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Volumn 102, Issue 1, 2016, Pages 22-36

Structural organization of membrane-inserted hexamers formed by Helicobacter pylori VacA toxin

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OLIGOMER; PROTEIN P33; PROTEIN P55; PROTEIN VARIANT; VACUOLATING TOXIN;

EID: 84988464628     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.13443     Document Type: Article
Times cited : (16)

References (88)
  • 1
    • 0036307727 scopus 로고    scopus 로고
    • Multiple oligomeric states of the Helicobacter pylori vacuolating toxin demonstrated by cryo-electron microscopy
    • Adrian, M., Cover, T.L., Dubochet, J., and Heuser, J.E. (2002) Multiple oligomeric states of the Helicobacter pylori vacuolating toxin demonstrated by cryo-electron microscopy. J Mol Biol 318: 121–133.
    • (2002) J Mol Biol , vol.318 , pp. 121-133
    • Adrian, M.1    Cover, T.L.2    Dubochet, J.3    Heuser, J.E.4
  • 2
    • 37349009928 scopus 로고    scopus 로고
    • Host-bacterial interactions in Helicobacter pylori infection
    • Amieva, M.R. and El-Omar, E.M. (2008) Host-bacterial interactions in Helicobacter pylori infection. Gastroenterology 134: 306–323.
    • (2008) Gastroenterology , vol.134 , pp. 306-323
    • Amieva, M.R.1    El-Omar, E.M.2
  • 3
    • 0028694306 scopus 로고
    • Schistosomes, liver flukes and, Helicobacter pylori, IARC monographs on the evaluation of carcinogenic risks to humans
    • Anonymous (1994). Schistosomes, liver flukes and Helicobacter pylori IARC monographs on the evaluation of carcinogenic risks to humans. In International Agency for Research on Cancer (Lyons, France).
    • (1994) International Agency for Research on Cancer (Lyons, France)
  • 4
    • 33645740999 scopus 로고    scopus 로고
    • The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases
    • Atherton, J.C. (2006) The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases. Ann Rev Pathol 1: 63–96.
    • (2006) Ann Rev Pathol , vol.1 , pp. 63-96
    • Atherton, J.C.1
  • 5
    • 70349211747 scopus 로고    scopus 로고
    • Coadaptation of Helicobacter pylori and humans: Ancient history, modern implications
    • Atherton, J.C. and Blaser, M.J. (2009) Coadaptation of Helicobacter pylori and humans: Ancient history, modern implications. J Clin Invest 119: 2475–2487.
    • (2009) J Clin Invest , vol.119 , pp. 2475-2487
    • Atherton, J.C.1    Blaser, M.J.2
  • 6
    • 0029059733 scopus 로고
    • Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori. Association of specific vacA types with cytotoxin production and peptic ulceration
    • Atherton, J.C., Cao, P., Peek, R.M., Jr., Tummuru, M.K., Blaser, M.J., and Cover, T.L. (1995) Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori. Association of specific vacA types with cytotoxin production and peptic ulceration. J Biol Chem 270: 17771–17777.
    • (1995) J Biol Chem , vol.270 , pp. 17771-17777
    • Atherton, J.C.1    Cao, P.2    Peek, R.M.3    Tummuru, M.K.4    Blaser, M.J.5    Cover, T.L.6
  • 7
    • 0017035495 scopus 로고
    • Binding of triton X-100 to diphtheria toxin, crossreacting material 45, and their fragments
    • Boquet, P., Silverman, M.S., Pappenheimer, A.M., Jr, and Vernon, W.B. (1976) Binding of triton X-100 to diphtheria toxin, crossreacting material 45, and their fragments. Proc Natl Acad Sci U S A 73: 4449–4453.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 4449-4453
    • Boquet, P.1    Silverman, M.S.2    Pappenheimer, A.M.3    Vernon, W.B.4
  • 9
    • 0037021457 scopus 로고    scopus 로고
    • The vacuolating toxin of Helicobacter pylori mimicks the CFTR-mediated chloride conductance
    • Campello, S., Tombola, F., Cabrini, G., and Zoratti, M. (2002) The vacuolating toxin of Helicobacter pylori mimicks the CFTR-mediated chloride conductance. FEBS Lett 532: 237–240.
    • (2002) FEBS Lett , vol.532 , pp. 237-240
    • Campello, S.1    Tombola, F.2    Cabrini, G.3    Zoratti, M.4
  • 10
  • 12
    • 84960145647 scopus 로고    scopus 로고
    • Helicobacter pylori diversity and Gastric cancer risk
    • Cover, T.L. (2016) Helicobacter pylori diversity and Gastric cancer risk. mBio 7: e01869.
    • (2016) mBio , vol.7
    • Cover, T.L.1
  • 13
    • 15944418287 scopus 로고    scopus 로고
    • Helicobacter pylori VacA, a paradigm for toxin multifunctionality
    • Cover, T.L., and Blanke, S.R. (2005) Helicobacter pylori VacA, a paradigm for toxin multifunctionality. Nat Rev 3: 320–332.
    • (2005) Nat Rev , vol.3 , pp. 320-332
    • Cover, T.L.1    Blanke, S.R.2
  • 14
    • 65449190100 scopus 로고    scopus 로고
    • Helicobacter pylori in health and disease
    • Cover, T.L., and Blaser, M.J. (2009) Helicobacter pylori in health and disease. Gastroenterology 136: 1863–1873.
    • (2009) Gastroenterology , vol.136 , pp. 1863-1873
    • Cover, T.L.1    Blaser, M.J.2
  • 15
    • 0030809535 scopus 로고    scopus 로고
    • Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly
    • Cover, T.L., Hanson, P.I., and Heuser, J.E. (1997) Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly. J Cell Biol 138: 759–769.
    • (1997) J Cell Biol , vol.138 , pp. 759-769
    • Cover, T.L.1    Hanson, P.I.2    Heuser, J.E.3
  • 16
    • 0033515072 scopus 로고    scopus 로고
    • The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH
    • Czajkowsky, D.M., Iwamoto, H., Cover, T.L., and Shao, Z. (1999) The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH. Proc Natl Acad Sci U S A 96: 2001–2006.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2001-2006
    • Czajkowsky, D.M.1    Iwamoto, H.2    Cover, T.L.3    Shao, Z.4
  • 17
    • 27744597020 scopus 로고    scopus 로고
    • Mimicry of a host anion channel by a Helicobacter pylori pore-forming toxin
    • Czajkowsky, D.M., Iwamoto, H., Szabo, G., Cover, T.L., and Shao, Z. (2005) Mimicry of a host anion channel by a Helicobacter pylori pore-forming toxin. Biophys J 89: 3093–3101.
    • (2005) Biophys J , vol.89 , pp. 3093-3101
    • Czajkowsky, D.M.1    Iwamoto, H.2    Szabo, G.3    Cover, T.L.4    Shao, Z.5
  • 18
    • 15444378399 scopus 로고    scopus 로고
    • Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy
    • Dang, T.X., Hotze, E.M., Rouiller, I., Tweten, R.K., and Wilson-Kubalek, E.M. (2005) Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy. J Struct Biol 150: 100–108.
    • (2005) J Struct Biol , vol.150 , pp. 100-108
    • Dang, T.X.1    Hotze, E.M.2    Rouiller, I.3    Tweten, R.K.4    Wilson-Kubalek, E.M.5
  • 19
    • 0028818757 scopus 로고
    • Low pH activates the vacuolating toxin of Helicobacter pylori, which becomes acid and pepsin resistant
    • de Bernard, M., Papini, E., de Filippis, V., Gottardi, E., Telford, J., Manetti, R., et al. (1995) Low pH activates the vacuolating toxin of Helicobacter pylori, which becomes acid and pepsin resistant. J Biol Chem 270: 23937–23940.
    • (1995) J Biol Chem , vol.270 , pp. 23937-23940
    • de Bernard, M.1    Papini, E.2    de Filippis, V.3    Gottardi, E.4    Telford, J.5    Manetti, R.6
  • 20
    • 84861648384 scopus 로고    scopus 로고
    • Global burden of cancers attributable to infections in 2008: A review and synthetic analysis
    • de Martel, C., Ferlay, J., Franceschi, S., Vignat, J., Bray, F., Forman, D., and Plummer, M. (2012) Global burden of cancers attributable to infections in 2008: A review and synthetic analysis. Lancet Oncol 13: 607–615.
    • (2012) Lancet Oncol , vol.13 , pp. 607-615
    • de Martel, C.1    Ferlay, J.2    Franceschi, S.3    Vignat, J.4    Bray, F.5    Forman, D.6    Plummer, M.7
  • 22
    • 77954058611 scopus 로고    scopus 로고
    • Helicobacter pylori VacA toxin/subunit p34: Targeting of an anion channel to the inner mitochondrial membrane
    • Domanska, G., Motz, C., Meinecke, M., Harsman, A., Papatheodorou, P., Reljic, B., et al. (2010) Helicobacter pylori VacA toxin/subunit p34: Targeting of an anion channel to the inner mitochondrial membrane. PLoS Pathog 6: e1000878.
    • (2010) PLoS Pathog , vol.6
    • Domanska, G.1    Motz, C.2    Meinecke, M.3    Harsman, A.4    Papatheodorou, P.5    Reljic, B.6
  • 23
    • 25144442682 scopus 로고    scopus 로고
    • High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy
    • El-Bez, C., Adrian, M., Dubochet, J., and Cover, T.L. (2005) High resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryo-negative staining electron microscopy. J Struct Biol 151: 215–228.
    • (2005) J Struct Biol , vol.151 , pp. 215-228
    • El-Bez, C.1    Adrian, M.2    Dubochet, J.3    Cover, T.L.4
  • 24
    • 0037146297 scopus 로고    scopus 로고
    • Helicobacter pylori and interleukin 1 genotyping: An opportunity to identify high-risk individuals for gastric carcinoma
    • Figueiredo, C., Machado, J.C., Pharoah, P., Seruca, R., Sousa, S., Carvalho, R., et al. (2002) Helicobacter pylori and interleukin 1 genotyping: An opportunity to identify high-risk individuals for gastric carcinoma. J Natl Cancer Inst 94: 1680–1687.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 1680-1687
    • Figueiredo, C.1    Machado, J.C.2    Pharoah, P.3    Seruca, R.4    Sousa, S.5    Carvalho, R.6
  • 25
    • 84946077218 scopus 로고    scopus 로고
    • An investigation of the effect of membrane curvature on transmembrane-domain dependent protein sorting in lipid bilayers
    • Fossati, M., Goud, B., Borgese, N., and Manneville, J.B. (2014) An investigation of the effect of membrane curvature on transmembrane-domain dependent protein sorting in lipid bilayers. Cell Logistics 4: e29087.
    • (2014) Cell Logistics , vol.4
    • Fossati, M.1    Goud, B.2    Borgese, N.3    Manneville, J.B.4
  • 26
    • 0028869723 scopus 로고
    • Gastric carcinoma
    • Fuchs, C.S., and Mayer, R.J. (1995) Gastric carcinoma. N Engl J Med 333: 32–41.
    • (1995) N Engl J Med , vol.333 , pp. 32-41
    • Fuchs, C.S.1    Mayer, R.J.2
  • 27
    • 0034388020 scopus 로고    scopus 로고
    • The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release
    • Galmiche, A., Rassow, J., Doye, A., Cagnol, S., Chambard, J.C., Contamin, S., et al. (2000) The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release. EMBO J 19: 6361–6370.
    • (2000) EMBO J , vol.19 , pp. 6361-6370
    • Galmiche, A.1    Rassow, J.2    Doye, A.3    Cagnol, S.4    Chambard, J.C.5    Contamin, S.6
  • 30
    • 34247528572 scopus 로고    scopus 로고
    • Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin
    • Gauthier, N.C., Monzo, P., Gonzalez, T., Doye, A., Oldani, A., Gounon, P., et al. (2007) Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin. J Cell Biol 177: 343–354.
    • (2007) J Cell Biol , vol.177 , pp. 343-354
    • Gauthier, N.C.1    Monzo, P.2    Gonzalez, T.3    Doye, A.4    Oldani, A.5    Gounon, P.6
  • 31
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation
    • Gebert, B., Fischer, W., Weiss, E., Hoffmann, R., and Haas, R. (2003) Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation. Science (New York, N.Y) 301: 1099–1102.
    • (2003) Science (New York, N.Y) , vol.301 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Weiss, E.3    Hoffmann, R.4    Haas, R.5
  • 32
    • 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
  • 33
    • 33644769071 scopus 로고    scopus 로고
    • A Helicobacter pylori vacuolating toxin mutant that fails to oligomerize has a dominant negative phenotype
    • Genisset, C., Galeotti, C.L., Lupetti, P., Mercati, D., Skibinski, D.A., Barone, S., et al. (2006) A Helicobacter pylori vacuolating toxin mutant that fails to oligomerize has a dominant negative phenotype. Infect Immun 74: 1786–1794.
    • (2006) Infect Immun , vol.74 , pp. 1786-1794
    • Genisset, C.1    Galeotti, C.L.2    Lupetti, P.3    Mercati, D.4    Skibinski, D.A.5    Barone, S.6
  • 34
    • 84864820769 scopus 로고    scopus 로고
    • The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a Jurkat T cell assay
    • Gonzalez-Rivera, C., Algood, H.M., Radin, J.N., McClain, M.S., and Cover, T.L. (2012) The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a Jurkat T cell assay. Infect Immun 80: 2578–2588.
    • (2012) Infect Immun , vol.80 , pp. 2578-2588
    • Gonzalez-Rivera, C.1    Algood, H.M.2    Radin, J.N.3    McClain, M.S.4    Cover, T.L.5
  • 36
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh, T., Erdmann, K.S., Roux, A., Habermann, B., Werner, H., and De Camilli, P. (2005) Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 9: 791–804.
    • (2005) Dev Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 37
    • 46449135449 scopus 로고    scopus 로고
    • Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes
    • Ivie, S.E., McClain, M.S., Torres, V.J., Algood, H.M., Lacy, D.B., Yang, R., Blanke, S.R., and Cover, T.L. (2008) Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes. Infect Immun 76: 2843–2851.
    • (2008) Infect Immun , vol.76 , pp. 2843-2851
    • Ivie, S.E.1    McClain, M.S.2    Torres, V.J.3    Algood, H.M.4    Lacy, D.B.5    Yang, R.6    Blanke, S.R.7    Cover, T.L.8
  • 38
    • 0033007098 scopus 로고    scopus 로고
    • VacA from Helicobacter pylori: A hexameric chloride channel
    • Iwamoto, H., Czajkowsky, D.M., Cover, T.L., Szabo, G., and Shao, Z. (1999) VacA from Helicobacter pylori: A hexameric chloride channel. FEBS Lett 450: 101–104.
    • (1999) FEBS Lett , vol.450 , pp. 101-104
    • Iwamoto, H.1    Czajkowsky, D.M.2    Cover, T.L.3    Szabo, G.4    Shao, Z.5
  • 39
    • 80053139817 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin a (VacA) engages the mitochondrial fission machinery to induce host cell death
    • Jain, P., Luo, Z.Q., and Blanke, S.R. (2011) Helicobacter pylori vacuolating cytotoxin a (VacA) engages the mitochondrial fission machinery to induce host cell death. Proc Natl Acad Sci U S A 108: 16032–16037.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16032-16037
    • Jain, P.1    Luo, Z.Q.2    Blanke, S.R.3
  • 40
  • 41
    • 84858226117 scopus 로고    scopus 로고
    • Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro
    • Jimenez-Soto, L.F., Rohrer, S., Jain, U., Ertl, C., Sewald, X., and Haas, R. (2012) Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro. Helicobacter 17: 133–139.
    • (2012) Helicobacter , vol.17 , pp. 133-139
    • Jimenez-Soto, L.F.1    Rohrer, S.2    Jain, U.3    Ertl, C.4    Sewald, X.5    Haas, R.6
  • 42
    • 1942501695 scopus 로고    scopus 로고
    • Membrane channel structure of Helicobacter pylori vacuolating toxin: Role of multiple GXXXG motifs in cylindrical channels
    • Kim, S., Chamberlain, A.K., and Bowie, J.U. (2004) Membrane channel structure of Helicobacter pylori vacuolating toxin: Role of multiple GXXXG motifs in cylindrical channels. Proc Natl Acad Sci U S A 101: 5988–5991.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5988-5991
    • Kim, S.1    Chamberlain, A.K.2    Bowie, J.U.3
  • 43
    • 0031928120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin
    • Lanzavecchia, S., Bellon, P.L., Lupetti, P., Dallai, R., Rappuoli, R., and Telford, J.L. (1998) Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin. J Struct Biol 121: 9–18.
    • (1998) J Struct Biol , vol.121 , pp. 9-18
    • Lanzavecchia, S.1    Bellon, P.L.2    Lupetti, P.3    Dallai, R.4    Rappuoli, R.5    Telford, J.L.6
  • 45
    • 0034043635 scopus 로고    scopus 로고
    • Natural diversity in the N terminus of the mature vacuolating cytotoxin of Helicobacter pylori determines cytotoxin activity
    • Letley, D.P., and Atherton, J.C. (2000) Natural diversity in the N terminus of the mature vacuolating cytotoxin of Helicobacter pylori determines cytotoxin activity. J Bacteriol 182: 3278–3280.
    • (2000) J Bacteriol , vol.182 , pp. 3278-3280
    • Letley, D.P.1    Atherton, J.C.2
  • 46
    • 0038712424 scopus 로고    scopus 로고
    • Determinants of non-toxicity in the gastric pathogen Helicobacter pylori
    • Letley, D.P., Rhead, J.L., Twells, R.J., Dove, B., and Atherton, J.C. (2003) Determinants of non-toxicity in the gastric pathogen Helicobacter pylori. J Biol Chem 278: 26734–26741.
    • (2003) J Biol Chem , vol.278 , pp. 26734-26741
    • Letley, D.P.1    Rhead, J.L.2    Twells, R.J.3    Dove, B.4    Atherton, J.C.5
  • 47
    • 79952114848 scopus 로고    scopus 로고
    • 3-D structures of macromolecules using single-particle analysis in EMAN
    • Ludtke, S.J. (2010) 3-D structures of macromolecules using single-particle analysis in EMAN. Methods Mol Biol (Clifton, N.J.) 673: 157–173.
    • (2010) Methods Mol Biol (Clifton, N.J.) , vol.673 , pp. 157-173
    • Ludtke, S.J.1
  • 48
    • 0029898566 scopus 로고    scopus 로고
    • Oligomeric and subunit structure of the Helicobacter pylori vacuolating cytotoxin
    • Lupetti, P., Heuser, J.E., Manetti, R., Massari, P., Lanzavecchia, S., Bellon, P.L., et al. (1996) Oligomeric and subunit structure of the Helicobacter pylori vacuolating cytotoxin. J Cell Biol 133: 801–807.
    • (1996) J Cell Biol , vol.133 , pp. 801-807
    • Lupetti, P.1    Heuser, J.E.2    Manetti, R.3    Massari, P.4    Lanzavecchia, S.5    Bellon, P.L.6
  • 49
    • 0021259505 scopus 로고
    • Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration
    • Marshall, B.J., and Warren, J.R. (1984) Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet 1: 1311–1315.
    • (1984) Lancet , vol.1 , pp. 1311-1315
    • Marshall, B.J.1    Warren, J.R.2
  • 50
    • 0035145404 scopus 로고    scopus 로고
    • Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization
    • McClain, M.S., Cao, P., and Cover, T.L. (2001a) Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization. Infect Immun 69: 1181–1184.
    • (2001) Infect Immun , vol.69 , pp. 1181-1184
    • McClain, M.S.1    Cao, P.2    Cover, T.L.3
  • 51
    • 0034750730 scopus 로고    scopus 로고
    • A 12-amino-acid segment, present in type s2 but not type s1 Helicobacter pylori VacA proteins, abolishes cytotoxin activity and alters membrane channel formation
    • McClain, M.S., Cao, P., Iwamoto, H., Vinion-Dubiel, A.D., Szabo, G., Shao, Z., and Cover, T.L. (2001b) A 12-amino-acid segment, present in type s2 but not type s1 Helicobacter pylori VacA proteins, abolishes cytotoxin activity and alters membrane channel formation. J Bacteriol 183: 6499–6508.
    • (2001) J Bacteriol , vol.183 , pp. 6499-6508
    • McClain, M.S.1    Cao, P.2    Iwamoto, H.3    Vinion-Dubiel, A.D.4    Szabo, G.5    Shao, Z.6    Cover, T.L.7
  • 52
    • 0037561932 scopus 로고    scopus 로고
    • Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin
    • McClain, M.S., Iwamoto, H., Cao, P., Vinion-Dubiel, A.D., Li, Y., Szabo, G., Shao, Z., and Cover, T.L. (2003) Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin. J Biol Chem 278: 12101–12108.
    • (2003) J Biol Chem , vol.278 , pp. 12101-12108
    • McClain, M.S.1    Iwamoto, H.2    Cao, P.3    Vinion-Dubiel, A.D.4    Li, Y.5    Szabo, G.6    Shao, Z.7    Cover, T.L.8
  • 53
    • 0033929821 scopus 로고    scopus 로고
    • Acid activation of Helicobacter pylori vacuolating cytotoxin (VacA) results in toxin internalization by eukaryotic cells
    • McClain, M.S., Schraw, W., Ricci, V., Boquet, P., and Cover, T.L. (2000) Acid activation of Helicobacter pylori vacuolating cytotoxin (VacA) results in toxin internalization by eukaryotic cells. Mol Microbiol 37: 433–442.
    • (2000) Mol Microbiol , vol.37 , pp. 433-442
    • McClain, M.S.1    Schraw, W.2    Ricci, V.3    Boquet, P.4    Cover, T.L.5
  • 54
    • 84955241226 scopus 로고    scopus 로고
    • Oligomerization but not membrane bending underlies the function of certain F-BAR proteins in cell motility and cytokinesis
    • McDonald, N.A., Vander Kooi, C.W., Ohi, M.D., and Gould, K.L. (2015) Oligomerization but not membrane bending underlies the function of certain F-BAR proteins in cell motility and cytokinesis. Dev Cell 35: 725–736.
    • (2015) Dev Cell , vol.35 , pp. 725-736
    • McDonald, N.A.1    Vander Kooi, C.W.2    Ohi, M.D.3    Gould, K.L.4
  • 55
    • 84905245869 scopus 로고    scopus 로고
    • Vacuolating cytotoxin genotypes are strong markers of gastric cancer and duodenal ulcer-associated Helicobacter pylori strains: A matched case-control study
    • Memon, A.A., Hussein, N.R., Miendje Deyi, V.Y., Burette, A., and Atherton, J.C. (2014) Vacuolating cytotoxin genotypes are strong markers of gastric cancer and duodenal ulcer-associated Helicobacter pylori strains: A matched case-control study. J Clin Microbiol 52: 2984–2989.
    • (2014) J Clin Microbiol , vol.52 , pp. 2984-2989
    • Memon, A.A.1    Hussein, N.R.2    Miendje Deyi, V.Y.3    Burette, A.4    Atherton, J.C.5
  • 57
    • 10744222029 scopus 로고    scopus 로고
    • Helicobacter pylori VacA activates the p38/activating transcription factor 2-mediated signal pathway in AZ-521 cells
    • Nakayama, M., Kimura, M., Wada, A., Yahiro, K., Ogushi, K., Niidome, T., et al. (2004) Helicobacter pylori VacA activates the p38/activating transcription factor 2-mediated signal pathway in AZ-521 cells. J Biol Chem 279: 7024–7028.
    • (2004) J Biol Chem , vol.279 , pp. 7024-7028
    • Nakayama, M.1    Kimura, M.2    Wada, A.3    Yahiro, K.4    Ogushi, K.5    Niidome, T.6
  • 58
    • 0026050956 scopus 로고
    • Helicobacter pylori infection and gastric carcinoma among Japanese Americans in Hawaii
    • Nomura, A., Stemmermann, G.N., Chyou, P.H., Kato, I., Perez-Perez, G.I., and Blaser, M.J. (1991) Helicobacter pylori infection and gastric carcinoma among Japanese Americans in Hawaii. N Engl J Med 325: 1132–1136.
    • (1991) N Engl J Med , vol.325 , pp. 1132-1136
    • Nomura, A.1    Stemmermann, G.N.2    Chyou, P.H.3    Kato, I.4    Perez-Perez, G.I.5    Blaser, M.J.6
  • 59
    • 0026721947 scopus 로고
    • pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349—-Lys
    • O'Keefe, D.O., Cabiaux, V., Choe, S., Eisenberg, D., and Collier, R.J. (1992) pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349—-Lys. Proc Natl Acad Sci U S A 89: 6202–6206.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6202-6206
    • O'Keefe, D.O.1    Cabiaux, V.2    Choe, S.3    Eisenberg, D.4    Collier, R.J.5
  • 60
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - powerful tools in modern electron microscopy
    • Ohi, M., Li, Y., Cheng, Y., and Walz, T. (2004) Negative staining and image classification - powerful tools in modern electron microscopy. Biol Proced Online 6: 23–34.
    • (2004) Biol Proced Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 61
    • 13144253096 scopus 로고    scopus 로고
    • The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating activity
    • Pagliaccia, C., de Bernard, M., Lupetti, P., Ji, X., Burroni, D., Cover, T.L., et al. (1998) The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating activity. Proc Natl Acad Sci U S A 95: 10212–10217.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 10212-10217
    • Pagliaccia, C.1    de Bernard, M.2    Lupetti, P.3    Ji, X.4    Burroni, D.5    Cover, T.L.6
  • 63
    • 0031603419 scopus 로고    scopus 로고
    • Action site and cellular effects of cytotoxin VacA produced by Helicobacter pylori
    • Papini, E., Satin, B., de Bernard, M., Molinari, M., Arico, B., Galli, C., et al. (1998a) Action site and cellular effects of cytotoxin VacA produced by Helicobacter pylori. Folia Microbiol 43: 279–284.
    • (1998) Folia Microbiol , vol.43 , pp. 279-284
    • Papini, E.1    Satin, B.2    de Bernard, M.3    Molinari, M.4    Arico, B.5    Galli, C.6
  • 64
    • 0032528956 scopus 로고    scopus 로고
    • Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin
    • Papini, E., Satin, B., Norais, N., de Bernard, M., Telford, J.L., Rappuoli, R., and Montecucco, C. (1998b) Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin. J Clin Invest 102: 813–820.
    • (1998) J Clin Invest , vol.102 , pp. 813-820
    • Papini, E.1    Satin, B.2    Norais, N.3    de Bernard, M.4    Telford, J.L.5    Rappuoli, R.6    Montecucco, C.7
  • 66
    • 77955782233 scopus 로고    scopus 로고
    • Structural organization of the functional domains of Clostridium difficile toxins a and B
    • Pruitt, R.N., Chambers, M.G., Ng, K.K., Ohi, M.D., and Lacy, D.B. (2010) Structural organization of the functional domains of Clostridium difficile toxins a and B. Proc Natl Acad Sci U S A 107: 13467–13472.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13467-13472
    • Pruitt, R.N.1    Chambers, M.G.2    Ng, K.K.3    Ohi, M.D.4    Lacy, D.B.5
  • 67
    • 79959476135 scopus 로고    scopus 로고
    • Helicobacter pylori VacA induces programmed necrosis in gastric epithelial cells
    • Radin, J.N., Gonzalez-Rivera, C., Ivie, S.E., McClain, M.S., and Cover, T.L. (2011) Helicobacter pylori VacA induces programmed necrosis in gastric epithelial cells. Infect Immun 79: 2535–2543.
    • (2011) Infect Immun , vol.79 , pp. 2535-2543
    • Radin, J.N.1    Gonzalez-Rivera, C.2    Ivie, S.E.3    McClain, M.S.4    Cover, T.L.5
  • 69
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ, W.P., and Engelman, D.M. (1999) TOXCAT: A measure of transmembrane helix association in a biological membrane. Proc Natl Acad Sci U S A 96: 863–868.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 70
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W.P., and Engelman, D.M. (2000) The GxxxG motif: A framework for transmembrane helix-helix association. J Mol Biol 296: 911–919.
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 71
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., Rasband, W.S., and Eliceiri, K.W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9: 671–675.
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 72
    • 39849084618 scopus 로고    scopus 로고
    • Sticky socks: Helicobacter pylori VacA takes shape
    • Sewald, X., Fischer, W., and Haas, R. (2008) Sticky socks: Helicobacter pylori VacA takes shape. Trend Microbiol 16: 89–92.
    • (2008) Trend Microbiol , vol.16 , pp. 89-92
    • Sewald, X.1    Fischer, W.2    Haas, R.3
  • 73
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T.R., Gao, H., Baxter, W.T., Asturias, F.J., Boisset, N., Leith, A., and Frank, J. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3: 1941–1974.
    • (2008) Nat Protoc , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 74
    • 0037057683 scopus 로고    scopus 로고
    • Helicobacter pylori infection
    • Suerbaum, S., and Michetti, P. (2002) Helicobacter pylori infection. N Engl J Med 347: 1175–1186.
    • (2002) N Engl J Med , vol.347 , pp. 1175-1186
    • Suerbaum, S.1    Michetti, P.2
  • 75
    • 2442682964 scopus 로고    scopus 로고
    • Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion
    • Sundrud, M.S., Torres, V.J., Unutmaz, D., and Cover, T.L. (2004) Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion. Proc Natl Acad Sci U S A 101: 7727–7732.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7727-7732
    • Sundrud, M.S.1    Torres, V.J.2    Unutmaz, D.3    Cover, T.L.4
  • 76
    • 13044317274 scopus 로고    scopus 로고
    • Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity
    • Szabo, I., Brutsche, S., Tombola, F., Moschioni, M., Satin, B., Telford, J.L., et al. (1999) Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity. EMBO J 18: 5517–5527.
    • (1999) EMBO J , vol.18 , pp. 5517-5527
    • Szabo, I.1    Brutsche, S.2    Tombola, F.3    Moschioni, M.4    Satin, B.5    Telford, J.L.6
  • 77
    • 84939600856 scopus 로고    scopus 로고
    • Role of GxxxG Motifs in transmembrane domain interactions
    • Teese, M.G., and Langosch, D. (2015) Role of GxxxG Motifs in transmembrane domain interactions. Biochemistry 54: 5125–5135.
    • (2015) Biochemistry , vol.54 , pp. 5125-5135
    • Teese, M.G.1    Langosch, D.2
  • 78
    • 65249135604 scopus 로고    scopus 로고
    • Effect of Helicobacter pylori's vacuolating cytotoxin on the autophagy pathway in gastric epithelial cells
    • Terebiznik, M.R., Raju, D., Vazquez, C.L., Torbricki, K., Kulkarni, R., Blanke, S.R., et al. (2009) Effect of Helicobacter pylori's vacuolating cytotoxin on the autophagy pathway in gastric epithelial cells. Autophagy 5: 370–379.
    • (2009) Autophagy , vol.5 , pp. 370-379
    • Terebiznik, M.R.1    Raju, D.2    Vazquez, C.L.3    Torbricki, K.4    Kulkarni, R.5    Blanke, S.R.6
  • 79
    • 0032981962 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: Possible implications for the mechanism of cellular vacuolation
    • Tombola, F., Carlesso, C., Szabo, I., de Bernard, M., Reyrat, J.M., Telford, J.L., et al. (1999a) Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: Possible implications for the mechanism of cellular vacuolation. Biophys J 76: 1401–1409.
    • (1999) Biophys J , vol.76 , pp. 1401-1409
    • Tombola, F.1    Carlesso, C.2    Szabo, I.3    de Bernard, M.4    Reyrat, J.M.5    Telford, J.L.6
  • 80
    • 0032749462 scopus 로고    scopus 로고
    • Inhibition of the vacuolating and anion channel activities of the VacA toxin of Helicobacter pylori
    • Tombola, F., Oregna, F., Brutsche, S., Szabo, I., Del Giudice, G., Rappuoli, R., et al. (1999b) Inhibition of the vacuolating and anion channel activities of the VacA toxin of Helicobacter pylori. FEBS Lett 460: 221–225.
    • (1999) FEBS Lett , vol.460 , pp. 221-225
    • Tombola, F.1    Oregna, F.2    Brutsche, S.3    Szabo, I.4    Del Giudice, G.5    Rappuoli, R.6
  • 81
    • 20444426199 scopus 로고    scopus 로고
    • Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin
    • Torres, V.J., Ivie, S.E., McClain, M.S., and Cover, T.L. (2005) Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin. J Biol Chem 280: 21107–21114.
    • (2005) J Biol Chem , vol.280 , pp. 21107-21114
    • Torres, V.J.1    Ivie, S.E.2    McClain, M.S.3    Cover, T.L.4
  • 82
    • 0033621333 scopus 로고    scopus 로고
    • A dominant negative mutant of Helicobacter pylori vacuolating toxin (VacA) inhibits VacA-induced cell vacuolation
    • Vinion-Dubiel, A.D., McClain, M.S., Czajkowsky, D.M., Iwamoto, H., Ye, D., Cao, P., et al. (1999) A dominant negative mutant of Helicobacter pylori vacuolating toxin (VacA) inhibits VacA-induced cell vacuolation. J Biol Chem 274: 37736–37742.
    • (1999) J Biol Chem , vol.274 , pp. 37736-37742
    • Vinion-Dubiel, A.D.1    McClain, M.S.2    Czajkowsky, D.M.3    Iwamoto, H.4    Ye, D.5    Cao, P.6
  • 83
    • 0035797916 scopus 로고    scopus 로고
    • Two distinctive cell binding patterns by vacuolating toxin fused with glutathione S-transferase: One high-affinity m1-specific binding and the other lower-affinity binding for variant m forms
    • Wang, W.C., Wang, H.J., and Kuo, C.H. (2001) Two distinctive cell binding patterns by vacuolating toxin fused with glutathione S-transferase: One high-affinity m1-specific binding and the other lower-affinity binding for variant m forms. Biochemistry 40: 11887–11896.
    • (2001) Biochemistry , vol.40 , pp. 11887-11896
    • Wang, W.C.1    Wang, H.J.2    Kuo, C.H.3
  • 85
    • 1642431978 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity
    • Willhite, D.C., and Blanke, S.R. (2004) Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity. Cell Microbiol 6: 143–154.
    • (2004) Cell Microbiol , vol.6 , pp. 143-154
    • Willhite, D.C.1    Blanke, S.R.2
  • 86
    • 0346850825 scopus 로고    scopus 로고
    • Cellular vacuolation and mitochondrial cytochrome c release are independent outcomes of Helicobacter pylori vacuolating cytotoxin activity that are each dependent on membrane channel formation
    • Willhite, D.C., Cover, T.L., and Blanke, S.R. (2003) Cellular vacuolation and mitochondrial cytochrome c release are independent outcomes of Helicobacter pylori vacuolating cytotoxin activity that are each dependent on membrane channel formation. J Biol Chem 278: 48204–48209.
    • (2003) J Biol Chem , vol.278 , pp. 48204-48209
    • Willhite, D.C.1    Cover, T.L.2    Blanke, S.R.3
  • 87
    • 0033579575 scopus 로고    scopus 로고
    • Activation of Helicobacter pylori VacA toxin by alkaline or acid conditions increases its binding to a 250-kDa receptor protein-tyrosine phosphatase beta
    • Yahiro, K., Niidome, T., Kimura, M., Hatakeyama, T., Aoyagi, H., Kurazono, H., et al. (1999) Activation of Helicobacter pylori VacA toxin by alkaline or acid conditions increases its binding to a 250-kDa receptor protein-tyrosine phosphatase beta. J Biol Chem 274: 36693–36699.
    • (1999) J Biol Chem , vol.274 , pp. 36693-36699
    • Yahiro, K.1    Niidome, T.2    Kimura, M.3    Hatakeyama, T.4    Aoyagi, H.5    Kurazono, H.6
  • 88
    • 0033515453 scopus 로고    scopus 로고
    • Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin
    • Ye, D., Willhite, D.C., and Blanke, S.R. (1999) Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin. J Biol Chem 274: 9277–9282.
    • (1999) J Biol Chem , vol.274 , pp. 9277-9282
    • Ye, D.1    Willhite, D.C.2    Blanke, S.R.3


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