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Volumn 6, Issue 7, 2014, Pages 2097-2114

Tailored Cyclodextrin Pore Blocker Protects Mammalian Cells from Clostridium difficile Binary Toxin CDT

Author keywords

Binary toxin; Cellular uptake; Clostridium difficile CDT; Membrane transport; Pore blocker; Translocation pore; cyclodextrin

Indexed keywords

BETA CYCLODEXTRIN DERIVATIVE; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; F ACTIN; PER 6 S (3 AMINOMETHYL)BENZYLTHIO BETA CYCLODEXTRIN; UNCLASSIFIED DRUG; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTECTIVE AGENT;

EID: 84904507553     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins6072097     Document Type: Article
Times cited : (15)

References (82)
  • 1
    • 77956871102 scopus 로고    scopus 로고
    • Clostridium difficile infection
    • Heinlen, L.; Ballard, J.D. Clostridium difficile infection. Am. J. Med. Sci. 2010, 340, 247-252.
    • (2010) Am. J. Med. Sci. , vol.340 , pp. 247-252
    • Heinlen, L.1    Ballard, J.D.2
  • 4
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: The ABCD model
    • Jank, T.; Aktories, K. Structure and mode of action of clostridial glucosylating toxins: The ABCD model. Trends Microbiol. 2008, 16, 222-229.
    • (2008) Trends Microbiol. , vol.16 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 5
    • 0023747353 scopus 로고
    • Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain
    • Popoff, M.R.; Rubin, E.J.; Gill, D.M.; Boquet, P. Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain. Infect. Immun. 1988, 56, 2299-2306.
    • (1988) Infect. Immun. , vol.56 , pp. 2299-2306
    • Popoff, M.R.1    Rubin, E.J.2    Gill, D.M.3    Boquet, P.4
  • 6
    • 0031004306 scopus 로고    scopus 로고
    • Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196
    • Perelle, S.; Gibert, M.; Bourlioux, P.; Corthier, G.; Popoff, M.R. Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196. Infect. Immun. 1997, 65, 1402-1407.
    • (1997) Infect. Immun. , vol.65 , pp. 1402-1407
    • Perelle, S.1    Gibert, M.2    Bourlioux, P.3    Corthier, G.4    Popoff, M.R.5
  • 7
    • 84891773348 scopus 로고    scopus 로고
    • Clostridium difficile binary toxin CDT: Mechanism, epidemiology, and potential clinical importance
    • Gerding, D.N.; Johnson, S.; Rupnik, M.; Aktories, K. Clostridium difficile binary toxin CDT: Mechanism, epidemiology, and potential clinical importance. Gut Microbes 2014, 5, 1-13.
    • (2014) Gut Microbes , vol.5 , pp. 1-13
    • Gerding, D.N.1    Johnson, S.2    Rupnik, M.3    Aktories, K.4
  • 8
    • 0034607782 scopus 로고    scopus 로고
    • Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile
    • Stubbs, S.; Rupnik, M.; Gibert, M.; Brazier, J.; Duerden, B.; Popoff, M.R. Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile. FEMS Microbiol. Lett. 2000, 186, 307-312.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 307-312
    • Stubbs, S.1    Rupnik, M.2    Gibert, M.3    Brazier, J.4    Duerden, B.5    Popoff, M.R.6
  • 9
    • 4544379887 scopus 로고    scopus 로고
    • Distribution of Clostridium difficile variant toxinotypes and strains with binary toxin genes among clinical isolates in an American hospital
    • Geric, B.; Rupnik, M.; Gerding, D.N.; Grabnar, M.; Johnson, S. Distribution of Clostridium difficile variant toxinotypes and strains with binary toxin genes among clinical isolates in an American hospital. J. Med. Microbiol. 2004, 53, 887-894.
    • (2004) J. Med. Microbiol. , vol.53 , pp. 887-894
    • Geric, B.1    Rupnik, M.2    Gerding, D.N.3    Grabnar, M.4    Johnson, S.5
  • 10
    • 2442420091 scopus 로고    scopus 로고
    • Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile
    • Goncalves, C.; Decre, D.; Barbut, F.; Burghoffer, B.; Petit, J.C. Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile. J. Clin. Microbiol. 2004, 42, 1933-1939.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1933-1939
    • Goncalves, C.1    Decre, D.2    Barbut, F.3    Burghoffer, B.4    Petit, J.C.5
  • 12
  • 13
    • 84891353755 scopus 로고    scopus 로고
    • Importance of toxin A, toxin B, and CDT in virulence of an epidemic Clostridium difficile strain
    • Kuehne, S.A.; Collery, M.M.; Kelly, M.L.; Cartman, S.T.; Cockayne, A.; Minton, N.P. Importance of toxin A, toxin B, and CDT in virulence of an epidemic Clostridium difficile strain. J. Infect. Dis. 2014, 209, 83-86.
    • (2014) J. Infect. Dis. , vol.209 , pp. 83-86
    • Kuehne, S.A.1    Collery, M.M.2    Kelly, M.L.3    Cartman, S.T.4    Cockayne, A.5    Minton, N.P.6
  • 15
    • 0019158135 scopus 로고
    • Purification and characterization of two components of botulinum C2 toxin
    • Ohishi, I.; Iwasaki, M.; Sakaguchi, G. Purification and characterization of two components of botulinum C2 toxin. Infect. Immun. 1980, 30, 668-673.
    • (1980) Infect. Immun. , vol.30 , pp. 668-673
    • Ohishi, I.1    Iwasaki, M.2    Sakaguchi, G.3
  • 16
    • 0022453775 scopus 로고
    • ADP-ribosylation of nonmuscle actin with component I of C2 toxin
    • Ohishi, I.; Tsuyama, S. ADP-ribosylation of nonmuscle actin with component I of C2 toxin. Biochem. Biophys. Res. Commun. 1986, 136, 802-806.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 802-806
    • Ohishi, I.1    Tsuyama, S.2
  • 17
    • 0029915545 scopus 로고    scopus 로고
    • Clostridial enteric diseases of domestic animals
    • Songer, J.G. Clostridial enteric diseases of domestic animals. Clin. Microbiol. Rev. 1996, 9, 216-234.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 216-234
    • Songer, J.G.1
  • 18
    • 0023024730 scopus 로고
    • Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity
    • Stiles, B.G.; Wilkins, T.D. Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity. Infect. Immun. 1986, 54, 683-688.
    • (1986) Infect. Immun. , vol.54 , pp. 683-688
    • Stiles, B.G.1    Wilkins, T.D.2
  • 19
    • 0022993253 scopus 로고
    • Clostridium perfringens iota toxin: Synergism between two proteins
    • Stiles, B.G.; Wilkins, T.D. Clostridium perfringens iota toxin: Synergism between two proteins. Toxicon 1986, 24, 767-773.
    • (1986) Toxicon , vol.24 , pp. 767-773
    • Stiles, B.G.1    Wilkins, T.D.2
  • 20
    • 84979834040 scopus 로고    scopus 로고
    • Clostridium perfringens iota-toxin: Structure and function
    • Sakurai, J.; Nagahama, M.; Oda, M.; Tsuge, H.; Kobayashi, K. Clostridium perfringens iota-toxin: Structure and function. Toxins 2009, 1, 208-228.
    • (2009) Toxins , vol.1 , pp. 208-228
    • Sakurai, J.1    Nagahama, M.2    Oda, M.3    Tsuge, H.4    Kobayashi, K.5
  • 21
    • 0023942902 scopus 로고
    • Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin
    • Popoff, M.R.; Boquet, P. Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin. Biochem. Biophys. Res. Commun. 1988, 152, 1361-1368.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 1361-1368
    • Popoff, M.R.1    Boquet, P.2
  • 22
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • Barth, H.; Aktories, K.; Popoff, M.R.; Stiles, B.G. Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins Microbiol. Mol. Biol. Rev. 2004, 8, 373-402.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.8 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 23
    • 80051924025 scopus 로고    scopus 로고
    • New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin
    • Barth, H.; Aktories, K. New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin. Eur. J. Cell. Biol. 2011, 90, 944-950.
    • (2011) Eur. J. Cell. Biol. , vol.90 , pp. 944-950
    • Barth, H.1    Aktories, K.2
  • 26
    • 84879571965 scopus 로고    scopus 로고
    • Clostridium difficile binary toxin CDT induces clustering of the lipolysis-stimulated lipoprotein receptor into lipid rafts
    • doi:10.1128/mBio.00244-13
    • Papatheodorou, P.; Hornuss, D.; Nölke, T.; Hemmasi, S.; Castonguay, J.; Picchianti, M.; Aktories, K. Clostridium difficile binary toxin CDT induces clustering of the lipolysis-stimulated lipoprotein receptor into lipid rafts. MBio 2013, 4, e00244-13. doi:10.1128/mBio.00244-13.
    • (2013) MBio , vol.4
    • Papatheodorou, P.1    Hornuss, D.2    Nölke, T.3    Hemmasi, S.4    Castonguay, J.5    Picchianti, M.6    Aktories, K.7
  • 28
    • 80855141250 scopus 로고    scopus 로고
    • Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90
    • Kaiser, E.; Kroll, C.; Ernst, K.; Schwan, C.; Popoff, M.R.; Fischer, G.; Buchner, J.; Aktories, K.; Barth, H. Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infect. Immun. 2011, 79, 3913-3921.
    • (2011) Infect. Immun. , vol.79 , pp. 3913-3921
    • Kaiser, E.1    Kroll, C.2    Ernst, K.3    Schwan, C.4    Popoff, M.R.5    Fischer, G.6    Buchner, J.7    Aktories, K.8    Barth, H.9
  • 29
    • 0034819726 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile
    • Gülke, I.; Pfeifer, G.; Liese, J.; Fritz, M.; Hofmann, F.; Aktories, K.; Barth, H. Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile. Infect. Immun. 2001, 69, 6004-6011.
    • (2001) Infect. Immun. , vol.69 , pp. 6004-6011
    • Gülke, I.1    Pfeifer, G.2    Liese, J.3    Fritz, M.4    Hofmann, F.5    Aktories, K.6    Barth, H.7
  • 30
    • 0024424942 scopus 로고
    • ADP-ribosylation of actin by clostridial toxins
    • Aktories, K.; Wegner, A. ADP-ribosylation of actin by clostridial toxins. J. Cell Biol. 1989, 109, 1385-1387.
    • (1989) J. Cell Biol. , vol.109 , pp. 1385-1387
    • Aktories, K.1    Wegner, A.2
  • 31
    • 0023612455 scopus 로고
    • Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177
    • Vandekerckhove, J.; Schering, B.; Bärmann, M.; Aktories, K. Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177. FEBS Lett. 1987, 225, 48-52.
    • (1987) FEBS Lett. , vol.225 , pp. 48-52
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 32
    • 0023848539 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates cytoplasmic ß/.-actin in arginine 177
    • Vandekerckhove, J.; Schering, B.; Bärmann, M.; Aktories, K. Botulinum C2 toxin ADP-ribosylates cytoplasmic ß/.-actin in arginine 177. J. Biol. Chem. 1988, 263, 696-700.
    • (1988) J. Biol. Chem. , vol.263 , pp. 696-700
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 33
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin
    • Schering, B.; Bärmann, M.; Chhatwal, G.S.; Geipel, U.; Aktories, K. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur. J. Biochem. 1988, 171, 225-229.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 225-229
    • Schering, B.1    Bärmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 34
    • 0024543962 scopus 로고
    • Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments
    • Weigt, C.; Just, I.; Wegner, A.; Aktories, K. Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments. FEBS Lett. 1989, 246, 181-184.
    • (1989) FEBS Lett. , vol.246 , pp. 181-184
    • Weigt, C.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 35
    • 0025778012 scopus 로고
    • Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase
    • Wiegers, W.; Just, I.; Müller, H.; Hellwig, A.; Traub, P.; Aktories, K. Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase. Eur. J. Cell Biol. 1991, 54, 237-245.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 237-245
    • Wiegers, W.1    Just, I.2    Müller, H.3    Hellwig, A.4    Traub, P.5    Aktories, K.6
  • 36
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • Schleberger, C.; Hochmann, H.; Barth, H.; Aktories, K.; Schulz, G.E. Structure and action of the binary C2 toxin from Clostridium botulinum. J. Mol. Biol. 2006, 364, 705-715.
    • (2006) J. Mol. Biol. , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 38
    • 0023708116 scopus 로고
    • ADP-ribosylated actin caps the barbed ends of actin filaments
    • Wegner, A.; Aktories, K. ADP-ribosylated actin caps the barbed ends of actin filaments. J. Biol. Chem. 1988, 263, 13739-13742.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13739-13742
    • Wegner, A.1    Aktories, K.2
  • 39
    • 73449097193 scopus 로고    scopus 로고
    • Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria
    • Schwan, C.; Stecher, B.; Tzivelekidis, T.; van Ham, M.; Rohde, M.; Hardt, W.D.; Wehland, J.; Aktories, K. Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria. PLoS Pathog. 2009, 5, e1000626.
    • (2009) PLoS Pathog. , vol.5
    • Schwan, C.1    Stecher, B.2    Tzivelekidis, T.3    van Ham, M.4    Rohde, M.5    Hardt, W.D.6    Wehland, J.7    Aktories, K.8
  • 42
    • 0035063194 scopus 로고    scopus 로고
    • Cellular uptake of the binary Clostridium perfringens iota-toxin
    • Blöcker, D.; Behlke, J.; Aktories, K.; Barth, H. Cellular uptake of the binary Clostridium perfringens iota-toxin. Infect. Immun. 2001, 69, 2980-2987.
    • (2001) Infect. Immun. , vol.69 , pp. 2980-2987
    • Blöcker, D.1    Behlke, J.2    Aktories, K.3    Barth, H.4
  • 43
    • 0034115695 scopus 로고    scopus 로고
    • Clostridium perfringens iota toxin: Binding studies and characterization of cell surface receptor by fluorescence-activated cytometry
    • Stiles, B.G.; Hale, M.L.; Marvaud, J.C.; Popoff, M.R. Clostridium perfringens iota toxin: Binding studies and characterization of cell surface receptor by fluorescence-activated cytometry. Infect. Immun 2000, 68, 3475-3484.
    • (2000) Infect. Immun , vol.68 , pp. 3475-3484
    • Stiles, B.G.1    Hale, M.L.2    Marvaud, J.C.3    Popoff, M.R.4
  • 44
    • 0036845021 scopus 로고    scopus 로고
    • Clostridium perfringens iota toxin: Characterization of the cell-associated iota b complex
    • Stiles, B.G.; Hale, M.L.; Marvaud, J.C.; Popoff, M.R. Clostridium perfringens iota toxin: Characterization of the cell-associated iota b complex. Biochem. J. 2002, 367, 801-808.
    • (2002) Biochem. J. , vol.367 , pp. 801-808
    • Stiles, B.G.1    Hale, M.L.2    Marvaud, J.C.3    Popoff, M.R.4
  • 45
    • 0345830908 scopus 로고    scopus 로고
    • Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization
    • Marvaud, J.C.; Stiles, B.G.; Chenal, A.; Gillet, D.; Gibert, M.; Smith, L.A.; Popoff, M.R. Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization. J. Biol. Chem. 2002, 277, 43659-43666.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43659-43666
    • Marvaud, J.C.1    Stiles, B.G.2    Chenal, A.3    Gillet, D.4    Gibert, M.5    Smith, L.A.6    Popoff, M.R.7
  • 46
    • 0036130586 scopus 로고    scopus 로고
    • Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells
    • Nagahama, M.; Nagayasu, K.; Kobayashi, K.; Sakurai, J. Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells. Infect. Immun. 2002, 70, 1909-1914.
    • (2002) Infect. Immun. , vol.70 , pp. 1909-1914
    • Nagahama, M.1    Nagayasu, K.2    Kobayashi, K.3    Sakurai, J.4
  • 48
    • 18144441577 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin: Low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells
    • Blöcker, D.; Pohlmann, K.; Haug, G.; Bachmeyer, C.; Benz, R.; Aktories, K.; Barth, H. Clostridium botulinum C2 toxin: Low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells. J. Biol. Chem. 2003, 278, 37360-37367.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37360-37367
    • Blöcker, D.1    Pohlmann, K.2    Haug, G.3    Bachmeyer, C.4    Benz, R.5    Aktories, K.6    Barth, H.7
  • 49
    • 33947393035 scopus 로고    scopus 로고
    • Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient
    • Gibert, M.; Marvaud, J.C.; Pereira, Y.; Hale, M.L.; Stiles, B.G.; Boquet, P.; Lamaze, C.; Popoff, M.R. Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient. FEBS Lett. 2007, 581, 1287-1296.
    • (2007) FEBS Lett. , vol.581 , pp. 1287-1296
    • Gibert, M.1    Marvaud, J.C.2    Pereira, Y.3    Hale, M.L.4    Stiles, B.G.5    Boquet, P.6    Lamaze, C.7    Popoff, M.R.8
  • 50
    • 0028286786 scopus 로고
    • Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. Formation of cation-selective channels and inhibition of channel function by chloroquine
    • Schmid, A.; Benz, R.; Just, I.; Aktories, K. Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. Formation of cation-selective channels and inhibition of channel function by chloroquine. J. Biol. Chem. 1994, 269, 16706-16711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16706-16711
    • Schmid, A.1    Benz, R.2    Just, I.3    Aktories, K.4
  • 51
    • 0035404038 scopus 로고    scopus 로고
    • Interaction of C2 toxin with lipid bilayer membranes and Vero cells: Inhibition of channel function by chloroquine and related compounds in vitro and intoxification in vivo
    • Bachmeyer, C.; Benz, R.; Barth, H.; Aktories, K.; Gilbert, M.; Popoff, M.R. Interaction of C2 toxin with lipid bilayer membranes and Vero cells: Inhibition of channel function by chloroquine and related compounds in vitro and intoxification in vivo. FASEB J. 2001, 15, 1658-1660.
    • (2001) FASEB J. , vol.15 , pp. 1658-1660
    • Bachmeyer, C.1    Benz, R.2    Barth, H.3    Aktories, K.4    Gilbert, M.5    Popoff, M.R.6
  • 52
    • 0037155268 scopus 로고    scopus 로고
    • Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes: Demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia
    • Knapp, O.; Benz, R.; Gibert, M.; Marvaud, J.C.; Popoff, M.R. Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes: Demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia. J. Biol. Chem. 2002, 277, 6143-6152.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6143-6152
    • Knapp, O.1    Benz, R.2    Gibert, M.3    Marvaud, J.C.4    Popoff, M.R.5
  • 53
    • 0037881855 scopus 로고    scopus 로고
    • Channel formation by the binding component of Clostridium botulinum C2 toxin: Glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo
    • Blöcker, D.; Bachmeyer, C.; Benz, R.; Aktories, K.; Barth, H. Channel formation by the binding component of Clostridium botulinum C2 toxin: Glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo. Biochemistry 2003, 42, 5368-5377.
    • (2003) Biochemistry , vol.42 , pp. 5368-5377
    • Blöcker, D.1    Bachmeyer, C.2    Benz, R.3    Aktories, K.4    Barth, H.5
  • 54
    • 49449106556 scopus 로고    scopus 로고
    • Amino acid residues involved in membrane insertion and pore formation of Clostridium botulinum C2 toxin
    • Lang, A.E.; Neumeyer, T.; Sun, J.; Collier, R.J.; Benz, R.; Aktories, K. Amino acid residues involved in membrane insertion and pore formation of Clostridium botulinum C2 toxin. Biochemistry 2008, 47, 8406-8413.
    • (2008) Biochemistry , vol.47 , pp. 8406-8413
    • Lang, A.E.1    Neumeyer, T.2    Sun, J.3    Collier, R.J.4    Benz, R.5    Aktories, K.6
  • 55
    • 0346333312 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin: Membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain
    • Haug, G.; Wilde, C.; Leemhuis, J.; Meyer, D.K.; Aktories, K.; Barth, H. Cellular uptake of Clostridium botulinum C2 toxin: Membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain. Biochemistry 2003, 42, 15284-15291.
    • (2003) Biochemistry , vol.42 , pp. 15284-15291
    • Haug, G.1    Wilde, C.2    Leemhuis, J.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 56
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • Krantz, B.A.; Finkelstein, A.; Collier, R.J. Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J. Mol. Biol. 2006, 355, 968-979.
    • (2006) J. Mol. Biol , vol.355 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 57
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • Haug, G.; Leemhuis, J.; Tiemann, D.; Meyer, D.K.; Aktories, K.; Barth, H. The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol. J. Biol. Chem. 2003, 278, 32266-32274.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 58
    • 64049084122 scopus 로고    scopus 로고
    • Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells
    • Kaiser, E.; Pust, S.; Kroll, C.; Barth, H. Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells. Cell. Microbiol. 2009, 11, 780-795.
    • (2009) Cell. Microbiol. , vol.11 , pp. 780-795
    • Kaiser, E.1    Pust, S.2    Kroll, C.3    Barth, H.4
  • 59
    • 2142662149 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins
    • Haug, G.; Aktories, K.; Barth, H. The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins. Infect. Immun. 2004, 72, 3066-3068.
    • (2004) Infect. Immun. , vol.72 , pp. 3066-3068
    • Haug, G.1    Aktories, K.2    Barth, H.3
  • 60
    • 84870946824 scopus 로고    scopus 로고
    • Obstructing toxin pathways by targeted pore blockage
    • Nestorovich, E.M.; Bezrukov, S.M. Obstructing toxin pathways by targeted pore blockage. Chem. Rev. 2012, 112, 6388-6430.
    • (2012) Chem. Rev. , vol.112 , pp. 6388-6430
    • Nestorovich, E.M.1    Bezrukov, S.M.2
  • 61
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J.A.; Collier, R.J. Anthrax toxin: Receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 2007, 76, 243-265.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 62
    • 70350708307 scopus 로고    scopus 로고
    • Membrane translocation by anthrax toxin
    • Collier, R.J. Membrane translocation by anthrax toxin. Mol. Aspects Med. 2009, 30, 413-422.
    • (2009) Mol. Aspects Med. , vol.30 , pp. 413-422
    • Collier, R.J.1
  • 63
    • 84901589119 scopus 로고    scopus 로고
    • Anthrax lethal and edema toxins in anthrax pathogenesis
    • doi:10.1016/j.tim.2014.02.012
    • Liu, S.; Moayeri, M.; Leppla, S.H. Anthrax lethal and edema toxins in anthrax pathogenesis. Trends Microbiol. 2014, doi:10.1016/j.tim.2014.02.012.
    • (2014) Trends Microbiol
    • Liu, S.1    Moayeri, M.2    Leppla, S.H.3
  • 64
    • 0141527488 scopus 로고    scopus 로고
    • Mechanism of C2-toxin inhibition by fluphenazine and related compounds: Investigation of their binding kinetics to the C2II-channel using the current noise analysis
    • Bachmeyer, C.; Orlik, F.; Barth, H.; Aktories, K.; Benz, R. Mechanism of C2-toxin inhibition by fluphenazine and related compounds: Investigation of their binding kinetics to the C2II-channel using the current noise analysis. J. Mol. Biol. 2003, 333, 527-540.
    • (2003) J. Mol. Biol. , vol.333 , pp. 527-540
    • Bachmeyer, C.1    Orlik, F.2    Barth, H.3    Aktories, K.4    Benz, R.5
  • 66
    • 42949085407 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin. Identification of the binding site for chloroquine and related compounds and influence of the binding site on properties of the C2II channel
    • Neumeyer, T.; Schiffler, B.; Maier, E.; Lang, A.E.; Aktories, K.; Benz, R. Clostridium botulinum C2 toxin. Identification of the binding site for chloroquine and related compounds and influence of the binding site on properties of the C2II channel. J. Biol. Chem. 2008, 283, 3904-3914.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3904-3914
    • Neumeyer, T.1    Schiffler, B.2    Maier, E.3    Lang, A.E.4    Aktories, K.5    Benz, R.6
  • 67
  • 68
    • 84892532262 scopus 로고    scopus 로고
    • Inhibitions of the translocation pore of Clostridium botulinum C2 toxin by tailored azolopyridinium salts protects human cells from intoxication
    • Bronnhuber, A.; Maier, E.; Riedl, Z.; Hajós, G.; Benz, R.; Barth, H. Inhibitions of the translocation pore of Clostridium botulinum C2 toxin by tailored azolopyridinium salts protects human cells from intoxication. Toxicology 2014, 316, 25-33.
    • (2014) Toxicology , vol.316 , pp. 25-33
    • Bronnhuber, A.1    Maier, E.2    Riedl, Z.3    Hajós, G.4    Benz, R.5    Barth, H.6
  • 69
    • 27244439667 scopus 로고    scopus 로고
    • Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design
    • Karginov, V.A.; Nestorovich, E.M.; Moayeri, M.; Leppla, S.H.; Bezrukov, S.M. Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design. Proc. Natl. Acad. Sci. USA 2005, 102, 15075-15080.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15075-15080
    • Karginov, V.A.1    Nestorovich, E.M.2    Moayeri, M.3    Leppla, S.H.4    Bezrukov, S.M.5
  • 74
    • 84866498531 scopus 로고    scopus 로고
    • Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins
    • Bezrukov, S.M.; Liu, X.; Karginov, V.A.; Wein, A.N.; Leppla, S.H.; Popoff, M.R.; Barth, H.; Nestorovich, E.M. Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins. Biophys. J. 2012, 103, 1208-1217.
    • (2012) Biophys. J. , vol.103 , pp. 1208-1217
    • Bezrukov, S.M.1    Liu, X.2    Karginov, V.A.3    Wein, A.N.4    Leppla, S.H.5    Popoff, M.R.6    Barth, H.7    Nestorovich, E.M.8
  • 75
    • 77954345106 scopus 로고    scopus 로고
    • Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor
    • Nestorovich, E.M.; Karginov, V.A.; Berezhkovskii, A.M.; Bezrukov, S.M. Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor. Biophys. J. 2010, 99, 134-143.
    • (2010) Biophys. J. , vol.99 , pp. 134-143
    • Nestorovich, E.M.1    Karginov, V.A.2    Berezhkovskii, A.M.3    Bezrukov, S.M.4
  • 76
    • 80051937100 scopus 로고    scopus 로고
    • Tailored ß-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxication
    • Nestorovich, E.M.; Karginov, V.A.; Popoff, M.R.; Bezrukov, S.M.; Barth, H. Tailored ß-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxication. PLoS One 2011, 6, e23927.
    • (2011) PLoS One , vol.6
    • Nestorovich, E.M.1    Karginov, V.A.2    Popoff, M.R.3    Bezrukov, S.M.4    Barth, H.5
  • 77
    • 84868584621 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of binding reactions as exemplified by anthrax toxin channel blockage with a cationic cyclodextrin derivative
    • Nestorovich, E.M.; Karginov, V.A.; Berezhkovskii, A.M.; Parsegian, V.A.; Bezrukov, S.M. Kinetics and thermodynamics of binding reactions as exemplified by anthrax toxin channel blockage with a cationic cyclodextrin derivative. Proc. Natl. Acad. Sci. USA 2012, 109, 18453-18458.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 18453-18458
    • Nestorovich, E.M.1    Karginov, V.A.2    Berezhkovskii, A.M.3    Parsegian, V.A.4    Bezrukov, S.M.5
  • 80
    • 0031016925 scopus 로고    scopus 로고
    • Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins
    • Perelle, S.; Scalzo, S.; Kochi, S.; Mock, M.; Popoff, M.R. Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins. FEMS Microbiol. Lett. 1997, 146, 117-121.
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 117-121
    • Perelle, S.1    Scalzo, S.2    Kochi, S.3    Mock, M.4    Popoff, M.R.5
  • 81
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig, K.; Olsnes, S. Diphtheria toxin entry into cells is facilitated by low pH. J. Cell Biol. 1980, 87, 828-832.
    • (1980) J. Cell Biol. , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 82
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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