메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Retargeting Clostridium difficile toxin B to neuronal cells as a potential vehicle for cytosolic delivery of therapeutic biomolecules to treat botulism

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLTRANSFERASE; BOTULINUM TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; GLUCOSYLTRANSFERASE; STREPTAVIDIN; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 81555221763     PISSN: 16878191     EISSN: 16878205     Source Type: Journal    
DOI: 10.1155/2012/760142     Document Type: Article
Times cited : (5)

References (30)
  • 1
    • 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 in Microbiology 2008 16 5 222 229
    • (2008) Trends in Microbiology , vol.16 , Issue.5 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 2
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • DOI 10.1074/jbc.M703062200
    • Egerer M., Giesemann T., Jank T., Fullner Satchell K. J., Aktories K., Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity Journal of Biological Chemistry 2007 282 35 25314 25321 (Pubitemid 47372781)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Fullner Satchell, K.J.4    Aktories, K.5
  • 4
    • 63649106579 scopus 로고    scopus 로고
    • Autocatalytic processing of Clostridium difficile toxin B: Binding of inositol hexakisphosphate
    • Egerer M., Giesemann T., Herrmann C., Aktorles K., Autocatalytic processing of Clostridium difficile toxin B: binding of inositol hexakisphosphate Journal of Biological Chemistry 2009 284 6 3389 3395
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.6 , pp. 3389-3395
    • Egerer, M.1    Giesemann, T.2    Herrmann, C.3    Aktorles, K.4
  • 5
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • Voth D. E., Ballard J. D., Clostridium difficile toxins: mechanism of action and role in disease Clinical Microbiology Reviews 2005 18 2 247 263 (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 6
    • 66549128701 scopus 로고    scopus 로고
    • Antibody-enhanced, Fc receptor-mediated endocytosis of Clostridium difficile toxin A
    • He X., Sun X., Wang J., Wang X., Zhang Q., Tzipori S., Feng H., Antibody-enhanced, Fc receptor-mediated endocytosis of Clostridium difficile toxin A Infection and Immunity 2009 77 6 2294 2303
    • (2009) Infection and Immunity , vol.77 , Issue.6 , pp. 2294-2303
    • He, X.1    Sun, X.2    Wang, J.3    Wang, X.4    Zhang, Q.5    Tzipori, S.6    Feng, H.7
  • 7
    • 75649147869 scopus 로고    scopus 로고
    • Piglet models of acute or chronic Clostridium difficile illness
    • Steele J., Feng H., Parry N., Tzipori S., Piglet models of acute or chronic Clostridium difficile illness Journal of Infectious Diseases 2010 201 3 428 434
    • (2010) Journal of Infectious Diseases , vol.201 , Issue.3 , pp. 428-434
    • Steele, J.1    Feng, H.2    Parry, N.3    Tzipori, S.4
  • 8
    • 56649108115 scopus 로고    scopus 로고
    • Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium
    • article 192
    • Yang G., Zhou B., Wang J., He X., Sun X., Nie W., Tzipori S., Feng H., Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium BMC Microbiology 2008 8, article 192
    • (2008) BMC Microbiology , vol.8
    • Yang, G.1    Zhou, B.2    Wang, J.3    He, X.4    Sun, X.5    Nie, W.6    Tzipori, S.7    Feng, H.8
  • 9
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the Major Steps in Botulinum Toxin Action
    • DOI 10.1146/annurev.pharmtox.44.101802.121554
    • Simpson L. L., Identification of the major steps in botulinum toxin action Annual Review of Pharmacology and Toxicology 2004 44 167 193 (Pubitemid 38263838)
    • (2004) Annual Review of Pharmacology and Toxicology , vol.44 , pp. 167-193
    • Simpson, L.L.1
  • 10
    • 22144452934 scopus 로고    scopus 로고
    • Beyond BOTOX: Advantages and limitations of individual botulinum neurotoxins
    • DOI 10.1016/j.tins.2005.06.001, PII S0166223605001578
    • Davletov B., Bajohrs M., Binz T., Beyond BOTOX: advantages and limitations of individual botulinum neurotoxins Trends in Neurosciences 2005 28 8 446 452 (Pubitemid 40982558)
    • (2005) Trends in Neurosciences , vol.28 , Issue.8 , pp. 446-452
    • Davletov, B.1    Bajohrs, M.2    Binz, T.3
  • 11
    • 33749268212 scopus 로고    scopus 로고
    • Entering neurons: Botulinum toxins and synaptic vesicle recycling
    • DOI 10.1038/sj.embor.7400796, PII 7400796
    • Verderio C., Rossetto O., Grumelli C., Frassoni C., Montecucco C., Matteoli M., Entering neurons: botulinum toxins and synaptic vesicle recycling EMBO Reports 2006 7 10 995 999 (Pubitemid 44480513)
    • (2006) EMBO Reports , vol.7 , Issue.10 , pp. 995-999
    • Verderio, C.1    Rossetto, O.2    Grumelli, C.3    Frassoni, C.4    Montecucco, C.5    Matteoli, M.6
  • 12
    • 0032508565 scopus 로고    scopus 로고
    • 1' binding subsite
    • DOI 10.1016/S0014-5793(98)01041-2, PII S0014579398010412
    • Schmidt J. J., Stafford R. G., Bostian K. A., Type A botulinum neurotoxin proteolytic activity: development of competitive inhibitors and implications for substrate specificity at the S1' binding subsite FEBS Letters 1998 435 1 61 64 (Pubitemid 28432015)
    • (1998) FEBS Letters , vol.435 , Issue.1 , pp. 61-64
    • Schmidt, J.J.1    Stafford, R.G.2    Bostian, K.A.3
  • 13
    • 77956059355 scopus 로고    scopus 로고
    • Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteases
    • Tremblay J. M., Kuo C. L., Abeijon C., Sepulveda J., Oyler G., Hu X., Jin M. M., Shoemaker C. B., Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteases Toxicon 2010 56 6 990 998
    • (2010) Toxicon , vol.56 , Issue.6 , pp. 990-998
    • Tremblay, J.M.1    Kuo, C.L.2    Abeijon, C.3    Sepulveda, J.4    Oyler, G.5    Hu, X.6    Jin, M.M.7    Shoemaker, C.B.8
  • 14
    • 77950022629 scopus 로고    scopus 로고
    • A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic -exosite binding region
    • Dong J., Thompson A. A., Fan Y., Lou J., Conrad F., Ho M., Pires-Alves M., Wilson B. A., Stevens R. C., Marks J. D., A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic -exosite binding region Journal of Molecular Biology 2010 397 4 1106 1118
    • (2010) Journal of Molecular Biology , vol.397 , Issue.4 , pp. 1106-1118
    • Dong, J.1    Thompson, A.A.2    Fan, Y.3    Lou, J.4    Conrad, F.5    Ho, M.6    Pires-Alves, M.7    Wilson, B.A.8    Stevens, R.C.9    Marks, J.D.10
  • 16
    • 79956353397 scopus 로고    scopus 로고
    • Accelerated neuronal cell recovery from botulinum neurotoxin intoxication by targeted ubiquitination
    • Kuo C. L., Oyler G. A., Shoemaker C. B., Accelerated neuronal cell recovery from botulinum neurotoxin intoxication by targeted ubiquitination PLoS ONE 2011 6 5
    • (2011) PLoS ONE , vol.6 , Issue.5
    • Kuo, C.L.1    Oyler, G.A.2    Shoemaker, C.B.3
  • 17
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • DOI 10.1038/nbt765
    • Keppler A., Gendreizig S., Gronemeyer T., Pick H., Vogel H., Johnsson K., A general method for the covalent labeling of fusion proteins with small molecules in vivo Nature Biotechnology 2003 21 1 86 89 (Pubitemid 36055833)
    • (2003) Nature Biotechnology , vol.21 , Issue.1 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 18
    • 0028784961 scopus 로고
    • Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen
    • LaPenotiere H. F., Clayton M. A., Middlebrook J. L., Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen Toxicon 1995 33 10 1383 1386
    • (1995) Toxicon , vol.33 , Issue.10 , pp. 1383-1386
    • Lapenotiere, H.F.1    Clayton, M.A.2    Middlebrook, J.L.3
  • 19
    • 0027284494 scopus 로고
    • Dithiothreitol generates an activated 250,000 mol. wt form of Clostridium difficile toxin B
    • Shoshan M. C., Bergman T., Thelestam M., Florin I., Dithiothreitol generates an activated 250,000 mol. wt form of Clostridium difficile toxin B Toxicon 1993 31 7 845 852
    • (1993) Toxicon , vol.31 , Issue.7 , pp. 845-852
    • Shoshan, M.C.1    Bergman, T.2    Thelestam, M.3    Florin, I.4
  • 21
    • 0037373083 scopus 로고    scopus 로고
    • Inhalational poisoning by botulinum toxin and inhalation vaccination with its heavy-chain component
    • DOI 10.1128/IAI.71.3.1147-1154.2003
    • Park J. B., Simpson L. L., Inhalational poisoning by botulinum toxin and inhalation vaccination with its heavy-chain component Infection and Immunity 2003 71 3 1147 1154 (Pubitemid 36254295)
    • (2003) Infection and Immunity , vol.71 , Issue.3 , pp. 1147-1154
    • Park, J.-B.1    Simpson, L.L.2
  • 22
    • 0242414631 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells
    • DOI 10.1074/jbc.M307540200
    • Pfeifer G., Schirmer J., Leemhuis J., Busch C., Meyer D. K., Aktories K., Barth H., Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells Journal of Biological Chemistry 2003 278 45 44535 44541 (Pubitemid 37377206)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44535-44541
    • Pfeifer, G.1    Schirmer, J.2    Leemhuis, J.3    Busch, C.4    Meyer, D.K.5    Aktories, K.6    Barth, H.7
  • 23
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek S., Papatheodorou P., Guttenberg G., Schubert R., Benz R., Aktories K., Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B Molecular Microbiology 2011 79 6 1643 1654
    • (2011) Molecular Microbiology , vol.79 , Issue.6 , pp. 1643-1654
    • Genisyuerek, S.1    Papatheodorou, P.2    Guttenberg, G.3    Schubert, R.4    Benz, R.5    Aktories, K.6
  • 25
    • 58149115498 scopus 로고    scopus 로고
    • Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile
    • Dingle T., Wee S., Mulvey G. L., Greco A., Kitova E. N., Sun J., Lin S., Klassen J. S., Palcic M. M., Ng K. K. S., Armstrong G. D., Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile Glycobiology 2008 18 9 698 706
    • (2008) Glycobiology , vol.18 , Issue.9 , pp. 698-706
    • Dingle, T.1    Wee, S.2    Mulvey, G.L.3    Greco, A.4    Kitova, E.N.5    Sun, J.6    Lin, S.7    Klassen, J.S.8    Palcic, M.M.9    Ng, K.K.S.10    Armstrong, G.D.11
  • 26
    • 0027998795 scopus 로고
    • Mutagenesis of the Clostridium difficile toxin B gene and effect on cytotoxic activity
    • DOI 10.1006/mpat.1994.1030
    • Barroso L. A., Moncrief J. S., Lyerly D. M., Wilkins T. D., Mutagenesis of the Clostridium difficile toxin B gene and effect on cytotoxic activity Microbial Pathogenesis 1994 16 4 297 303 (Pubitemid 24253074)
    • (1994) Microbial Pathogenesis , vol.16 , Issue.4 , pp. 297-303
    • Barroso, L.A.1    Moncrief, J.S.2    Lyerly, D.M.3    Wilkins, T.D.4
  • 27
    • 79951955447 scopus 로고    scopus 로고
    • Adaptation of Clostridium difficile toxin A for use as a protein translocation system
    • Kern S. M., Feig A. L., Adaptation of Clostridium difficile toxin A for use as a protein translocation system Biochemical and Biophysical Research Communications 2011 405 4 570 574
    • (2011) Biochemical and Biophysical Research Communications , vol.405 , Issue.4 , pp. 570-574
    • Kern, S.M.1    Feig, A.L.2
  • 30
    • 3342955474 scopus 로고    scopus 로고
    • Structural features of the botulinum neurotoxin molecule that govern binding and transcytosis across polarized human intestinal epithelial cells
    • DOI 10.1124/jpet.104.066845
    • A. B.Maksymowych and L. L. Simpson, "Structural features of the botulinum neurotoxin molecule that govern binding and transcytosis across polarized human intestinal epithelial cells," Journal of Pharmacology and Experimental Therapeutics, vol. 310, no. 2, pp. 633-641, 2004. (Pubitemid 38988908)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.310 , Issue.2 , pp. 633-641
    • Maksymowych, A.B.1    Simpson, L.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.