메뉴 건너뛰기




Volumn 1, Issue 3, 2009, Pages 309-317

Hemagglutinin-33 in the neurotoxin complex of typec A Clostridium botulinum is a Heat Shock Protein

Author keywords

Chaperone; Heat shock proteins; Heat stress; Hemagglutinin; HSPs; Immunoblot; Neurotoxin; Neurotoxin complex; Protection

Indexed keywords

BOTULINUM TOXIN; HEAT SHOCK PROTEIN; HEMAGGLUTININ; HEMAGGLUTININ 33; NEUROTOXIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 79952941872     PISSN: 17547326     EISSN: 17547318     Source Type: Journal    
DOI: 10.1504/TBJ.2009.031682     Document Type: Article
Times cited : (6)

References (34)
  • 2
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., Liberek, K., Skowyra, D., Zylicz, M. and Georgopoulos, C. (1991) 'Biological role and regulation of universally conserved Heat Shock proteins', J. Biol. Chem., Vol. 266, pp.24233-24236. (Pubitemid 21908929)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.36 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 3
    • 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.', Biochem., Vol. 38, pp.6903-6910.
    • (1999) Biochem. , vol.38 , pp. 6903-6910
    • Cai, S.1    Sarkar, H.K.2    Singh, B.R.3
  • 4
    • 0028785161 scopus 로고
    • In situ characterization of Clostridium botulinum neurotoxin synthesis and export
    • Call, J.E., Cooke, P.H. and Miller, A.J. (1995) 'In situ characterization of Clostridium botulinum neurotoxin synthesis and export', J. Appl. Bacteriol., Vol. 79, pp.257-263.
    • (1995) J. Appl. Bacteriol. , vol.79 , pp. 257-263
    • Call, J.E.1    Cooke, P.H.2    Miller, A.J.3
  • 5
    • 54749110992 scopus 로고    scopus 로고
    • A protease-resistant novel hemagglutinin purified from type a Clostridium botulinum
    • DOI 10.1023/A:1022590514771
    • Fu, F.N., Sharma, S.K. and Singh, B.R. (1998) 'Purification, biological activity and molecular properties of novel hemagglutinin from Type A Clostridium botulinum', J. Prot. Chem., Vol. 17, pp.53-60. (Pubitemid 28086476)
    • (1998) Journal of Protein Chemistry , vol.17 , Issue.1 , pp. 53-60
    • Fu, F.-N.1    Sharma, S.K.2    Singh, B.R.3
  • 6
    • 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, S., Hirai, Y., Nagamachi, E. and Oguma, K. (1997) 'The hemagglutinin of C. 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', Microbiol., Vol. 143, pp.3841-3847. (Pubitemid 28004616)
    • (1997) Microbiology , vol.143 , Issue.12 , pp. 3841-3847
    • Fujinaga, Y.1    Inoue, K.2    Watanabe, S.3    Yokota, K.4    Hirai, Y.5    Nagamachi, E.6    Oguma, K.7
  • 7
    • 68849102962 scopus 로고    scopus 로고
    • A novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption
    • Fujinaga, Y., Matsumura, T., Jin, Y., Takegahara, Y. and Sugawara, Y. (2009) 'A novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption', Toxicon, Vol. 54, pp.583-586.
    • (2009) Toxicon , vol.54 , pp. 583-586
    • Fujinaga, Y.1    Matsumura, T.2    Jin, Y.3    Takegahara, Y.4    Sugawara, Y.5
  • 8
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J. and Shambrook, J. (1992) 'Protein folding in the cell', Nature, Vol. 355, pp.33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Shambrook, J.2
  • 9
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • DOI 10.1016/0968-0004(94)90169-4
    • Hartl, F.U., Hlodan, R. and Langer, T. (1994) 'Molecular chaperones in protein folding: the art of avoiding sticky situations', Trends Biochem. Sci., Vol. 19, pp.20-25. (Pubitemid 24028727)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.1 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 10
    • 61449163955 scopus 로고    scopus 로고
    • Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins - Differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C
    • Jin, Y., Takegahara, Y., Sugawara, Y., Matsumura, T. and Fujinaga, Y. (2009) 'Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins - differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C', Microbiol., Vol. 155, pp.35-45.
    • (2009) Microbiol. , vol.155 , pp. 35-45
    • Jin, Y.1    Takegahara, Y.2    Sugawara, Y.3    Matsumura, T.4    Fujinaga, Y.5
  • 12
    • 62649097660 scopus 로고    scopus 로고
    • Immunological characterization of the subunits of type A Botulinum Neurotoxin and different components of its associated proteins
    • Kukreja, K., Chang, T.Z., Cai, S., Lindo, P., Riding, S., Zhou, Y., Ravichandran, R. and Singh, B.R. (2009) 'Immunological characterization of the subunits of type A Botulinum Neurotoxin and different components of its associated proteins', Toxicon, Vol. 53, pp.616-624.
    • (2009) Toxicon , vol.53 , pp. 616-624
    • Kukreja, K.1    Chang, T.Z.2    Cai, S.3    Lindo, P.4    Riding, S.5    Zhou, Y.6    Ravichandran, R.7    Singh, B.R.8
  • 13
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts
    • Li, G.C. and Werb, Z. (1982) 'Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts', Proc. Natl. Acad. Sci., USA, Vol. 79, pp.3218-3222.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 14
    • 0024151897 scopus 로고
    • Genetic regulation of heat shock proteins
    • Lindquist, S. and Craig, E.A. (1988) 'Genetic regulation of heat shock proteins', Ann. Rev. Genet., Vol. 22, pp.631-677.
    • (1988) Ann. Rev. Genet. , vol.22 , pp. 631-677
    • Lindquist, S.1    Craig, E.A.2
  • 15
    • 0025089029 scopus 로고
    • Foodborne disease due to Bacillus and Clostridium species
    • DOI 10.1016/0140-6736(90)92431-G
    • Lund, B.M. (1990) 'Foodborne disease due to Bacillus and Clostridium species', Lancet, Vol. 336, pp.982-986. (Pubitemid 20349600)
    • (1990) Lancet , vol.336 , Issue.8721 , pp. 982-986
    • Lund, B.M.1
  • 16
    • 0029188297 scopus 로고
    • Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostoc and therapeutics
    • Macario, A.J.L. (1995) 'Heat-shock proteins and molecular chaperones: implications for pathogenesis, diagnostoc and therapeutics', Int. J. Clin. Lab. Res., Vol. 25, pp.59-70.
    • (1995) Int. J. Clin. Lab. Res. , vol.25 , pp. 59-70
    • MacArio, A.J.L.1
  • 17
    • 38049150493 scopus 로고    scopus 로고
    • The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption
    • Matsumura, T., Jin, Y., Kabumoto, Y., Takegahara, Y., Oguma, K., Lencer, W.I. and Fujinaga, Y. (2008) 'The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption', Cell Microbiol., Vol. 10, pp.355-364.
    • (2008) Cell Microbiol. , vol.10 , pp. 355-364
    • Matsumura, T.1    Jin, Y.2    Kabumoto, Y.3    Takegahara, Y.4    Oguma, K.5    Lencer, W.I.6    Fujinaga, Y.7
  • 18
    • 0032432067 scopus 로고    scopus 로고
    • Diversity in protein synthesis and viability of Helicobacter pylori coccoid forms in response to various stimuli
    • Mizoguchi, H., Fujioka, T., Kishi, K., Nishizono, A., Kodama, R. and Nashu, M. (1998) 'Diversity in protein synthesis and viability of H. pylori coccoid form in response to various stimuli', Infect. Immun., Vol. 66, pp.5555-5560. (Pubitemid 29044660)
    • (1998) Infection and Immunity , vol.66 , Issue.11 , pp. 5555-5560
    • Mizoguchi, H.1    Fujioka, T.2    Kishi, K.3    Nishizono, A.4    Kodama, R.5    Nasu, M.6
  • 19
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R.I. and Santoro, M.G. (1998) 'Stress inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection', Nature Biotechnol., Vol. 16, pp.833-838. (Pubitemid 28405852)
    • (1998) Nature Biotechnology , vol.16 , Issue.9 , pp. 833-838
    • Morimoto, R.I.1    Gabriella Santoro, M.2
  • 20
    • 0021693955 scopus 로고
    • The genetics and regulation of heat shock proteins
    • Neidhardt, F.C., VanBogelen, R.A. and Vaughn, V. (1984) 'The genetics and regulation of heat shock proteins', Ann. Rev. Genet., Vol. 18, pp.295-329.
    • (1984) Ann. Rev. Genet. , vol.18 , pp. 295-329
    • Neidhardt, F.C.1    Vanbogelen, R.A.2    Vaughn, V.3
  • 21
    • 33947285071 scopus 로고    scopus 로고
    • Role of nontoxic components of serotype D botulinum toxin complex in permeation through a Caco-2 cell monolayer, a model for intestinal epithelium
    • DOI 10.1111/j.1574-695X.2006.00205.x
    • Niwa, K., Koyama, K., Inoue, S., Suzuki, T., Hasegawa, K., Watanabe, T., Ikeda, T. and Ohyama, T. (2007) 'Role of nontoxic components of serotype D botulinum toxin complex in permeation through a Caco-2 cell monolayer, a model for intestinal epithelium', FEMS Immunol. Med. Microbiol., Vol. 49, pp.346-352. (Pubitemid 46435011)
    • (2007) FEMS Immunology and Medical Microbiology , vol.49 , Issue.3 , pp. 346-352
    • Niwa, K.1    Koyama, K.2    Inoue, S.-I.3    Suzuki, T.4    Hasegawa, K.5    Watanabe, T.6    Ikeda, T.7    Ohyama, T.8
  • 22
    • 0025113660 scopus 로고
    • Inductiobn of heat shock proteins during solvent formation, Clostridium acetobutalicum
    • Pich, A., Narberhaus, F. and Bahl, H. (1990) 'Inductiobn of heat shock proteins during solvent formation, Clostridium acetobutalicum.', Appl. Microbiol. Biotechnol., Vol. 33, pp.697-700.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 697-700
    • Pich, A.1    Narberhaus, F.2    Bahl, H.3
  • 23
    • 67649292434 scopus 로고    scopus 로고
    • How do the Botulinum Neurotoxins block neurotransmitter release: From botulism to the molecular mechanism of action
    • Poulain, B., Popoff, M and Molgo, J. (2008) 'How do the Botulinum Neurotoxins block neurotransmitter release: from botulism to the molecular mechanism of action', The Botulinum J. Vol. 1, pp.14-87.
    • (2008) The Botulinum J. , vol.1 , pp. 14-87
    • Poulain, B.1    Popoff, M.2    Molgo, J.3
  • 24
    • 0020286209 scopus 로고
    • Clostridium botulinum toxins
    • Sakaguchi, G. (1983) 'Clostridium botulinum toxins', Pharmac. Ther., Vol. 19, pp.165-194. (Pubitemid 13112836)
    • (1982) Pharmacology and Therapeutics , vol.19 , Issue.2 , pp. 165-194
    • Sakaguchi, G.1
  • 25
    • 0033695937 scopus 로고    scopus 로고
    • Immunological properties of Hn-33 purified from type A Clostridium botulinum
    • Sharma, S. and Singh, B.R. (2000) 'Immunological properties of Hn-33 purified from type A Clostridium botulinum', J. Nat. Toxin, Vol. 9, pp.357-362.
    • (2000) J. Nat. Toxin , vol.9 , pp. 357-362
    • Sharma, S.1    Singh, B.R.2
  • 26
    • 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. Toxin., Vol. 7, pp.239-253. (Pubitemid 28456460)
    • (1998) Journal of Natural Toxins , vol.7 , Issue.3 , pp. 239-253
    • Sharma, S.K.1    Singh, B.R.2
  • 27
    • 53149125684 scopus 로고    scopus 로고
    • Molecular properties of a hemagglutinin purified from type A Clostridium botulinum
    • Sharma, S.K., Fu, F.N. and Singh, B.R. (1999) 'Molecular properties of a hemagglutinin purified from type A Clostridium botulinum', J. Prot. Chem., Vol. 1, pp.29-38. (Pubitemid 29117422)
    • (1999) Journal of Protein Chemistry , vol.18 , Issue.1 , pp. 29-38
    • Sharma, S.K.1    Fu, F.-N.2    Singh, B.R.3
  • 28
    • 53149114193 scopus 로고    scopus 로고
    • Identification of DnaJ-like chaperone in Clostridium botulinum type A
    • Shukla, H.D. and Singh, B.R. (1999) 'Identification of DnaJ-like chaperone in Clostridium botulinum type A', J. Prot. Chem., Vol. 18, pp.603-608.
    • (1999) J. Prot. Chem. , vol.18 , pp. 603-608
    • Shukla, H.D.1    Singh, B.R.2
  • 29
    • 0028912028 scopus 로고
    • Physico-chemical and immunological characterization of the type e botulinum neurotoxin binding proteins purified from Clostridium botulinum
    • Singh, B.R., Foley, J. and Lafontaine, C. (1995) 'Physico-chemical and immunological characterization of the type E botulinum neurotoxin binding proteins purified from Clostridium botulinum', J. Prot. Chem., Vol. 14, pp.7-18.
    • (1995) J. Prot. Chem. , vol.14 , pp. 7-18
    • Singh, B.R.1    Foley, J.2    Lafontaine, C.3
  • 30
    • 0025029317 scopus 로고
    • Synthesis of species-specific stress proteins by virulent strains of Listeria monocytogenes
    • Sokolovic, Z., Fuchs, A. and Goebel, W. (1990) 'Synthesis of species-specific stress proteins by virulent strains of Listeria monocytogens', Infect. Immun., Vol. 58, pp.3582-3587. (Pubitemid 20353356)
    • (1990) Infection and Immunity , vol.58 , Issue.11 , pp. 3582-3587
    • Sokolovic, Z.1    Fuchs, A.2    Goebel, W.3
  • 31
    • 0002424105 scopus 로고
    • Botulogenic properties of vegetables with special reference to the molecular size of toxin in them
    • Sugii, S. and Sakaguchi, G. (1977) 'Botulogenic properties of vegetables with special reference to the molecular size of toxin in them', J. Food Safety, Vol. 1, pp.53-65.
    • (1977) J. Food Safety , vol.1 , pp. 53-65
    • Sugii, S.1    Sakaguchi, G.2
  • 32
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • DOI 10.1074/jbc.273.18.11032
    • Veinger, L., Diamant, S., Buchner, J. and Goloubinoff, P. (1998) 'The small heat shock protein IbpB from E. coli stablizes stress-denatured proteins for subsequent refolding by a multichaperone network', J. Biol. Chem., Vol. 273, pp.11032-11037. (Pubitemid 28204946)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 33
    • 0030903131 scopus 로고    scopus 로고
    • Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • Vickery, L.E., Silberg, J.J. and Ta, D.T. (1997) 'Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system form E. coli.', Prot. Sci., Vol. 6, pp.1047-1056. (Pubitemid 27194145)
    • (1997) Protein Science , vol.6 , Issue.5 , pp. 1047-1056
    • Vickery, L.E.1    Silberg, J.J.2    Ta, D.T.3
  • 34
    • 20444479445 scopus 로고    scopus 로고
    • Hemagglutinin-33 of type A botulinum neurotoxin complex binds with synaptotagmin II
    • DOI 10.1111/j.1742-4658.2005.04688.x
    • Zhou, Y., Foss, S., Lindo, P., Sarkar, H. and Singh, B.R. (2005) 'Hemagglutinin-33 of type A botulinum neurotoxin complex binds with synaptotagmin II', FEBS J., Vol. 272, pp.2717-2726. (Pubitemid 40825419)
    • (2005) FEBS Journal , vol.272 , Issue.11 , pp. 2717-2726
    • Zhou, Y.1    Foss, S.2    Lindo, P.3    Sarkar, H.4    Singh, B.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.