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Volumn 46, Issue 49, 2007, Pages 14316-14324

Comparative role of neurotoxin-associated proteins in the structural stability and endopeptidase activity of botulinum neurotoxin complex types A and E

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM NEUROTOXIN COMPLEX; ENDOPEPTIDASE ACTIVITY; PROTEOLYTIC DIGESTION; STRUCTURAL STABILITY;

EID: 37049016293     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701564f     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 37049232988 scopus 로고
    • The most poisonous poison
    • Lamanna, C. (1959) The most poisonous poison, Science 130, 763-772.
    • (1959) Science , vol.130 , pp. 763-772
    • Lamanna, C.1
  • 2
    • 0033887387 scopus 로고    scopus 로고
    • Intimate details of the most poisonous poison
    • Singh, B. R. (2000) Intimate details of the most poisonous poison, Nat. Struct. Biol. 7, 617-619.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 617-619
    • Singh, B.R.1
  • 3
    • 3142744650 scopus 로고    scopus 로고
    • Botulinum neurotoxin: The neuromuscular junction revisited
    • Coffield, J. A. (2003) Botulinum neurotoxin: the neuromuscular junction revisited, Crict. Rev. Neurobiol. 15, 175-195.
    • (2003) Crict. Rev. Neurobiol , vol.15 , pp. 175-195
    • Coffield, J.A.1
  • 4
    • 1942439990 scopus 로고    scopus 로고
    • The therapeutic potential of botulinum toxin
    • Klien, A. W. (2004) The therapeutic potential of botulinum toxin, Dermatol. Surg. 30, 452-455.
    • (2004) Dermatol. Surg , vol.30 , pp. 452-455
    • Klien, A.W.1
  • 5
    • 22844451959 scopus 로고    scopus 로고
    • Expanding use of botulinum toxin
    • Bhidayasiri, R., and Truong, D. D. (2005) Expanding use of botulinum toxin, J. Neurol. Sci. 235, 1-9.
    • (2005) J. Neurol. Sci , vol.235 , pp. 1-9
    • Bhidayasiri, R.1    Truong, D.D.2
  • 6
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C., and Schiavo, G. (1995) Structure and function of tetanus and botulinum neurotoxins, Q. Rev. Biophys. 28, 423-472.
    • (1995) Q. Rev. Biophys , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 7
    • 17144377560 scopus 로고    scopus 로고
    • Botulinum toxin: Mechanisms of action
    • Dressler, D., and Saberi, F. A. (2005) Botulinum toxin: mechanisms of action, Eur. Neurol. 53, 3-9.
    • (2005) Eur. Neurol , vol.53 , pp. 3-9
    • Dressler, D.1    Saberi, F.A.2
  • 10
    • 0033065263 scopus 로고    scopus 로고
    • Structure-function relationship of clostridial neurotoxins
    • Li, L., and Singh, B. R. (1999) Structure-function relationship of clostridial neurotoxins, J. Toxicol., Toxin Rev. 18, 95-112.
    • (1999) J. Toxicol., Toxin Rev , vol.18 , pp. 95-112
    • Li, L.1    Singh, B.R.2
  • 11
    • 33645086131 scopus 로고    scopus 로고
    • Clostridial neurotoxins: Structure-function led design of new therapeutics
    • Chaddock, J. A., and Marks, P. M. H. (2006) Clostridial neurotoxins: structure-function led design of new therapeutics, Cell. Mol. Life Sci. 63, 540-51.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 540-551
    • Chaddock, J.A.1    Marks, P.M.H.2
  • 12
    • 0031866118 scopus 로고    scopus 로고
    • Biophysical characterization of the stability of the 150 kDa botulinum toxin, the nontoxic component, and the 900-kDa botulinum toxin complex species
    • Chen, F., Kuziemko, G. M., and Stevens, R. C. (1998) Biophysical characterization of the stability of the 150 kDa botulinum toxin, the nontoxic component, and the 900-kDa botulinum toxin complex species, Infect. Immun. 66, 2420-2425.
    • (1998) Infect. Immun , vol.66 , pp. 2420-2425
    • Chen, F.1    Kuziemko, G.M.2    Stevens, R.C.3
  • 13
    • 0034121745 scopus 로고    scopus 로고
    • Humeau, Y., Doussau, Grant, F., N. J., and Poulain, B. (2000) How botulinum and tetanus neurotoxins block neurotransmitter release, Biochimie 82, 427-46.
    • Humeau, Y., Doussau, Grant, F., N. J., and Poulain, B. (2000) How botulinum and tetanus neurotoxins block neurotransmitter release, Biochimie 82, 427-46.
  • 15
    • 0011113530 scopus 로고    scopus 로고
    • Brin, M. F, Jankovic, J, and Hallet, M, Eds, pp, Lipincott Williams and Wilkins, Philadelphia
    • Singh, B. R. (2002) in Scientific and Therapeutic Aspects of Botulinum Toxin (Brin, M. F., Jankovic, J., and Hallet, M., Eds.) pp 75-88, Lipincott Williams and Wilkins, Philadelphia.
    • (2002) Scientific and Therapeutic Aspects of Botulinum Toxin , pp. 75-88
    • Singh, B.R.1
  • 16
    • 3042769298 scopus 로고    scopus 로고
    • The story of clostridium botulinum: From food poisoning to botox
    • Ting, P. T., and Freiman, A. (2004) The story of clostridium botulinum: from food poisoning to botox, Clin. Med. 4, 258-261.
    • (2004) Clin. Med , vol.4 , pp. 258-261
    • Ting, P.T.1    Freiman, A.2
  • 17
    • 0032491905 scopus 로고    scopus 로고
    • Molecular characterization of type E Clostridium botulinum and comparison to other types of Clostridium botulinum
    • Li, B., Qian, X., Sarkar, H. K., and Singh, B. R. (1998) Molecular characterization of type E Clostridium botulinum and comparison to other types of Clostridium botulinum, Biochim. Biophys. Acta 1395, 21-1.
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 21-21
    • Li, B.1    Qian, X.2    Sarkar, H.K.3    Singh, B.R.4
  • 18
    • 1942502773 scopus 로고    scopus 로고
    • Enhancement of the endopeptidase activity of purified neurotoxins A and E by an isolated component of the native neurotoxin associated proteins
    • Sharma, S., and Singh, B. R. (2004) Enhancement of the endopeptidase activity of purified neurotoxins A and E by an isolated component of the native neurotoxin associated proteins, Biochemistry 43, 4791-4798.
    • (2004) Biochemistry , vol.43 , pp. 4791-4798
    • Sharma, S.1    Singh, B.R.2
  • 19
    • 0031435919 scopus 로고    scopus 로고
    • The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin
    • Fujinaga, Y., Inoue, K., Watanabe, S., Yokota, K., Hirai, Y., Nagamachi, E., and Oguma, K. (1997) The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin, Microbiology 143, 3841-3847.
    • (1997) Microbiology , vol.143 , pp. 3841-3847
    • Fujinaga, Y.1    Inoue, K.2    Watanabe, S.3    Yokota, K.4    Hirai, Y.5    Nagamachi, E.6    Oguma, K.7
  • 20
    • 2942555014 scopus 로고    scopus 로고
    • Molecular characterization of binding subcomponents of Clostridium botulinum type C progenitor toxin for intestinal epithelial cells and erythrocytes
    • Fujinaga, Y., Inoue, K., Watanabe, S., Sakaguchi, Y., Arimitsu, H., Lee, J .C., Jin, Y., Matsumura, T., Kabumoto, Y., Watanabe, T., and Ohyama, T. (2004) Molecular characterization of binding subcomponents of Clostridium botulinum type C progenitor toxin for intestinal epithelial cells and erythrocytes, Microbiology 150, 1529-1538.
    • (2004) Microbiology , vol.150 , pp. 1529-1538
    • Fujinaga, Y.1    Inoue, K.2    Watanabe, S.3    Sakaguchi, Y.4    Arimitsu, H.5    Lee, J.C.6    Jin, Y.7    Matsumura, T.8    Kabumoto, Y.9    Watanabe, T.10    Ohyama, T.11
  • 22
    • 16244423360 scopus 로고    scopus 로고
    • Clostridium botulinum: A bug with beauty and weapon
    • Shukla, H. D., and Sharma, S. K. (2005) Clostridium botulinum: A bug with beauty and weapon, Crit. Rev. Microbiol. 31, 11-18.
    • (2005) Crit. Rev. Microbiol , vol.31 , pp. 11-18
    • Shukla, H.D.1    Sharma, S.K.2
  • 23
    • 0033602922 scopus 로고    scopus 로고
    • Enhancement of the endopeptidase activity of botulinum neurotoxin by its associated proteins and dithiothreitol
    • Cai, S., Sarkar, H. K., and Singh, B. R. (1999) Enhancement of the endopeptidase activity of botulinum neurotoxin by its associated proteins and dithiothreitol, Biochemistry 38, 6903-6910.
    • (1999) Biochemistry , vol.38 , pp. 6903-6910
    • Cai, S.1    Sarkar, H.K.2    Singh, B.R.3
  • 24
    • 0020286209 scopus 로고
    • Clostridium botulinum toxins
    • Sakaguchi, G. (1983) Clostridium botulinum toxins, Pharmacol. Ther. 19, 165-194.
    • (1983) Pharmacol. Ther , vol.19 , pp. 165-194
    • Sakaguchi, G.1
  • 25
    • 37049023388 scopus 로고    scopus 로고
    • Novel proteins within the type E botulinum neurotoxin complex,
    • U.S. Patent No. 6,699,966
    • Singh, B. R. and Zhang, Z. (2004) Novel proteins within the type E botulinum neurotoxin complex, U.S. Patent No. 6,699,966.
    • (2004)
    • Singh, B.R.1    Zhang, Z.2
  • 26
    • 0029597914 scopus 로고
    • Botulinum versus tetanus neurotoxins: Why is botulinum neurotoxin but not tetanus neurotoxin a food poison?
    • Singh, B. R., Li, B., and Read, D. (1995) Botulinum versus tetanus neurotoxins: why is botulinum neurotoxin but not tetanus neurotoxin a food poison?, Toxicon 33, 1541-1547.
    • (1995) Toxicon , vol.33 , pp. 1541-1547
    • Singh, B.R.1    Li, B.2    Read, D.3
  • 27
    • 0021128925 scopus 로고
    • Purification and amino acid composition of type A botulinum neurotoxin
    • DasGupta, B. R., and Satyamoorthy, V. (1984) Purification and amino acid composition of type A botulinum neurotoxin, Toxicon 22, 415-424.
    • (1984) Toxicon , vol.22 , pp. 415-424
    • DasGupta, B.R.1    Satyamoorthy, V.2
  • 28
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of β-turns
    • Chang, C., Wu, C., and Yang, J. (1978) Circular dichroic analysis of protein conformation: inclusion of β-turns, Anal. Biochem. 91, 13-31.
    • (1978) Anal. Biochem , vol.91 , pp. 13-31
    • Chang, C.1    Wu, C.2    Yang, J.3
  • 29
    • 0032515962 scopus 로고    scopus 로고
    • Role of zinc in the structure and toxic activity of botulinum neurotoxin
    • Fu, F., Lomneth, R. B., Cai, S., and Singh, B. R. (1998) Role of zinc in the structure and toxic activity of botulinum neurotoxin, Biochemistry 37, 5267-5278.
    • (1998) Biochemistry , vol.37 , pp. 5267-5278
    • Fu, F.1    Lomneth, R.B.2    Cai, S.3    Singh, B.R.4
  • 30
    • 0023219317 scopus 로고
    • Unfolding pathway of myoglobin: Effect of denaturants on solvent accessibility to tyrosyl residues detected by second derivative spectroscopy
    • Ragone, R., Colonna, G., Bismuto, E., and Irace, G. (1987) Unfolding pathway of myoglobin: effect of denaturants on solvent accessibility to tyrosyl residues detected by second derivative spectroscopy, Biochemistry 26, 2130-2134.
    • (1987) Biochemistry , vol.26 , pp. 2130-2134
    • Ragone, R.1    Colonna, G.2    Bismuto, E.3    Irace, G.4
  • 31
    • 0024566869 scopus 로고
    • Structure of heavy and light chain subunits of type A botulinum neurotoxin analyzed by circular dichroism and fluorescence measurements
    • Singh, B. R., and DasGupta, B. R. (1989) Structure of heavy and light chain subunits of type A botulinum neurotoxin analyzed by circular dichroism and fluorescence measurements, Mol. Cell. Biochem. 86, 87-95.
    • (1989) Mol. Cell. Biochem , vol.86 , pp. 87-95
    • Singh, B.R.1    DasGupta, B.R.2
  • 32
    • 0028912028 scopus 로고
    • Physicochemical and immunological characterization of type E botulinum neurotoxin binding protein purified from Clostridium botulinum
    • Singh, B. R., Foley, J., and Lafontaine, C. (1995) Physicochemical and immunological characterization of type E botulinum neurotoxin binding protein purified from Clostridium botulinum, J. Protein Chem. 14, 7-18.
    • (1995) J. Protein Chem , vol.14 , pp. 7-18
    • Singh, B.R.1    Foley, J.2    Lafontaine, C.3
  • 33
    • 1942422576 scopus 로고    scopus 로고
    • Organization and regulation of neurotoxin genes in Clostridium botulinum and Clostridium tetani
    • Raffestien, S., Marvaud, J. C., Cerrato, R., Dupuy, B., and Popoff, M. (2004) Organization and regulation of neurotoxin genes in Clostridium botulinum and Clostridium tetani, Anaerobe 10, 93-100.
    • (2004) Anaerobe , vol.10 , pp. 93-100
    • Raffestien, S.1    Marvaud, J.C.2    Cerrato, R.3    Dupuy, B.4    Popoff, M.5
  • 35
    • 0025099402 scopus 로고
    • Thermodynamics of thermal and athermal denaturation of gamma-crystallins: Changes in conformational stability upon glutathione reaction
    • Kono, M., Sen, A. C., and Chakravarti, B. (1990) Thermodynamics of thermal and athermal denaturation of gamma-crystallins: changes in conformational stability upon glutathione reaction, Biochemistry 29, 464-470.
    • (1990) Biochemistry , vol.29 , pp. 464-470
    • Kono, M.1    Sen, A.C.2    Chakravarti, B.3
  • 36
    • 28244483285 scopus 로고    scopus 로고
    • Biologically active novel conformational state of botulinum, the most poisonous poison
    • Kukreja, R., and Singh, B. R. (2005) Biologically active novel conformational state of botulinum, the most poisonous poison, J. Biol. Chem. 280, 39346-39352.
    • (2005) J. Biol. Chem , vol.280 , pp. 39346-39352
    • Kukreja, R.1    Singh, B.R.2
  • 37
    • 0000695967 scopus 로고
    • Heat-induced conformational changes in phaseolin and its relation to proteolysis
    • Deshpande, S. S., and Damodaran, S. (1989) Heat-induced conformational changes in phaseolin and its relation to proteolysis, Biochim. Biophys. Acta, 998, 179-188.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 179-188
    • Deshpande, S.S.1    Damodaran, S.2
  • 38
    • 0034730087 scopus 로고    scopus 로고
    • Role of zinc binding in type A botulinum neurotoxin light chain's toxic structure
    • Li, L., and Singh, B. R. (2000) Role of zinc binding in type A botulinum neurotoxin light chain's toxic structure, Biochemistry 39, 10581-10586.
    • (2000) Biochemistry , vol.39 , pp. 10581-10586
    • Li, L.1    Singh, B.R.2
  • 39
    • 0039842494 scopus 로고    scopus 로고
    • Spectroscopic analysis of pH-Induced changes in the molecular features of type A botulinum neurotoxin light chain
    • Li, L., and Singh, B. R. (2000) Spectroscopic analysis of pH-Induced changes in the molecular features of type A botulinum neurotoxin light chain, Biochemistry 39, 6646-6474.
    • (2000) Biochemistry , vol.39 , pp. 6646-6474
    • Li, L.1    Singh, B.R.2
  • 40
    • 0025103812 scopus 로고
    • Conformational changes associated with the nicking and activation of botulinum neurotoxin type E
    • Singh, B. R., and DasGupta, B. R. (1990) Conformational changes associated with the nicking and activation of botulinum neurotoxin type E, Biophys. Chem. 38, 123-130.
    • (1990) Biophys. Chem , vol.38 , pp. 123-130
    • Singh, B.R.1    DasGupta, B.R.2
  • 41
    • 0021759419 scopus 로고
    • Determination of Tyrosine exposure in proteins by Second-Derivative Spectroscopy
    • Ragone, R., Colonna, G., Balestrieri, C., Servillo, L., and Irace, G. (1984) Determination of Tyrosine exposure in proteins by Second-Derivative Spectroscopy, Biochemistry 23, 1871-1875.
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 42
    • 0025647664 scopus 로고
    • Structural Analysis of Botulinum Neurotoxin type A and E in aqueous and nonpolar solvents by Fourier Transform Infrared, Second Derivative UV Absorption, and Circular Dichroic Spectroscopies
    • Singh, B. R., Wasacz, F. M., Strand, S., Jacobsen, R. J., and DasGupta, B. R. (1990) Structural Analysis of Botulinum Neurotoxin type A and E in aqueous and nonpolar solvents by Fourier Transform Infrared, Second Derivative UV Absorption, and Circular Dichroic Spectroscopies, J. Protein Chem. 9, 705-713.
    • (1990) J. Protein Chem , vol.9 , pp. 705-713
    • Singh, B.R.1    Wasacz, F.M.2    Strand, S.3    Jacobsen, R.J.4    DasGupta, B.R.5
  • 43
    • 33747188659 scopus 로고    scopus 로고
    • Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting
    • Singh, B. R. (2006) Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting, Neurotox. Res. 9, 73-92.
    • (2006) Neurotox. Res , vol.9 , pp. 73-92
    • Singh, B.R.1
  • 44
    • 0027248876 scopus 로고
    • Tetanus and botulinum neurotoxins: A new group of zinc proteases
    • Montecucco, C., and Schiavo, G. (1993) Tetanus and botulinum neurotoxins: a new group of zinc proteases, Trends Biochem. Sci. 18, 324-327.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 45
    • 0035909839 scopus 로고    scopus 로고
    • Role of the disulfide cleavage induced molten globule state of type A botulinum neurotoxin in its endopeptidase activity
    • Cai, S., and Singh, B. R. (2001) Role of the disulfide cleavage induced molten globule state of type A botulinum neurotoxin in its endopeptidase activity, Biochemistry 50, 15327-15333.
    • (2001) Biochemistry , vol.50 , pp. 15327-15333
    • Cai, S.1    Singh, B.R.2
  • 46
    • 54749110992 scopus 로고    scopus 로고
    • A protease-resistant novel hemagglutinin purified from type A Clostridium botulinum
    • Fu, F. N., Sharma, S. K., and Singh, B. R. (1998) A protease-resistant novel hemagglutinin purified from type A Clostridium botulinum, J. Protein Chem. 17, 53-60.
    • (1998) J. Protein Chem , vol.17 , pp. 53-60
    • Fu, F.N.1    Sharma, S.K.2    Singh, B.R.3
  • 47
    • 0032189946 scopus 로고    scopus 로고
    • Hemagglutinin binding mediated protection of botulinum neurotoxin from proteolysis
    • Sharma, S. K., and Singh, B. R. (1998) Hemagglutinin binding mediated protection of botulinum neurotoxin from proteolysis, J. Nat. Toxins 7, 239-253.
    • (1998) J. Nat. Toxins , vol.7 , pp. 239-253
    • Sharma, S.K.1    Singh, B.R.2
  • 48
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy, D. B., Tepp, W., Cohen, A. C., DasGupta, B. R., and Stevens, R. C. (1998) Crystal structure of botulinum neurotoxin type A and implications for toxicity, Nat. Struct. Biol. 5, 898-902.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    DasGupta, B.R.4    Stevens, R.C.5
  • 49
    • 0024564405 scopus 로고
    • Effect of tetranitromethane on the biological activities of botulinum neurotoxin types A, B and E
    • Woody, M. A., and DasGupta, B. R. (1989) Effect of tetranitromethane on the biological activities of botulinum neurotoxin types A, B and E, Mol. Cell. Biochem. 85, 159-169.
    • (1989) Mol. Cell. Biochem , vol.85 , pp. 159-169
    • Woody, M.A.1    DasGupta, B.R.2


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