F.6    et al7
  • 37
    • 4644236321 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli activates the RhoA signaling pathway via the stimulation of GEF-H1
    • Matsuzawa T, Kuwae A, Yoshida S, Sasakawa C, Abe A. Enteropathogenic Escherichia coli activates the RhoA signaling pathway via the stimulation of GEF-H1. EMBO J 2004, 23:3570-3582.
    • (2004) EMBO J , vol.23 , pp. 3570-3582
    • Matsuzawa, T.1    Kuwae, A.2    Yoshida, S.3    Sasakawa, C.4    Abe, A.5
  • 38
    • 25444439530 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli type III effectors EspG and EspG2 alter epithelial paracellular permeability
    • Matsuzawa T, Kuwae A, Abe A. Enteropathogenic Escherichia coli type III effectors EspG and EspG2 alter epithelial paracellular permeability. Infect Immun 2005, 73:6283-6289.
    • (2005) Infect Immun , vol.73 , pp. 6283-6289
    • Matsuzawa, T.1    Kuwae, A.2    Abe, A.3
  • 39
    • 38849122594 scopus 로고    scopus 로고
    • Real-time analysis of effector translocation by the type III secretion system of enteropathogenic Escherichia coli
    • Mills E, Baruch K, Charpentier X, Kobi S, Rosenshine I. Real-time analysis of effector translocation by the type III secretion system of enteropathogenic Escherichia coli. Cell Host Microbe 2008, 3:104-113.
    • (2008) Cell Host Microbe , vol.3 , pp. 104-113
    • Mills, E.1    Baruch, K.2    Charpentier, X.3    Kobi, S.4    Rosenshine, I.5
  • 40
    • 26844442270 scopus 로고    scopus 로고
    • Binding of intimin with Tir on the bacterial surface is prerequisite for the barrier disruption induced by enteropathogenic Escherichia coli
    • Miyake M, Hanajima M, Matsuzawa T, Kobayashi C, Minami M, Abe A, Horiguchi Y. Binding of intimin with Tir on the bacterial surface is prerequisite for the barrier disruption induced by enteropathogenic Escherichia coli. Biochem Biophys Res Commun 2005, 337:922-927.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 922-927
    • Miyake, M.1    Hanajima, M.2    Matsuzawa, T.3    Kobayashi, C.4    Minami, M.5    Abe, A.6    Horiguchi, Y.7
  • 41
    • 0344851638 scopus 로고    scopus 로고
    • Disruption of cell polarity by enteropathogenic Escherichia coli enables basolateral membrane proteins to migrate apically and to potentiate physiological consequences
    • Muza-Moons MM, Koutsouris A, Hecht G. Disruption of cell polarity by enteropathogenic Escherichia coli enables basolateral membrane proteins to migrate apically and to potentiate physiological consequences. Infect Immun 2003, 71:7069-7078.
    • (2003) Infect Immun , vol.71 , pp. 7069-7078
    • Muza-Moons, M.M.1    Koutsouris, A.2    Hecht, G.3
  • 42
    • 6344235634 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway
    • Nougayrede JP, Donnenberg MS. Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway. Cell Microbiol 2004, 6:1097-1111.
    • (2004) Cell Microbiol , vol.6 , pp. 1097-1111
    • Nougayrede, J.P.1    Donnenberg, M.S.2
  • 43
    • 51949110637 scopus 로고    scopus 로고
    • EspF Interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability
    • Peralta-Ramirez J, Hernandez JM, Manning-Cela R, Luna-Munoz J, Garcia-Tovar C, Nougayrede JP. EspF Interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability. Infect Immun 2008, 76:3854-3868.
    • (2008) Infect Immun , vol.76 , pp. 3854-3868
    • Peralta-Ramirez, J.1    Hernandez, J.M.2    Manning-Cela, R.3    Luna-Munoz, J.4    Garcia-Tovar, C.5    Nougayrede, J.P.6    et al7
  • 44
    • 0042029685 scopus 로고    scopus 로고
    • Calpain regulates enterocyte brush border actin assembly and pathogenic Escherichia coli-mediated effacement
    • Potter DA, Srirangam A, Fiacco KA, Brocks D, Hawes J, Herndon C. Calpain regulates enterocyte brush border actin assembly and pathogenic Escherichia coli-mediated effacement. J Biol Chem 2003, 278:30403-30412.
    • (2003) J Biol Chem , vol.278 , pp. 30403-30412
    • Potter, D.A.1    Srirangam, A.2    Fiacco, K.A.3    Brocks, D.4    Hawes, J.5    Herndon, C.6    et al7
  • 45
    • 33646357752 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli EspF effector molecule inhibits PI-3 kinase-mediated uptake independently of mitochondrial targeting
    • Quitard S, Dean P, Maresca M, Kenny B. The enteropathogenic Escherichia coli EspF effector molecule inhibits PI-3 kinase-mediated uptake independently of mitochondrial targeting. Cell Microbiol 2006, 8:972-981.
    • (2006) Cell Microbiol , vol.8 , pp. 972-981
    • Quitard, S.1    Dean, P.2    Maresca, M.3    Kenny, B.4
  • 46
    • 34447638896 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli (EPEC) inactivate innate immune responses prior to compromising epithelial barrier function
    • Ruchaud-Sparagano MH, Maresca M, Kenny B. Enteropathogenic Escherichia coli (EPEC) inactivate innate immune responses prior to compromising epithelial barrier function. Cell Microbiol 2007, 9:1909-1921.
    • (2007) Cell Microbiol , vol.9 , pp. 1909-1921
    • Ruchaud-Sparagano, M.H.1    Maresca, M.2    Kenny, B.3
  • 49
    • 21544465048 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli type III effectors EspG and EspG2 disrupt the microtubule network of intestinal epithelial cells
    • Shaw RK, Smollett K, Cleary J, Garmendia J, Straatman-Iwanowska A, Frankel G, Knutton S. Enteropathogenic Escherichia coli type III effectors EspG and EspG2 disrupt the microtubule network of intestinal epithelial cells. Infect Immun 2005a, 73:4385-4390.
    • (2005) Infect Immun , vol.73 , pp. 4385-4390
    • Shaw, R.K.1    Smollett, K.2    Cleary, J.3    Garmendia, J.4    Straatman-Iwanowska, A.5    Frankel, G.6    Knutton, S.7
  • 50
    • 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 RK, Cleary J, Murphy MS, Frankel G, Knutton S. 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 2005b, 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
  • 51
    • 0036227735 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli induces modification of the focal adhesions of infected host cells
    • Shifrin Y, Kirschner J, Geiger B, Rosenshine I. Enteropathogenic Escherichia coli induces modification of the focal adhesions of infected host cells. Cell Microbiol 2002, 4:235-243.
    • (2002) Cell Microbiol , vol.4 , pp. 235-243
    • Shifrin, Y.1    Kirschner, J.2    Geiger, B.3    Rosenshine, I.4
  • 52
    • 0033853899 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions
    • Simonovic I, Rosenberg J, Koutsouris A, Hecht G. Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions. Cell Microbiol 2000, 2:305-315.
    • (2000) Cell Microbiol , vol.2 , pp. 305-315
    • Simonovic, I.1    Rosenberg, J.2    Koutsouris, A.3    Hecht, G.4
  • 53
    • 77649211841 scopus 로고    scopus 로고
    • The bacterial virulence factor NleA is required for the disruption of intestinal tight junctions by enteropathogenic Escherichia coli
    • Thanabalasuriar A, Koutsouris A, Weflen A, Mimee M, Hecht G, Gruenheid S. The bacterial virulence factor NleA is required for the disruption of intestinal tight junctions by enteropathogenic Escherichia coli. Cell Microbiol 2010, 12:31-41.
    • (2010) Cell Microbiol , vol.12 , pp. 31-41
    • Thanabalasuriar, A.1    Koutsouris, A.2    Weflen, A.3    Mimee, M.4    Hecht, G.5    Gruenheid, S.6
  • 54
    • 17144379342 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli EspG disrupts microtubules and in conjunction with Orf3 enhances perturbation of the tight junction barrier
    • Tomson FL, Viswanathan VK, Kanack KJ, Kanteti RP, Straub KV, Menet M. Enteropathogenic Escherichia coli EspG disrupts microtubules and in conjunction with Orf3 enhances perturbation of the tight junction barrier. Mol Microbiol 2005, 56:447-464.
    • (2005) Mol Microbiol , vol.56 , pp. 447-464
    • Tomson, F.L.1    Viswanathan, V.K.2    Kanack, K.J.3    Kanteti, R.P.4    Straub, K.V.5    Menet, M.6    et al7
  • 55
    • 30944434681 scopus 로고    scopus 로고
    • Changes in tight junctional resistance of the cervical epithelium are associated with modulation of content and phosphorylation of occludin 65-kilodalton and 50-kilodalton forms
    • Zhu L, Li X, Zeng R, Gorodeski GI. Changes in tight junctional resistance of the cervical epithelium are associated with modulation of content and phosphorylation of occludin 65-kilodalton and 50-kilodalton forms. Endocrinology 2006, 147:977-989.
    • (2006) Endocrinology , vol.147 , pp. 977-989
    • Zhu, L.1    Li, X.2    Zeng, R.3    Gorodeski, G.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.