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Volumn 2, Issue 7, 2010, Pages 1825-1847

Identification of Small Molecule Inhibitors of Clostridium Perfringens ε-toxin cytotoxicity using a Cell-Based High-Throughput Screen

Author keywords

Bacterial toxins; Cell membrane permeability; Clostridium perfringens; Drug evaluation; Preclinical; Small molecule libraries; Structure activity relationship

Indexed keywords

4 [3 (AZEPAN 1 YL) 6 OXO 6H ANTHRA[1,9 CD]ISOXAZOL 5 YLAMINO]BUTANOIC ACID; 4 TERT BUTYL N CYCLOOCTYLBENZAMIDE; ANTISERUM; CLOSTRIDIUM EPSILON TOXIN; CLOSTRIDIUM TOXIN; N CYCLOHEXYL 7 METHOXY N METHYLFURO[2,3 B]QUINOLINE 2 CARBOXAMIDE; UNCLASSIFIED DRUG;

EID: 79952078425     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins2071825     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0020073392 scopus 로고
    • Bacterial toxins: A table of lethal amounts
    • Gill, D.M. Bacterial toxins: A table of lethal amounts. Microbiol. Rev. 1982, 46, 86-94.
    • (1982) Microbiol. Rev , vol.46 , pp. 86-94
    • Gill, D.M.1
  • 2
    • 0030753994 scopus 로고    scopus 로고
    • Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides
    • Minami, J.; Katayama, S.; Matsushita, O.; Matsushita, C.; Okabe, A. Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides. Microbiol. Immunol. 1997, 41, 527-535.
    • (1997) Microbiol. Immunol , vol.41 , pp. 527-535
    • Minami, J.1    Katayama, S.2    Matsushita, O.3    Matsushita, C.4    Okabe, A.5
  • 3
    • 34147168598 scopus 로고
    • Clostridium welchii epsilon toxin in the intestinal contents of man
    • Gleeson-White, M.H.; Bullen, J.J. Clostridium welchii epsilon toxin in the intestinal contents of man. Lancet 1955, 268, 384-385.
    • (1955) Lancet , vol.268 , pp. 384-385
    • Gleeson-White, M.H.1    Bullen, J.J.2
  • 4
    • 34147191999 scopus 로고
    • Recovery of clostridium welchii type d from man
    • Kohn, J.; Warrack, G.H. Recovery of clostridium welchii type d from man. Lancet 1955, 268, 385.
    • (1955) Lancet , vol.268 , pp. 385
    • Kohn, J.1    Warrack, G.H.2
  • 7
    • 34147133733 scopus 로고
    • Isolation of Clostridium perfringens type D from a case of gas gangrene
    • Morinaga, G.; Nakamura, T.; Yoshizawa, J.; Nishida, S. Isolation of Clostridium perfringens type D from a case of gas gangrene. J. Bacteriol. 1965, 90, 826.
    • (1965) J. Bacteriol , vol.90 , pp. 826
    • Morinaga, G.1    Nakamura, T.2    Yoshizawa, J.3    Nishida, S.4
  • 9
    • 34548412159 scopus 로고    scopus 로고
    • Distribution of Clostridium perfringens epsilon toxin in the brains of acutely intoxicated mice and its effect upon glial cells
    • Soler-Jover, A.; Dorca, J.; Popoff, M.R.; Gibert, M.; Saura, J.; Tusell, J.M.; Serratosa, J.; Blasi, J.; Martin-Satue, M. Distribution of Clostridium perfringens epsilon toxin in the brains of acutely intoxicated mice and its effect upon glial cells. Toxicon 2007, 50, 530-540.
    • (2007) Toxicon , vol.50 , pp. 530-540
    • Soler-Jover, A.1    Dorca, J.2    Popoff, M.R.3    Gibert, M.4    Saura, J.5    Tusell, J.M.6    Serratosa, J.7    Blasi, J.8    Martin-Satue, M.9
  • 10
    • 0041823310 scopus 로고    scopus 로고
    • Accumulation of Clostridium perfringens epsilon-toxin in the mouse kidney and its possible biological significance
    • Tamai, E.; Ishida, T.; Miyata, S.; Matsushita, O.; Suda, H.; Kobayashi, S.; Sonobe, H.; Okabe, A. Accumulation of Clostridium perfringens epsilon-toxin in the mouse kidney and its possible biological significance. Infect. Immun. 2003, 71, 5371-5375.
    • (2003) Infect. Immun , vol.71 , pp. 5371-5375
    • Tamai, E.1    Ishida, T.2    Miyata, S.3    Matsushita, O.4    Suda, H.5    Kobayashi, S.6    Sonobe, H.7    Okabe, A.8
  • 11
    • 0035957956 scopus 로고    scopus 로고
    • Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane
    • Miyata, S.; Matsushita, O.; Minami, J.; Katayama, S.; Shimamoto, S.; Okabe, A. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J. Biol. Chem. 2001, 276, 13778-13783.
    • (2001) J. Biol. Chem , vol.276 , pp. 13778-13783
    • Miyata, S.1    Matsushita, O.2    Minami, J.3    Katayama, S.4    Shimamoto, S.5    Okabe, A.6
  • 12
    • 0037130957 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of madin-darby canine kidney cells and rat synaptosomes
    • Miyata, S.; Minami, J.; Tamai, E.; Matsushita, O.; Shimamoto, S.; Okabe, A. Clostridium perfringens epsilon-toxin forms a heptameric pore within the detergent-insoluble microdomains of madin-darby canine kidney cells and rat synaptosomes. J. Biol. Chem. 2002, 277, 39463-39468.
    • (2002) J. Biol. Chem , vol.277 , pp. 39463-39468
    • Miyata, S.1    Minami, J.2    Tamai, E.3    Matsushita, O.4    Shimamoto, S.5    Okabe, A.6
  • 13
    • 0030769466 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complex
    • Petit, L.; Gibert, M.; Gillet, D.; Laurent-Winter, C.; Boquet, P.; Popoff, M.R. Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complex. J. Bacteriol. 1997, 179, 6480-6487.
    • (1997) J. Bacteriol , vol.179 , pp. 6480-6487
    • Petit, L.1    Gibert, M.2    Gillet, D.3    Laurent-Winter, C.4    Boquet, P.5    Popoff, M.R.6
  • 14
    • 0035844180 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon toxin induces a rapid change of cell membrane permeability to ions and forms channels in artificial lipid bilayers
    • Petit, L.; Maier, E.; Gibert, M.; Popoff, M.R.; Benz, R. Clostridium perfringens epsilon toxin induces a rapid change of cell membrane permeability to ions and forms channels in artificial lipid bilayers. J. Biol. Chem. 2001, 276, 15736-15740.
    • (2001) J. Biol. Chem , vol.276 , pp. 15736-15740
    • Petit, L.1    Maier, E.2    Gibert, M.3    Popoff, M.R.4    Benz, R.5
  • 15
    • 0037343595 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon toxin rapidly decreases membrane barrier permeability of polarized MDCK cells
    • Petit, L.; Gibert, M.; Gourch, A.; Bens, M.; Vandewalle, A.; Popoff, M.R. Clostridium perfringens epsilon toxin rapidly decreases membrane barrier permeability of polarized MDCK cells. Cell. Microbiol. 2003, 5, 155-164.
    • (2003) Cell. Microbiol , vol.5 , pp. 155-164
    • Petit, L.1    Gibert, M.2    Gourch, A.3    Bens, M.4    Vandewalle, A.5    Popoff, M.R.6
  • 16
    • 34147173804 scopus 로고    scopus 로고
    • Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxin
    • McClain, M.S.; Cover, T.L. Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxin. Infect. Immun. 2007, 75, 1785-1793.
    • (2007) Infect. Immun , vol.75 , pp. 1785-1793
    • McClain, M.S.1    Cover, T.L.2
  • 17
    • 0032189204 scopus 로고    scopus 로고
    • Assembly of Clostridium perfringens epsilon-toxin on MDCK cell membrane
    • Nagahama, M.; Ochi, S.; Sakurai, J. Assembly of Clostridium perfringens epsilon-toxin on MDCK cell membrane. J. Nat. Toxins 1998, 7, 291-302.
    • (1998) J. Nat. Toxins , vol.7 , pp. 291-302
    • Nagahama, M.1    Ochi, S.2    Sakurai, J.3
  • 18
    • 0029803821 scopus 로고    scopus 로고
    • Assessment of aspects of the toxicity of Clostridium perfringens epsilon-toxin using the MDCK cell line
    • Lindsay, C.D. Assessment of aspects of the toxicity of Clostridium perfringens epsilon-toxin using the MDCK cell line. Hum. Exp. Toxicol. 1996, 15, 904-908.
    • (1996) Hum. Exp. Toxicol , vol.15 , pp. 904-908
    • Lindsay, C.D.1
  • 19
    • 0023968899 scopus 로고
    • The passive protection of lambs against Clostridium perfringens type D with semi-purified hyperimmune serum
    • Odendaal, M.W.; Visser, J.J.; Botha, W.J.; Prinsloo, H. The passive protection of lambs against Clostridium perfringens type D with semi-purified hyperimmune serum. Onderstepoort J. Vet. Res. 1988, 55, 47-50.
    • (1988) Onderstepoort J. Vet. Res , vol.55 , pp. 47-50
    • Odendaal, M.W.1    Visser, J.J.2    Botha, W.J.3    Prinsloo, H.4
  • 20
    • 0032564217 scopus 로고    scopus 로고
    • Variability of serum antibody responses of goat kids to a commercial Clostridium perfringens epsilon toxoid vaccine
    • Uzal, F.A.; Bodero, D.A.; Kelly, W.R.; Nielsen, K. Variability of serum antibody responses of goat kids to a commercial Clostridium perfringens epsilon toxoid vaccine. Vet. Rec. 1998, 143, 472-474.
    • (1998) Vet. Rec , vol.143 , pp. 472-474
    • Uzal, F.A.1    Bodero, D.A.2    Kelly, W.R.3    Nielsen, K.4
  • 21
    • 0003975382 scopus 로고    scopus 로고
    • 8th ed.; Merck and Co., Inc.: Whitehouse Station, NJ, USA
    • Aiello, S.E. Merck Veterinary Manual, 8th ed.; Merck and Co., Inc.: Whitehouse Station, NJ, USA, 2003.
    • (2003) Merck Veterinary Manual
    • Aiello, S.E.1
  • 22
    • 70350399473 scopus 로고    scopus 로고
    • Dominant-negative inhibitors of the Clostridium perfringens epsilontoxin
    • Pelish, T.M.; McClain, M.S. Dominant-negative inhibitors of the Clostridium perfringens epsilontoxin. J. Biol. Chem. 2009, 284, 29446-29453.
    • (2009) J. Biol. Chem , vol.284 , pp. 29446-29453
    • Pelish, T.M.1    McClain, M.S.2
  • 23
    • 0032621382 scopus 로고    scopus 로고
    • Development of monoclonal antibodies suitable for use in antigen quantification potency tests for clostridial veterinary vaccines
    • Hauer, P.J.; Clough, N.E. Development of monoclonal antibodies suitable for use in antigen quantification potency tests for clostridial veterinary vaccines. Dev. Biol. Stand. 1999, 101, 85-94.
    • (1999) Dev. Biol. Stand , vol.101 , pp. 85-94
    • Hauer, P.J.1    Clough, N.E.2
  • 24
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang, J.H.; Chung, T.D.; Oldenburg, K.R. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 1999, 4, 67-73.
    • (1999) J. Biomol. Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 25
    • 0028156994 scopus 로고
    • Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin
    • Payne, D.W.; Williamson, E.D.; Havard, H.; Modi, N.; Brown, J. Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin. FEMS Microbiol. Lett. 1994, 116, 161-167.
    • (1994) FEMS Microbiol. Lett , vol.116 , pp. 161-167
    • Payne, D.W.1    Williamson, E.D.2    Havard, H.3    Modi, N.4    Brown, J.5
  • 26
    • 33745621325 scopus 로고    scopus 로고
    • Hts-corrector: Software for the statistical analysis and correction of experimental high-throughput screening data
    • Makarenkov, V.; Kevorkov, D.; Zentilli, P.; Gagarin, A.; Malo, N.; Nadon, R. Hts-corrector: Software for the statistical analysis and correction of experimental high-throughput screening data. Bioinformatics 2006, 22, 1408-1409.
    • (2006) Bioinformatics , vol.22 , pp. 1408-1409
    • Makarenkov, V.1    Kevorkov, D.2    Zentilli, P.3    Gagarin, A.4    Malo, N.5    Nadon, R.6
  • 27
    • 0002182927 scopus 로고
    • A survey of sampling from contaminated distributions
    • Olkin, I., Ed.; Stanford University Press: Stanford, CA, USA
    • Tukey, J.W. A survey of sampling from contaminated distributions. In Contributions to Probability and Statistics; Olkin, I., Ed.; Stanford University Press: Stanford, CA, USA, 1960; pp. 448-485.
    • (1960) Contributions to Probability and Statistics , pp. 448-485
    • Tukey, J.W.1
  • 29
    • 3242669872 scopus 로고    scopus 로고
    • Improved statistical methods for hit selection in high-throughput screening
    • Brideau, C.; Gunter, B.; Pikounis, B.; Liaw, A. Improved statistical methods for hit selection in high-throughput screening. J. Biomol. Screen. 2003, 8, 634-647.
    • (2003) J. Biomol. Screen , vol.8 , pp. 634-647
    • Brideau, C.1    Gunter, B.2    Pikounis, B.3    Liaw, A.4
  • 30
    • 47149104497 scopus 로고    scopus 로고
    • Increased efficiency for performing colony formation assays in 96-well plates: Novel applications to combination therapies and high-throughput screening
    • Katz, D.; Ito, E.; Lau, K.S.; Mocanu, J.D.; Bastianutto, C.; Schimmer, A.D.; Liu, F.F. Increased efficiency for performing colony formation assays in 96-well plates: Novel applications to combination therapies and high-throughput screening. Biotechniques 2008, 44, ix-xiv.
    • (2008) Biotechniques , vol.44
    • Katz, D.1    Ito, E.2    Lau, K.S.3    Mocanu, J.D.4    Bastianutto, C.5    Schimmer, A.D.6    Liu, F.F.7
  • 31
    • 0037040347 scopus 로고    scopus 로고
    • Poor solubility limiting significance of in-vitro studies with HIV protease inhibitors
    • Weiss, J.; Burhenne, J.; Riedel, K.D.; Haefeli, W.E. Poor solubility limiting significance of in-vitro studies with HIV protease inhibitors. AIDS 2002, 16, 674-676.
    • (2002) AIDS , vol.16 , pp. 674-676
    • Weiss, J.1    Burhenne, J.2    Riedel, K.D.3    Haefeli, W.E.4
  • 32
    • 31044448805 scopus 로고    scopus 로고
    • Evaluation of inhibitory potencies for compounds inhibiting P-glycoprotein but without maximum effects: F2 values
    • Weiss, J.; Haefeli, W.E. Evaluation of inhibitory potencies for compounds inhibiting P-glycoprotein but without maximum effects: F2 values. Drug Metab. Dispos. 2006, 34, 203-207.
    • (2006) Drug Metab. Dispos , vol.34 , pp. 203-207
    • Weiss, J.1    Haefeli, W.E.2
  • 34
    • 0036687614 scopus 로고    scopus 로고
    • Passive antibody administration (immediate immunity) as a specific defense against biological weapons
    • Casadevall, A. Passive antibody administration (immediate immunity) as a specific defense against biological weapons. Emerg. Infect. Dis. 2002, 8, 833-841.
    • (2002) Emerg. Infect. Dis , vol.8 , pp. 833-841
    • Casadevall, A.1
  • 35
    • 4344592437 scopus 로고    scopus 로고
    • Discovery of a small molecule that inhibits the interaction of anthrax edema factor with its cellular activator, calmodulin
    • Lee, Y.S.; Bergson, P.; He, W.S.; Mrksich, M.; Tang, W.J. Discovery of a small molecule that inhibits the interaction of anthrax edema factor with its cellular activator, calmodulin. Chem. Biol. 2004, 11, 1139-1146.
    • (2004) Chem. Biol , vol.11 , pp. 1139-1146
    • Lee, Y.S.1    Bergson, P.2    He, W.S.3    Mrksich, M.4    Tang, W.J.5
  • 36
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • Soelaiman, S.; Wei, B.Q.; Bergson, P.; Lee, Y.S.; Shen, Y.; Mrksich, M.; Shoichet, B.K.; Tang, W.J. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem. 2003, 278, 25990-25997.
    • (2003) J. Biol. Chem , vol.278 , pp. 25990-25997
    • Soelaiman, S.1    Wei, B.Q.2    Bergson, P.3    Lee, Y.S.4    Shen, Y.5    Mrksich, M.6    Shoichet, B.K.7    Tang, W.J.8
  • 40
    • 34548490308 scopus 로고    scopus 로고
    • Identification and characterization of small molecules that inhibit intracellular toxin transport
    • Saenz, J.B.; Doggett, T.A.; Haslam, D.B. Identification and characterization of small molecules that inhibit intracellular toxin transport. Infect. Immun. 2007, 75, 4552-4561.
    • (2007) Infect. Immun , vol.75 , pp. 4552-4561
    • Saenz, J.B.1    Doggett, T.A.2    Haslam, D.B.3
  • 41
    • 77954141743 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of ricin and shiga toxin using a cell-based high-throughput screen
    • doi:10.1016/j.toxicon.2010.03.016
    • Wahome, P.G.; Bai, Y.; Neal, L.M.; Robertus, J.D.; Mantis, N.J. Identification of small-molecule inhibitors of ricin and shiga toxin using a cell-based high-throughput screen. Toxicon 2010, doi:10.1016/j.toxicon.2010.03.016.
    • (2010) Toxicon
    • Wahome, P.G.1    Bai, Y.2    Neal, L.M.3    Robertus, J.D.4    Mantis, N.J.5
  • 42
    • 0036896008 scopus 로고    scopus 로고
    • Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxininduced intestinal fluid secretion
    • Ma, T.; Thiagarajah, J.R.; Yang, H.; Sonawane, N.D.; Folli, C.; Galietta, L.J.; Verkman, A.S. Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxininduced intestinal fluid secretion. J. Clin. Invest. 2002, 110, 1651-1658.
    • (2002) J. Clin. Invest , vol.110 , pp. 1651-1658
    • Ma, T.1    Thiagarajah, J.R.2    Yang, H.3    Sonawane, N.D.4    Folli, C.5    Galietta, L.J.6    Verkman, A.S.7
  • 44
    • 3542993232 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin
    • Cole, A.R.; Gibert, M.; Popoff, M.; Moss, D.S.; Titball, R.W.; Basak, A.K. Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat. Struct. Mol. Biol. 2004, 11, 797-798.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 797-798
    • Cole, A.R.1    Gibert, M.2    Popoff, M.3    Moss, D.S.4    Titball, R.W.5    Basak, A.K.6
  • 45
    • 0027976196 scopus 로고
    • Structure of the aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M.W.; Buckley, J.T.; Postma, J.P.; Tucker, A.D.; Leonard, K.; Pattus, F.; Tsernoglou, D. Structure of the aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 1994, 367, 292-295.
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.P.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6    Tsernoglou, D.7
  • 49
    • 33745809902 scopus 로고    scopus 로고
    • Hit discovery and hit-to-lead approaches
    • Keseru, G.M.; Makara, G.M. Hit discovery and hit-to-lead approaches. Drug Discov. Today 2006, 11, 741-748.
    • (2006) Drug Discov. Today , vol.11 , pp. 741-748
    • Keseru, G.M.1    Makara, G.M.2


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