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mBio
Volumn 7, Issue 3, 2016, Pages
EspC, an autotransporter protein secreted by enteropathogenic Escherichia coli, causes apoptosis and necrosis through caspase and calpain activation, including direct procaspase-3 cleavage
Author keywords

[No Author keywords available]
Indexed keywords

CALPAIN; CASPASE; CASPASE 3; CASPASE 9; CYTOCHROME C; ESCHERICHIA COLI PROTEIN; ESPC PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROCASPASE 3; PROTEIN BAX; PROTEIN BCL 2; UNCLASSIFIED DRUG; ESPC PROTEIN, E COLI;
EID: 84978933826     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00479-16     Document Type: Article
Times cited : (28)
References (70)
  • 2
    • 0020508377 scopus 로고
    • Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines
    • Moon HW, Whipp SC, Argenzio RA, Levine MM, Giannella RA. 1983. Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines. Infect Immun 41: 1340-1351.
    • (1983) Infect Immun , vol.41 , pp. 1340-1351
    • Moon, H.W.1    Whipp, S.C.2    Argenzio, R.A.3    Levine, M.M.4    Giannella, R.A.5
  • 3
    • 0028945803 scopus 로고
    • A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens
    • McDaniel TK, Jarvis KG, Donnenberg MS, Kaper JB. 1995. A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proc Natl Acad Sci U S A 92: 1664-1668. http://dx.doi.org/10.1073/pnas.92.5.1664.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1664-1668
    • McDaniel, T.K.1    Jarvis, K.G.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 4
    • 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. 1997. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91: 511-520. http://dx.doi.org/10.1016/S0092-8674(00)80437-7.
    • (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
  • 5
    • 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. 2001. EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella flexneri. Infect Immun 69: 4027-4033. http://dx.doi.org/10.1128/IAI.69.6.4027-4033.2001.
    • (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
  • 6
    • 0035095037 scopus 로고    scopus 로고
    • Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function
    • McNamara BP, Koutsouris A, O’Connell CB, Nougayréde JP, Donnenberg MS, Hecht G. 2001. Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function. J Clin Invest 107: 621-629. http://dx.doi.org/10.1172/JCI11138.
    • (2001) J Clin Invest , vol.107 , pp. 621-629
    • McNamara, B.P.1    Koutsouris, A.2    O’Connell, C.B.3    Nougayréde, J.P.4    Donnenberg, M.S.5    Hecht, G.6
  • 8
    • 84925248876 scopus 로고    scopus 로고
    • Bringing down the host: Enteropathogenic and enterohaemorrhagic Escherichia coli effector-mediated subversion of host innate immune pathways
    • Santos AS, Finlay BB. 2015. Bringing down the host: enteropathogenic and enterohaemorrhagic Escherichia coli effector-mediated subversion of host innate immune pathways. Cell Microbiol 17: 318-332. http:// dx.doi.org/10.1111/cmi.12412.
    • (2015) Cell Microbiol , vol.17 , pp. 318-332
    • Santos, A.S.1    Finlay, B.B.2
  • 9
    • 84930986928 scopus 로고    scopus 로고
    • Role of virulence factors on host inflammatory response induced by diarrheagenic Escherichia coli pathotypes
    • Sanchez-Villamil J, Navarro-Garcia F. 2015. Role of virulence factors on host inflammatory response induced by diarrheagenic Escherichia coli pathotypes. Future Microbiol 10: 1009-1033. http://dx.doi.org/10.2217/ fmb.15.17.
    • (2015) Future Microbiol , vol.10 , pp. 1009-1033
    • Sanchez-Villamil, J.1    Navarro-Garcia, F.2
  • 10
    • 6344235634 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway
    • Nougayrède JP, Donnenberg MS. 2004. Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway. Cell Microbiol 6: 1097-1111. http://dx.doi.org/10.1111/j.1462-5822.2004.00421.x.
    • (2004) Cell Microbiol , vol.6 , pp. 1097-1111
    • Nougayrède, J.P.1    Donnenberg, M.S.2
  • 11
    • 84905252142 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli dynamically regulates EGFR signaling in intestinal epithelial cells
    • Roxas JL, Ryan K, Vedantam G, Viswanathan VK. 2014. Enteropathogenic Escherichia coli dynamically regulates EGFR signaling in intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol 307: G374-G380. http://dx.doi.org/10.1152/ajpgi.00312.2013.
    • (2014) Am J Physiol Gastrointest Liver Physiol , vol.307
    • Roxas, J.L.1    Ryan, K.2    Vedantam, G.3    Viswanathan, V.K.4
  • 12
    • 0035048465 scopus 로고    scopus 로고
    • Role of EspF in host cell death induced by enteropathogenic Escherichia coli
    • Crane JK, McNamara BP, Donnenberg MS. 2001. Role of EspF in host cell death induced by enteropathogenic Escherichia coli. Cell Microbiol 3: 197-211. http://dx.doi.org/10.1046/j.1462-5822.2001.00103.x.
    • (2001) Cell Microbiol , vol.3 , pp. 197-211
    • Crane, J.K.1    McNamara, B.P.2    Donnenberg, M.S.3
  • 13
    • 13244259426 scopus 로고    scopus 로고
    • Targeting of enteropathogenic Escherichia coli EspF to host mitochondria is essential for bacterial pathogenesis: Critical role of the 16th leucine residue in EspF
    • Nagai T, Abe A, Sasakawa C. 2005. Targeting of enteropathogenic Escherichia coli EspF to host mitochondria is essential for bacterial pathogenesis: critical role of the 16th leucine residue in EspF. J Biol Chem 280: 2998-3011. http://dx.doi.org/10.1074/jbc.M411550200.
    • (2005) J Biol Chem , vol.280 , pp. 2998-3011
    • Nagai, T.1    Abe, A.2    Sasakawa, C.3
  • 14
    • 33846911072 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2
    • Nougayrède JP, Foster GH, Donnenberg MS. 2007. Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2. Cell Microbiol 9: 680-693. http://dx.doi.org/10.1111/j.1462-5822.2006.00820.x.
    • (2007) Cell Microbiol , vol.9 , pp. 680-693
    • Nougayrède, J.P.1    Foster, G.H.2    Donnenberg, M.S.3
  • 15
    • 0034518855 scopus 로고    scopus 로고
    • Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria
    • Kenny B, Jepson M. 2000. Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria. Cell Microbiol 2: 579-590. http://dx.doi.org/10.1046/j.1462-5822.2000.00082.x.
    • (2000) Cell Microbiol , vol.2 , pp. 579-590
    • Kenny, B.1    Jepson, M.2
  • 16
    • 33748449456 scopus 로고    scopus 로고
    • Citrobacter rodentium infection causes both mitochondrial dysfunction and intestinal epithelial barrier disruption in vivo: Role of mitochondrial associated protein (Map)
    • Ma C, Wickham ME, Guttman JA, Deng W, Walker J, Madsen KL, Jacobson K, Vogl WA, Finlay BB, Vallance BA. 2006. Citrobacter rodentium infection causes both mitochondrial dysfunction and intestinal epithelial barrier disruption in vivo: role of mitochondrial associated protein (Map). Cell Microbiol 8: 1669-1686. http://dx.doi.org/10.1111/j.1462-5822.2006.00741.x.
    • (2006) Cell Microbiol , vol.8 , pp. 1669-1686
    • Ma, C.1    Wickham, M.E.2    Guttman, J.A.3    Deng, W.4    Walker, J.5    Madsen, K.L.6    Jacobson, K.7    Vogl, W.A.8    Finlay, B.B.9    Vallance, B.A.10
  • 17
    • 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. 2002. Co-ordinate regulation of distinct host cell signalling pathways by multifunctional enteropathogenic Escherichia coli effector molecules. Mol Microbiol 44: 1095-1107. http://dx.doi.org/10.1046/j.1365-2958.2002.02952.x.
    • (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
  • 18
    • 33644866844 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli (EPEC) Map effector is imported into the mitochondrial matrix by the TOM/Hsp70 system and alters organelle morphology
    • Papatheodorou P, Domańska G, Oxle M, Mathieu J, Selchow O, Kenny B, Rassow J. 2006. The enteropathogenic Escherichia coli (EPEC) Map effector is imported into the mitochondrial matrix by the TOM/Hsp70 system and alters organelle morphology. Cell Microbiol 8: 677-689. http:// dx.doi.org/10.1111/j.1462-5822.2005.00660.x.
    • (2006) Cell Microbiol , vol.8 , pp. 677-689
    • Papatheodorou, P.1    Domańska, G.2    Oxle, M.3    Mathieu, J.4    Selchow, O.5    Kenny, B.6    Rassow, J.7
  • 19
    • 10744230521 scopus 로고    scopus 로고
    • Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycleG2/M transition
    • Marchès O, Ledger TN, Boury M, Ohara M, Tu X, Goffaux F, Mainil J, Rosenshine I, Sugai M, De Rycke J, Oswald E. 2003. Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycleG2/M transition. Mol Microbiol 50: 1553-1567. http://dx.doi.org/10.1046/j.1365-2958.2003.03821.x.
    • (2003) Mol Microbiol , vol.50 , pp. 1553-1567
    • Marchès, O.1    Ledger, T.N.2    Boury, M.3    Ohara, M.4    Tu, X.5    Goffaux, F.6    Mainil, J.7    Rosenshine, I.8    Sugai, M.9    De Rycke, J.10    Oswald, E.11
  • 20
    • 33750577279 scopus 로고    scopus 로고
    • Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway
    • Taieb F, Nougayrède JP, Watrin C, Samba-Louaka A, Oswald E. 2006. Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway. Cell Microbiol 8: 1910-1921. http://dx.doi.org/10.1111/j.1462-5822.2006.00757.x.
    • (2006) Cell Microbiol , vol.8 , pp. 1910-1921
    • Taieb, F.1    Nougayrède, J.P.2    Watrin, C.3    Samba-Louaka, A.4    Oswald, E.5
  • 21
    • 84954358763 scopus 로고    scopus 로고
    • Structure of the cyclomodulin Cif from pathogenic Escherichia coli
    • Hsu Y, Jubelin G, Taieb F, Nougayrède JP, Oswald E, Stebbins CE. 2008. Structure of the cyclomodulin Cif from pathogenic Escherichia coli. J Mol Biol 384: 465-477. http://dx.doi.org/10.1016/j.jmb.2008.09.051.
    • (2008) J Mol Biol , vol.384 , pp. 465-477
    • Hsu, Y.1    Jubelin, G.2    Taieb, F.3    Nougayrède, J.P.4    Oswald, E.5    Stebbins, C.E.6
  • 22
    • 55749091664 scopus 로고    scopus 로고
    • Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin-dependent kinase inhibitors p21 and p27
    • Samba-Louaka A, Nougayrède JP, Watrin C, Jubelin G, Oswald E, Taieb F. 2008. Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin-dependent kinase inhibitors p21 and p27. Cell Microbiol 10: 2496-2508. http://dx.doi.org/10.1111/j.1462-5822.2008.01224.x.
    • (2008) Cell Microbiol , vol.10 , pp. 2496-2508
    • Samba-Louaka, A.1    Nougayrède, J.P.2    Watrin, C.3    Jubelin, G.4    Oswald, E.5    Taieb, F.6
  • 24
    • 72449156546 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells
    • Samba-Louaka A, Nougayrède JP, Watrin C, Oswald E, Taieb F. 2009. The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells. Infect Immun 77: 5471-5477. http://dx.doi.org/10.1128/IAI.00860-09.
    • (2009) Infect Immun , vol.77 , pp. 5471-5477
    • Samba-Louaka, A.1    Nougayrède, J.P.2    Watrin, C.3    Oswald, E.4    Taieb, F.5
  • 25
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui J, Yao Q, Li S, Ding X, Lu Q, Mao H, Liu L, Zheng N, Chen S, Shao F. 2010. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science 329: 1215-1218. http:// dx.doi.org/10.1126/science.1193844.
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5    Mao, H.6    Liu, L.7    Zheng, N.8    Chen, S.9    Shao, F.10
  • 26
    • 77957153145 scopus 로고    scopus 로고
    • Interactions between bacterial pathogens and mitochondrial cell death pathways
    • Rudel T, Kepp O, Kozjak-Pavlovic V. 2010. Interactions between bacterial pathogens and mitochondrial cell death pathways. Nat Rev Microbiol 8: 693-705. http://dx.doi.org/10.1038/nrmicro2421.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 693-705
    • Rudel, T.1    Kepp, O.2    Kozjak-Pavlovic, V.3
  • 27
    • 84911484235 scopus 로고    scopus 로고
    • The cell death response to enteropathogenic Escherichia coli infection
    • Wong Fok Lung T, Pearson JS, Schuelein R, Hartland EL. 2014. The cell death response to enteropathogenic Escherichia coli infection. Cell Microbiol 16: 1736-1745. http://dx.doi.org/10.1111/cmi.12371.
    • (2014) Cell Microbiol , vol.16 , pp. 1736-1745
    • Wong Fok Lung, T.1    Pearson, J.S.2    Schuelein, R.3    Hartland, E.L.4
  • 28
    • 0035158936 scopus 로고    scopus 로고
    • espC pathogenicity island of enteropathogenic Escherichia coli encodes an enterotoxin
    • Mellies JL, Navarro-Garcia F, Okeke I, Frederickson J, Nataro JP, Kaper JB. 2001. espC pathogenicity island of enteropathogenic Escherichia coli encodes an enterotoxin. Infect Immun 69: 315-324. http://dx.doi.org/10.1128/IAI.69.1.315-324.2001.
    • (2001) Infect Immun , vol.69 , pp. 315-324
    • Mellies, J.L.1    Navarro-Garcia, F.2    Okeke, I.3    Frederickson, J.4    Nataro, J.P.5    Kaper, J.B.6
  • 29
    • 0029961503 scopus 로고    scopus 로고
    • Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins
    • Stein M, Kenny B, Stein MA, Finlay BB. 1996. Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins. J Bacteriol 178: 6546-6554.
    • (1996) J Bacteriol , vol.178 , pp. 6546-6554
    • Stein, M.1    Kenny, B.2    Stein, M.A.3    Finlay, B.B.4
  • 30
    • 84871886228 scopus 로고    scopus 로고
    • Autotransporter protein-encoding genes of diarrheagenic Escherichia coli are found in both typical and atypical enteropathogenic E. coli strains
    • Abreu AG, Bueris V, Porangaba TM, Sircili MP, Navarro-Garcia F, EliasWP. 2013. Autotransporter protein-encoding genes of diarrheagenic Escherichia coli are found in both typical and atypical enteropathogenic E. coli strains. Appl Environ Microbiol 79: 411-414. http://dx.doi.org/10.1128/AEM.02635-12.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 411-414
    • Abreu, A.G.1    Bueris, V.2    Porangaba, T.M.3    Sircili, M.P.4    Navarro-Garcia, F.5    Elias, W.P.6
  • 31
    • 33645519983 scopus 로고    scopus 로고
    • Efficient translocation of EspC into epithelial cells depends on enteropathogenic Escherichia coli and host cell contact
    • Vidal JE, Navarro-García F. 2006. Efficient translocation of EspC into epithelial cells depends on enteropathogenic Escherichia coli and host cell contact. Infect Immun 74: 2293-2303. http://dx.doi.org/10.1128/ IAI.74.4.2293-2303.2006.
    • (2006) Infect Immun , vol.74 , pp. 2293-2303
    • Vidal, J.E.1    Navarro-García, F.2
  • 32
    • 51449093493 scopus 로고    scopus 로고
    • EspC translocation into epithelial cells by enteropathogenic Escherichia coli requires a concerted participation of type V and III secretion systems
    • Vidal JE, Navarro-García F. 2008. EspC translocation into epithelial cells by enteropathogenic Escherichia coli requires a concerted participation of type V and III secretion systems. Cell Microbiol 10: 1975-1986. http:// dx.doi.org/10.1111/j.1462-5822.2008.01181.x.
    • (2008) Cell Microbiol , vol.10 , pp. 1975-1986
    • Vidal, J.E.1    Navarro-García, F.2
  • 33
    • 2542576380 scopus 로고    scopus 로고
    • The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli
    • Navarro-García F, Canizalez-Roman A, Sui BQ, Nataro JP, Azamar Y. 2004. The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli. Infect Immun 72: 3609-3621. http://dx.doi.org/10.1128/IAI.72.6.3609-3621.2004.
    • (2004) Infect Immun , vol.72 , pp. 3609-3621
    • Navarro-García, F.1    Canizalez-Roman, A.2    Sui, B.Q.3    Nataro, J.P.4    Azamar, Y.5
  • 34
    • 84900410436 scopus 로고    scopus 로고
    • EspC promotes epithelial cell detachment by enteropathogenic Escherichia coli via sequential cleavages of a cytoskeletal protein and then focal adhesion proteins
    • Navarro-Garcia F, Serapio-Palacios A, Vidal JE, Salazar MI, Tapia-Pastrana G. 2014. EspC promotes epithelial cell detachment by enteropathogenic Escherichia coli via sequential cleavages of a cytoskeletal protein and then focal adhesion proteins. Infect Immun 82: 2255-2265. http:// dx.doi.org/10.1128/IAI.01386-13.
    • (2014) Infect Immun , vol.82 , pp. 2255-2265
    • Navarro-Garcia, F.1    Serapio-Palacios, A.2    Vidal, J.E.3    Salazar, M.I.4    Tapia-Pastrana, G.5
  • 35
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang KK. 2000. Calpain and caspase: can you tell the difference? Trends Neurosci 23: 20-26. http://dx.doi.org/10.1016/S0166-2236(99)01479-4.
    • (2000) Trends Neurosci , vol.23 , pp. 20-26
    • Wang, K.K.1
  • 36
    • 0034105784 scopus 로고    scopus 로고
    • Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes
    • Cain K, Bratton SB, Langlais C, Walker G, Brown DG, Sun XM, Cohen GM. 2000. Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes. J Biol Chem 275: 6067-6070. http://dx.doi.org/10.1074/jbc.275.9.6067.
    • (2000) J Biol Chem , vol.275 , pp. 6067-6070
    • Cain, K.1    Bratton, S.B.2    Langlais, C.3    Walker, G.4    Brown, D.G.5    Sun, X.M.6    Cohen, G.M.7
  • 37
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green DR, Kroemer G. 2004. The pathophysiology of mitochondrial cell death. Science 305: 626-629. http://dx.doi.org/10.1126/science.1099320.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 38
    • 0035544583 scopus 로고    scopus 로고
    • Two-color fluorescence detection of poly(ADP-ribose) polymerase-1 (PARP-1) cleavage andDNAstrand breaks in etoposide-induced apoptotic cells
    • Soldani C, Bottone MG, Pellicciari C, Scovassi AI. 2001. Two-color fluorescence detection of poly(ADP-ribose) polymerase-1 (PARP-1) cleavage andDNAstrand breaks in etoposide-induced apoptotic cells. Eur J Histochem 45: 389-392. http://dx.doi.org/10.4081/1648.
    • (2001) Eur J Histochem , vol.45 , pp. 389-392
    • Soldani, C.1    Bottone, M.G.2    Pellicciari, C.3    Scovassi, A.I.4
  • 39
    • 0029155828 scopus 로고
    • Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells
    • Kenny B, Finlay BB. 1995. Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells. Proc Natl Acad Sci U S A 92: 7991-7995. http://dx.doi.org/10.1073/pnas.92.17.7991.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7991-7995
    • Kenny, B.1    Finlay, B.B.2
  • 41
    • 0030867842 scopus 로고    scopus 로고
    • Cleavage of focal adhesion kinase by caspases during apoptosis
    • Wen LP, Fahrni JA, Troie S, Guan JL, Orth K, Rosen GD. 1997. Cleavage of focal adhesion kinase by caspases during apoptosis. J Biol Chem 272: 26056-26061. http://dx.doi.org/10.1074/jbc.272.41.26056.
    • (1997) J Biol Chem , vol.272 , pp. 26056-26061
    • Wen, L.P.1    Fahrni, J.A.2    Troie, S.3    Guan, J.L.4    Orth, K.5    Rosen, G.D.6
  • 42
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1beta-convertingenzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R, Raser KJ, Stafford D, Hajimohammadreza I, Posner A, Allen H, Talanian RV, Yuen P, Gilbertsen RB, Wang KK. 1996. Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1beta-convertingenzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochem J 319: 683-690. http:// dx.doi.org/10.1042/bj3190683.
    • (1996) Biochem J , vol.319 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6    Talanian, R.V.7    Yuen, P.8    Gilbertsen, R.B.9    Wang, K.K.10
  • 43
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • Jänicke RU, Ng P, Sprengart ML, Porter AG. 1998. Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J Biol Chem 273: 15540-15545. http://dx.doi.org/10.1074/jbc.273.25.15540.
    • (1998) J Biol Chem , vol.273 , pp. 15540-15545
    • Jänicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 44
    • 84883755553 scopus 로고    scopus 로고
    • Mitochondrial regulation of cell death
    • Tait SW, Green DR. 2013. Mitochondrial regulation of cell death. Cold Spring Harbor Perspect Biol 5: a008706. http://dx.doi.org/10.1101/ cshperspect.a008706.
    • (2013) Cold Spring Harbor Perspect Biol , vol.5
    • Tait, S.W.1    Green, D.R.2
  • 45
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S, Martinou JC. 2000. Mitochondria as the central control point of apoptosis. Trends Cell Biol 10: 369-377. http://dx.doi.org/10.1016/S0962-8924(00)01803-1.
    • (2000) Trends Cell Biol , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 46
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. 2007. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87: 99-163. http://dx.doi.org/10.1152/physrev.00013.2006.
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 48
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489. http://dx.doi.org/10.1016/S0092-8674(00)80434-1.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 49
    • 0032085941 scopus 로고    scopus 로고
    • Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
    • Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES. 1998. Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell 1: 949-957. http://dx.doi.org/10.1016/S1097-2765(00)80095-7.
    • (1998) Mol Cell , vol.1 , pp. 949-957
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Alnemri, E.S.4
  • 50
    • 77956908962 scopus 로고    scopus 로고
    • Regulation of the Apaf-1-caspase-9 apoptosome
    • Bratton SB, Salvesen GS. 2010. Regulation of the Apaf-1-caspase-9 apoptosome. J Cell Sci 123: 3209-3214. http://dx.doi.org/10.1242/jcs.073643.
    • (2010) J Cell Sci , vol.123 , pp. 3209-3214
    • Bratton, S.B.1    Salvesen, G.S.2
  • 52
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC. 1994. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371: 346-347. http://dx.doi.org/10.1038/371346a0.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 53
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis
    • Kaufmann SH, Desnoyers S, Ottaviano Y, Davidson NE, Poirier GG. 1993. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res 53: 3976-3985.
    • (1993) Cancer Res , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 54
    • 84938790688 scopus 로고    scopus 로고
    • The serine protease EspC from enteropathogenic Escherichia coli regulates pore formation and cytotoxicity mediated by the type III secretion system
    • Guignot J, Segura A, Tran Van Nhieu G. 2015. The serine protease EspC from enteropathogenic Escherichia coli regulates pore formation and cytotoxicity mediated by the type III secretion system. PLoS Pathog 11: e1005013. http://dx.doi.org/10.1371/journal.ppat.1005013.
    • (2015) PLoS Pathog , vol.11
    • Guignot, J.1    Segura, A.2    Tran Van Nhieu, G.3
  • 55
    • 84871886228 scopus 로고    scopus 로고
    • Autotransporter protein-encoding genes of diarrheagenic Escherichia coli are found in both typical and atypical enteropathogenic E. coli strains
    • Abreu AG, Bueris V, Porangaba TM, Sircili MP, Navarro-Garcia F, EliasWP. 2013. Autotransporter protein-encoding genes of diarrheagenic Escherichia coli are found in both typical and atypical enteropathogenic E. coli strains. Appl Environ Microbiol 79: 411-414. http://dx.doi.org/10.1128/AEM.02635-12.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 411-414
    • Abreu, A.G.1    Bueris, V.2    Porangaba, T.M.3    Sircili, M.P.4    Navarro-Garcia, F.5    Elias, W.P.6
  • 56
    • 78049491292 scopus 로고    scopus 로고
    • Distribution of non-locus of enterocyte effacement pathogenic island-related genes in Escherichia coli carrying eae from patients with diarrhea and healthy individuals in Japan
    • Narimatsu H, Ogata K, Makino Y, Ito K. 2010. Distribution of non-locus of enterocyte effacement pathogenic island-related genes in Escherichia coli carrying eae from patients with diarrhea and healthy individuals in Japan. J Clin Microbiol 48: 4107-4114. http://dx.doi.org/10.1128/ JCM.00677-10.
    • (2010) J Clin Microbiol , vol.48 , pp. 4107-4114
    • Narimatsu, H.1    Ogata, K.2    Makino, Y.3    Ito, K.4
  • 57
  • 59
    • 82755189495 scopus 로고    scopus 로고
    • Calpains: An elaborate proteolytic system
    • Ono Y, Sorimachi H. 2012. Calpains: an elaborate proteolytic system. Biochim Biophys Acta 1824: 224-236. http://dx.doi.org/10.1016/ j.bbapap.2011.08.005.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 224-236
    • Ono, Y.1    Sorimachi, H.2
  • 60
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A. 2006. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 7: 880-885. http://dx.doi.org/10.1038/sj.embor.7400779.
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 63
    • 84976875392 scopus 로고    scopus 로고
    • The subdomain 2 of the autotransporter Pet is the ligand site for recognizing Pet receptor on the epithelial cell surface
    • 25 April
    • Chavez-Dueñas L, Serapio-Palacios A, Nava-Acosta R, Navarro-Garcia F. 25 April 2016. The subdomain 2 of the autotransporter Pet is the ligand site for recognizing Pet receptor on the epithelial cell surface. Infect Immun http://dx.doi.org/10.1128/IAI.01528-15.
    • (2016) Infect Immun
    • Chavez-Dueñas, L.1    Serapio-Palacios, A.2    Nava-Acosta, R.3    Navarro-Garcia, F.4
  • 64
    • 0029933731 scopus 로고    scopus 로고
    • A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation
    • Rosenshine I, Ruschkowski S, Stein M, Reinscheid DJ, Mills SD, Finlay BB. 1996. A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation. EMBO J 15: 2613-2624.
    • (1996) EMBO J , vol.15 , pp. 2613-2624
    • Rosenshine, I.1    Ruschkowski, S.2    Stein, M.3    Reinscheid, D.J.4    Mills, S.D.5    Finlay, B.B.6
  • 65
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645. http://dx.doi.org/10.1073/pnas.120163297.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 66
    • 79959995937 scopus 로고    scopus 로고
    • Ion channel inhibitors block caspase activation by mechanisms other than restoring intracellular potassium concentration
    • Benítez-Rangel E, García L, Namorado MC, Reyes JL, Guerrero-Hernández A. 2011. Ion channel inhibitors block caspase activation by mechanisms other than restoring intracellular potassium concentration. Cell Death Dis 2: e113. http://dx.doi.org/10.1038/cddis.2010.93.
    • (2011) Cell Death Dis , vol.2
    • Benítez-Rangel, E.1    García, L.2    Namorado, M.C.3    Reyes, J.L.4    Guerrero-Hernández, A.5
  • 67
    • 4644286884 scopus 로고    scopus 로고
    • Assaying cytochrome c translocation during apoptosis
    • Waterhouse NJ, Steel R, Kluck R, Trapani JA. 2004. Assaying cytochrome c translocation during apoptosis. Methods Mol Biol 284: 307-313. http://dx.doi.org/10.1385/1-59259-816-1: 307.
    • (2004) Methods Mol Biol , vol.284 , pp. 307-313
    • Waterhouse, N.J.1    Steel, R.2    Kluck, R.3    Trapani, J.A.4
  • 68
    • 0018148992 scopus 로고
    • Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are noninvasive
    • Levine MM, Bergquist EJ, Nalin DR, Waterman DH, Hornick RB, Young CR, Sotman S. 1978. Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are noninvasive. Lancet i: 1119-1122.
    • (1978) Lancet , vol.1 , pp. 1119-1122
    • Levine, M.M.1    Bergquist, E.J.2    Nalin, D.R.3    Waterman, D.H.4    Hornick, R.B.5    Young, C.R.6    Sotman, S.7
  • 69
    • 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 KG, Girón JA, Jerse AE, McDaniel TK, Donnenberg MS, Kaper JB. 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 U S A 92: 7996-8000. http://dx.doi.org/10.1073/pnas.92.17.7996.
    • (1995) Proc Natl Acad Sci U S A , 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
  • 70
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer HW, Roulland-Dussoix D. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol 41: 459-472. http://dx.doi.org/10.1016/0022-2836(69)90288-5.
    • (1969) J Mol Biol , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2

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