메뉴 건너뛰기




Volumn 88, Issue 4, 2010, Pages 877-884

Functional and structural characterization of soluble recombinant epsilon toxin of Clostridium perfringens D, causative agent of enterotoxaemia

Author keywords

Clostridium perfringens; Enterotoxaemia .MDCK cells; Epsilon toxin

Indexed keywords

ANION EXCHANGE CHROMATOGRAPHY; BIOLOGICAL ACTIVITIES; CAUSATIVE AGENTS; CLOSTRIDIUM PERFRINGENS; CYTOTOXIC; ECONOMIC CONCERNS; ENTEROTOXAEMIA .MDCK CELLS; EPSILON TOXIN; EPSILON TOXINS; HEPTAMERS; MADIN-DARBY CANINE KIDNEY CELLS; MDCK CELLS; MOUSE BRAIN; SOLUBLE PROTEINS; STRUCTURAL CHARACTERIZATION; WESTERN BLOTTING;

EID: 79952110947     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2785-y     Document Type: Article
Times cited : (23)

References (28)
  • 2
    • 0015861610 scopus 로고
    • Pathology of Clostridium welchii type D enterotoxaemia. II. Structural and ultrastructural alterations in the tissues of lambs and mice
    • Gardner DE (1973) Pathology of Clostridium welchii type D enterotoxaemia. II. Structural and ultrastructural alterations in the tissues of lambs and mice. J Comp Pathol 83:509-524
    • (1973) J Comp Pathol , vol.83 , pp. 509-524
    • Gardner, D.E.1
  • 3
    • 0030600374 scopus 로고    scopus 로고
    • Molecular cloning of Clostridium perfringens epsilon-toxin gene and its high level expression in E. coli
    • DOI 10.1006/bbrc.1996.1422
    • Goswami PP, Rupa P, Prihar NS, Garg LC (1996) Molecular cloning of Clostridium perfringens epsilon-toxin gene and its high level expression in E coli. Biochem Biophys Res Commun 226:735-740 (Pubitemid 26348541)
    • (1996) Biochemical and Biophysical Research Communications , vol.226 , Issue.3 , pp. 735-740
    • Goswami, P.P.1    Rupa, P.2    Prihar, N.S.3    Garg, L.C.4
  • 4
    • 0015845099 scopus 로고
    • Conformational studies on modified proteins and peptides. VII. Conformation of epsilonprototoxin and epsilon-toxin from Clostridium perfringens. Conformational changes associated with toxicity
    • Habeeb AF, Lee CL, Atassi MZ (1973) Conformational studies on modified proteins and peptides. VII. Conformation of epsilonprototoxin and epsilon-toxin from Clostridium perfringens. Conformational changes associated with toxicity. Biochim Biophys Acta 322:245-250
    • (1973) Biochim Biophys Acta , vol.322 , pp. 245-250
    • Habeeb, A.F.1    Lee, C.L.2    Atassi, M.Z.3
  • 5
    • 0025947639 scopus 로고
    • Staphylococcus aureus α-toxin: Dual mechanism of binding to target cells
    • Hildebrand A, Pohl M, Bhakdi S (1991) Staphylococcus aureus a- toxin. Dual mechanism of binding to target cells. J Biol Chem 266:17195-17200 (Pubitemid 21907924)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17195-17200
    • Hildebrand, A.1    Pohl, M.2    Bhakdi, S.3
  • 6
    • 0026542943 scopus 로고
    • Cloning and nucleotide sequencing of the Clostridium perfringens epsilontoxin gene and its expression in Escherichia coli
    • Hunter SE, Clarke IN, Kelly DC, Titball RW (1992) Cloning and nucleotide sequencing of the Clostridium perfringens epsilontoxin gene and its expression in Escherichia coli. Infect Immun 60:102-110
    • (1992) Infect Immun , vol.60 , pp. 102-110
    • Hunter, S.E.1    Clarke, I.N.2    Kelly, D.C.3    Titball, R.W.4
  • 7
    • 72049121494 scopus 로고    scopus 로고
    • Identification of the channel-forming domain of Clostridium perfringens Epsilon-toxin (ETX
    • Knapp O, Maier E, Benz R, Geny B, Popoff MR (2009) Identification of the channel-forming domain of Clostridium perfringens Epsilon-toxin (ETX). Biochim Biophys Acta 1788:2584-2593
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2584-2593
    • Knapp, O.1    Maier, E.2    Benz, R.3    Geny, B.4    Popoff, M.R.5
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins using the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins using the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0026713528 scopus 로고
    • Deamidation: A source of microheterogeneity in pharmaceutical proteins
    • Liu DT (1992) Deamidation: A source of microheterogeneity in pharmaceutical proteins. Trends Biotechnol 10:364-369
    • (1992) Trends Biotechnol , vol.10 , pp. 364-369
    • Liu, D.T.1
  • 10
    • 1942486713 scopus 로고    scopus 로고
    • New insights into the cytotoxic mechanisms of Clostridium perfringens enterotoxin
    • DOI 10.1016/j.anaerobe.2003.11.004, PII S1075996403001707
    • McClane BA, Chakrabarti G (2004) New insights into the cytotoxic mechanisms of Clostridium perfringens enterotoxin. Anaerobe 10:107-114 (Pubitemid 38519811)
    • (2004) Anaerobe , vol.10 , Issue.2 , pp. 107-114
    • McClane, B.A.1    Chakrabarti, G.2
  • 11
    • 0026520229 scopus 로고
    • High-affinity binding of Clostridium perfringens epsilon toxin to rat brain
    • Nagahama M, Sakurai J (1992) High-affinity binding of Clostridium perfringens epsilon toxin to rat brain. Infect Immun 60:1237-1240
    • (1992) Infect Immun , vol.60 , pp. 1237-1240
    • Nagahama, M.1    Sakurai, J.2
  • 12
    • 0036157171 scopus 로고    scopus 로고
    • Two-dimensional analysis of exoproteins of methicillin-resistant Staphylococcus aureus (MRSA) for possible epidemiological applications
    • Nakano M, Kawano Y, Kawagish M, Hasegawa T, Linuma Y, Oht M (2002) Two-dimensional analysis of exoproteins of methicillinresistant Staphylococcus aureus for possible epidemiological applications. Microbiol Immunol 46:11-22 (Pubitemid 34101082)
    • (2002) Microbiology and Immunology , vol.46 , Issue.1 , pp. 11-22
    • Nakano, M.1    Kawano, Y.2    Kawagishi, M.3    Hasegawa, T.4    Iinuma, Y.5    Ohta, M.6
  • 13
    • 21644447824 scopus 로고    scopus 로고
    • Interaction of an 40 kDa protein from regenerating rat liver with the -148 to -124 region of c-jun complexed with RLjunRP coincides with enhanced c-jun expression in proliferating rat liver
    • DOI 10.1111/j.1432-1033.2004.04458.x
    • Ohri S, Sharma D, Dixit A (2004) Interaction of an approximately 40 kDa protein from regenerating rat liver with the -148 to -124 region of c-jun complexed with RLjunRP coincides with enhanced c-jun expression in proliferating rat liver. Eur J Biochem 271:4892-4902 (Pubitemid 40065592)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.23-24 , pp. 4892-4902
    • Ohri, S.1    Sharma, D.2    Dixit, A.3
  • 14
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • DOI 10.1016/j.pbiomolbio.2004.01.009, PII S0079610704000033
    • Parker MW, Feil SC (2005) Pore-forming protein toxins: From structure to function. Prog Biophys Mol Biol 88:91-142 (Pubitemid 39547775)
    • (2005) Progress in Biophysics and Molecular Biology , vol.88 , Issue.1 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 15
    • 0028156994 scopus 로고
    • Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin
    • DOI 10.1016/0378-1097(94)90068-X
    • Payne DW, Williamson ED, Harvard H, Modi N, Brown J (1994) Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin. FEMS Microbiol Lett 116:161-168 (Pubitemid 24069292)
    • (1994) FEMS Microbiology Letters , vol.116 , Issue.2 , pp. 161-168
    • Payne, D.W.1    Williamson, E.D.2    Havard, H.3    Modi, N.4    Brown, J.5
  • 16
    • 0033755938 scopus 로고    scopus 로고
    • Determination of the origin of charge heterogeneity in a murine monoclonal antibody
    • Perkins M, Theiler R, Lunte S, Jeschke M (2000) Determination of the origin of charge heterogeneity in a murine monoclonal antibody. Pharm Res 17:1110-1117
    • (2000) Pharm Res , vol.17 , pp. 1110-1117
    • Perkins, M.1    Theiler, R.2    Lunte, S.3    Jeschke, M.4
  • 18
    • 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 MR, Benz R (2001) Clostridium perfringens epsilon toxin induces a rapid change of cell membrane permeability to ions and forms channels in artificial lipid bilayers. J Biol Chem 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
  • 19
    • 0042326608 scopus 로고    scopus 로고
    • Investigation of the pore-forming mechanism of a cytolytic Δ-endotoxin from Bacillus thuringiensis
    • DOI 10.1042/BJ20030437
    • Promodonkoy B, Ellar DJ (2003) Investigation of the pore-forming mechanism of a cytolytic delta-endotoxin from Bacillus thuringiensis. Biochem J 374:255-259 (Pubitemid 37046950)
    • (2003) Biochemical Journal , vol.374 , Issue.1 , pp. 255-259
    • Promdonkoy, B.1    Ellar, D.J.2
  • 20
    • 0023603533 scopus 로고
    • Carboxyl groups in Clostridium perfringens epsilon toxin
    • DOI 10.1016/0882-4010(87)90017-9
    • Sakurai J, Nagahama M (1987) Carboxyl groups in Clostridium perfringens epsilon toxin. Microb Pathog 3:469-474 (Pubitemid 18029280)
    • (1987) Microbial Pathogenesis , vol.3 , Issue.6 , pp. 469-474
    • Sakurai, J.1    Nagahama, M.2
  • 21
    • 0030881601 scopus 로고    scopus 로고
    • Generation of a membrane bound pre-pore complex is necessary for poreformation by C. perfringens alpha-toxin
    • Sellman BR, Tweten RK, Kagan BL (1997) Generation of a membrane bound pre-pore complex is necessary for poreformation by C. perfringens alpha-toxin. Mol Microbiol 25:429-440
    • (1997) Mol Microbiol , vol.25 , pp. 429-440
    • Sellman, B.R.1    Tweten, R.K.2    Kagan, B.L.3
  • 22
    • 34548412159 scopus 로고    scopus 로고
    • Distribution of Clostridium perfringens epsilon toxin in the brains of acutely intoxicated mice and its effect upon glial cells
    • DOI 10.1016/j.toxicon.2007.04.025, PII S0041010107001663
    • Soler-Jover A, Dorca J, Popoff MR, Gibert M, Saura J, Tusell JM, Serratosa J, Blasi J, Martín-Satué M (2007) Distribution of Clostridium perfringens epsilon toxin in the brains of acutely intoxicated mice and its effect upon glial cells. Toxicon 50:530-540 (Pubitemid 47368587)
    • (2007) Toxicon , vol.50 , Issue.4 , 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
  • 23
    • 0343775797 scopus 로고    scopus 로고
    • Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells
    • DOI 10.1006/mpat.1999.0323
    • Steinthorsdottir V, Halldorsson H, Andresson OS (2000) Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells. Microb Pathog 28:45-50 (Pubitemid 30037815)
    • (2000) Microbial Pathogenesis , vol.28 , Issue.1 , pp. 45-50
    • Steinthorsdottir, V.1    Halldorsson, H.2    Andresson, O.S.3
  • 24
    • 0041823310 scopus 로고    scopus 로고
    • Accumulation of Clostridium perfringens epsilon-toxin in the mouse kidney and its possible biological significance
    • DOI 10.1128/IAI.71.9.5371-5375.2003
    • Tamai E, Inida T, Matsushita O, Suda O, Sonobe H, Okabe A (2003) Accumulation of Clostridium perfringens epsilon-toxin in the mouse kidney and its possible biological significance. Infect Immun 71:5371-5375 (Pubitemid 37070786)
    • (2003) Infection and Immunity , vol.71 , Issue.9 , 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
  • 25
    • 0040318126 scopus 로고
    • Crystalline epsilon-prototoxin from Clostridium welchii
    • Thomson RO (1962) Crystalline epsilon-prototoxin from Clostridium welchii. Nature 193:69-70
    • (1962) Nature , vol.193 , pp. 69-70
    • Thomson, R.O.1
  • 26
    • 79952220502 scopus 로고    scopus 로고
    • Clostridium perfringens vaccines
    • Titball RW (2009) Clostridium perfringens vaccines. Vaccine 27 (suppl 4):D44-D47
    • (2009) Vaccine , vol.27 , Issue.SUPPL. 4
    • Titball, R.W.1
  • 27
    • 0017760744 scopus 로고
    • Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation
    • Worthington RW, Mulders MSG (1977) Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation. Infect Immun 18:549-551 (Pubitemid 8231936)
    • (1977) Infection and Immunity , vol.18 , Issue.2 , pp. 549-551
    • Worthington, R.W.1    Mulders, M.S.G.2
  • 28
    • 0035011534 scopus 로고    scopus 로고
    • Clostridium perfringens prototoxin-induced alteration of endothelial barrier antigen (EBA) immunoreactivity at the blood-brain barrier (BBB)
    • DOI 10.1006/exnr.2001.7652
    • Zhu C, Ghabriel MN, Blumbergs DC, Reilly PL, Manavis J, Youssef J, Hatami S, Finnie JW (2001) Clostridium perfringens prototoxin-induced alteration of endothelial barrier antigen (EBA) immunoreactivity at the blood-brain barrier (BBB). Exp Neurol 169:72-82 (Pubitemid 32424324)
    • (2001) Experimental Neurology , vol.169 , Issue.1 , pp. 72-82
    • Zhu, C.1    Ghabriel, M.N.2    Blumbergs, P.C.3    Reilly, P.L.4    Manavis, J.5    Youssef, J.6    Hatami, S.7    Finnie J.W8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.