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Volumn 13, Issue 11, 2011, Pages 1731-1743

Double anchorage to the membrane and intact inter-chain disulfide bond are required for the low pH induced entry of tetanus and botulinum neurotoxins into neurons

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; METALLOPROTEINASE; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TETANUS TOXIN; UNCLASSIFIED DRUG;

EID: 80054105849     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2011.01654.x     Document Type: Article
Times cited : (57)

References (83)
  • 1
    • 33748769520 scopus 로고    scopus 로고
    • A structural perspective of the sequence variability within botulinum neurotoxin subtypes A1-A4
    • Arndt, J.W., Jacobson, M.J., Abola, E.E., Forsyth, C.M., Tepp, W.H., Marks, J.D., etal. (2006) A structural perspective of the sequence variability within botulinum neurotoxin subtypes A1-A4. J Mol Biol 362: 733-742.
    • (2006) J Mol Biol , vol.362 , pp. 733-742
    • Arndt, J.W.1    Jacobson, M.J.2    Abola, E.E.3    Forsyth, C.M.4    Tepp, W.H.5    Marks, J.D.6
  • 2
    • 57349090665 scopus 로고    scopus 로고
    • Very fast prediction and rationalization of pka values for protein ligand complexes
    • Bas, D.C., Rogers, D.M., and Jensen, J.H. (2008) Very fast prediction and rationalization of pka values for protein ligand complexes. Proteins 73: 765-783.
    • (2008) Proteins , vol.73 , pp. 765-783
    • Bas, D.C.1    Rogers, D.M.2    Jensen, J.H.3
  • 3
    • 0028040137 scopus 로고
    • Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule
    • Beise, J., Hahnen, J., Andersen-Beckh, B., and Dreyer, F. (1994) Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule. Naunyn Schmiedebergs Arch Pharmacol 349: 66-73.
    • (1994) Naunyn Schmiedebergs Arch Pharmacol , vol.349 , pp. 66-73
    • Beise, J.1    Hahnen, J.2    Andersen-Beckh, B.3    Dreyer, F.4
  • 4
    • 65949090949 scopus 로고    scopus 로고
    • Cell entry strategy of clostridial neurotoxins
    • Binz, T., and Rummel, A. (2009) Cell entry strategy of clostridial neurotoxins. J Neurochem 109: 1584-1595.
    • (2009) J Neurochem , vol.109 , pp. 1584-1595
    • Binz, T.1    Rummel, A.2
  • 5
    • 0023662110 scopus 로고
    • The N-terminal half of the heavy chain of botulinum type a neurotoxin forms channels in planar phospholipid bilayers
    • Blaustein, R.O., Germann, W.J., Finkelstein, A., and DasGupta, B.R. (1987) The N-terminal half of the heavy chain of botulinum type a neurotoxin forms channels in planar phospholipid bilayers. FEBS Lett 226: 115-120.
    • (1987) FEBS Lett , vol.226 , pp. 115-120
    • Blaustein, R.O.1    Germann, W.J.2    Finkelstein, A.3    DasGupta, B.R.4
  • 6
    • 0020368289 scopus 로고
    • Tetanus toxin fragment forms channels in lipid vesicles at low pH
    • Boquet, P., and Duflot, E. (1982) Tetanus toxin fragment forms channels in lipid vesicles at low pH. Proc Natl Acad Sci USA 79: 7614-7618.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7614-7618
    • Boquet, P.1    Duflot, E.2
  • 7
    • 33845885528 scopus 로고    scopus 로고
    • Structural basis of cell surface receptor recognition by botulinum neurotoxin B
    • Chai, Q., Arndt, J.W., Dong, M., Tepp, W.H., Johnson, E.A., Chapman, E.R., etal. (2006) Structural basis of cell surface receptor recognition by botulinum neurotoxin B. Nature 444: 1096-1100.
    • (2006) Nature , vol.444 , pp. 1096-1100
    • Chai, Q.1    Arndt, J.W.2    Dong, M.3    Tepp, W.H.4    Johnson, E.A.5    Chapman, E.R.6
  • 8
    • 46849085158 scopus 로고    scopus 로고
    • Molecular basis for tetanus toxin coreceptor interactions
    • Chen, C., Baldwin, M.R., and Barbieri, J.T. (2008) Molecular basis for tetanus toxin coreceptor interactions. Biochemistry 47: 7179-7186.
    • (2008) Biochemistry , vol.47 , pp. 7179-7186
    • Chen, C.1    Baldwin, M.R.2    Barbieri, J.T.3
  • 9
    • 70350371732 scopus 로고    scopus 로고
    • Gangliosides as high affinity receptors for tetanus neurotoxin
    • Chen, C., Fu, Z., Kim, J.P., Barbieri, J.T., and Baldwin, M.R. (2009) Gangliosides as high affinity receptors for tetanus neurotoxin. J Biol Chem 284: 26569-26577.
    • (2009) J Biol Chem , vol.284 , pp. 26569-26577
    • Chen, C.1    Fu, Z.2    Kim, J.P.3    Barbieri, J.T.4    Baldwin, M.R.5
  • 10
    • 0034878448 scopus 로고    scopus 로고
    • Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century
    • Collier, R.J. (2001) Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. Toxicon 39: 1793-1803.
    • (2001) Toxicon , vol.39 , pp. 1793-1803
    • Collier, R.J.1
  • 11
    • 22144452934 scopus 로고    scopus 로고
    • Beyond botox: advantages and limitations of individual botulinum neurotoxins
    • Davletov, B., Bajohrs, M., and Binz, T. (2005) Beyond botox: advantages and limitations of individual botulinum neurotoxins. Trends Neurosci 28: 446-452.
    • (2005) Trends Neurosci , vol.28 , pp. 446-452
    • Davletov, B.1    Bajohrs, M.2    Binz, T.3
  • 12
    • 0027442858 scopus 로고
    • A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly
    • De Paiva, A., Poulain, B., Lawrence, G.W., Shone, C.C., Tauc, L., and Dolly, J.O. (1993) A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly. J Biol Chem 268: 20838-20844.
    • (1993) J Biol Chem , vol.268 , pp. 20838-20844
    • De Paiva, A.1    Poulain, B.2    Lawrence, G.W.3    Shone, C.C.4    Tauc, L.5    Dolly, J.O.6
  • 13
    • 33646248918 scopus 로고    scopus 로고
    • SV2 is the protein receptor for botulinum neurotoxin A
    • Dong, M., Yeh, F., Tepp, W.H., Dean, C., Johnson, E.A., Janz, R., etal. (2006) SV2 is the protein receptor for botulinum neurotoxin A. Science 312: 592-596.
    • (2006) Science , vol.312 , pp. 592-596
    • Dong, M.1    Yeh, F.2    Tepp, W.H.3    Dean, C.4    Johnson, E.A.5    Janz, R.6
  • 14
    • 58549094719 scopus 로고    scopus 로고
    • Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons
    • Dong, M., Liu, H., Tepp, W.H., Johnson, E.A., Janz, R., and Chapman, E.R. (2008) Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons. Mol Biol Cell 19: 5226-5237.
    • (2008) Mol Biol Cell , vol.19 , pp. 5226-5237
    • Dong, M.1    Liu, H.2    Tepp, W.H.3    Johnson, E.A.4    Janz, R.5    Chapman, E.R.6
  • 15
    • 0022485787 scopus 로고
    • Ion-conducting channels produced by botulinum toxin in planar lipid membranes
    • Donovan, J.J., and Middlebrook, J.L. (1986) Ion-conducting channels produced by botulinum toxin in planar lipid membranes. Biochemistry 25: 2872-2876.
    • (1986) Biochemistry , vol.25 , pp. 2872-2876
    • Donovan, J.J.1    Middlebrook, J.L.2
  • 16
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement
    • Draper, R.K., and Simon, M.I. (1980) The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement. J Cell Biol 87: 849-854.
    • (1980) J Cell Biol , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 17
    • 1442349932 scopus 로고    scopus 로고
    • Role of metals in the biological activity of clostridium botulinum neurotoxins
    • Eswaramoorthy, S., Kumaran, D., Keller, J., and Swaminathan, S. (2004) Role of metals in the biological activity of clostridium botulinum neurotoxins. Biochemistry 43: 2209-2216.
    • (2004) Biochemistry , vol.43 , pp. 2209-2216
    • Eswaramoorthy, S.1    Kumaran, D.2    Keller, J.3    Swaminathan, S.4
  • 18
    • 34547509346 scopus 로고    scopus 로고
    • Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes
    • Fischer, A., and Montal, M. (2007a) Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes. Proc Natl Acad Sci USA 104: 10447-10452.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10447-10452
    • Fischer, A.1    Montal, M.2
  • 19
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • Fischer, A., and Montal, M. (2007b) Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes. J Biol Chem 282: 29604-29611.
    • (2007) J Biol Chem , vol.282 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 20
    • 58149252452 scopus 로고    scopus 로고
    • Botulinum neurotoxin devoid of receptor binding domain translocates active protease
    • Fischer, A., Mushrush, D.J., Lacy, D.B., and Montal, M. (2008) Botulinum neurotoxin devoid of receptor binding domain translocates active protease. PLoS Pathog 4: e1000245.
    • (2008) PLoS Pathog , vol.4
    • Fischer, A.1    Mushrush, D.J.2    Lacy, D.B.3    Montal, M.4
  • 21
    • 0035943672 scopus 로고    scopus 로고
    • The crystal structure of tetanus toxin HC fragment complexed with a synthetic gt1b analogue suggests cross-linking between ganglioside receptors and the toxin
    • Fotinou, C., Emsley, P., Black, I., Ando, H., Ishida, H., Kiso, M., etal. (2001) The crystal structure of tetanus toxin HC fragment complexed with a synthetic gt1b analogue suggests cross-linking between ganglioside receptors and the toxin. J Biol Chem 276: 32274-32281.
    • (2001) J Biol Chem , vol.276 , pp. 32274-32281
    • Fotinou, C.1    Emsley, P.2    Black, I.3    Ando, H.4    Ishida, H.5    Kiso, M.6
  • 22
    • 53149135499 scopus 로고    scopus 로고
    • Calcein permeability of liposomes mediated by type A botulinum neurotoxin and its light and heavy chains
    • Fu, F.N., and Singh, B.R. (1999) Calcein permeability of liposomes mediated by type A botulinum neurotoxin and its light and heavy chains. J Protein Chem 18: 701-707.
    • (1999) J Protein Chem , vol.18 , pp. 701-707
    • Fu, F.N.1    Singh, B.R.2
  • 23
    • 0037015327 scopus 로고    scopus 로고
    • Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation
    • Fu, F., Busath, D.D., and Singh, B.R. (2002) Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation. Biophys Chem 99: 17-29.
    • (2002) Biophys Chem , vol.99 , pp. 17-29
    • Fu, F.1    Busath, D.D.2    Singh, B.R.3
  • 24
    • 67649210455 scopus 로고    scopus 로고
    • Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype f
    • Fu, Z., Chen, C., Barbieri, J.T., Kim, J.P., and Baldwin, M.R. (2009) Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype f. Biochemistry 48: 5631-5641.
    • (2009) Biochemistry , vol.48 , pp. 5631-5641
    • Fu, Z.1    Chen, C.2    Barbieri, J.T.3    Kim, J.P.4    Baldwin, M.R.5
  • 25
    • 0027477039 scopus 로고
    • Role of acidic lipids in the translocation and channel activity of colicins A and N in Escherichia coli cells
    • van der Goot, F.G., Didat, N., Pattus, F., Dowhan, W., and Letellier, L. (1993) Role of acidic lipids in the translocation and channel activity of colicins A and N in Escherichia coli cells. Eur J Biochem 213: 217-221.
    • (1993) Eur J Biochem , vol.213 , pp. 217-221
    • van der Goot, F.G.1    Didat, N.2    Pattus, F.3    Dowhan, W.4    Letellier, L.5
  • 26
    • 0347318063 scopus 로고    scopus 로고
    • N-glycosylation is essential for vesicular targeting of synaptotagmin 1
    • Han, W., Rhee, J., Maximov, A., Lao, Y., Mashimo, T., Rosenmund, C., etal. (2004) N-glycosylation is essential for vesicular targeting of synaptotagmin 1. Neuron 41: 85-99.
    • (2004) Neuron , vol.41 , pp. 85-99
    • Han, W.1    Rhee, J.2    Maximov, A.3    Lao, Y.4    Mashimo, T.5    Rosenmund, C.6
  • 27
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes
    • Hoch, D.H., Romero-Mira, M., Ehrlich, B.E., Finkelstein, A., DasGupta, B.R., and Simpson, L.L. (1985) Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc Natl Acad Sci USA 82: 1692-1696.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    DasGupta, B.R.5    Simpson, L.L.6
  • 28
    • 26444482019 scopus 로고    scopus 로고
    • Common binding site for disialyllactose and tri-peptide in c-fragment of tetanus neurotoxin
    • Jayaraman, S., Eswaramoorthy, S., Kumaran, D., and Swaminathan, S. (2005) Common binding site for disialyllactose and tri-peptide in c-fragment of tetanus neurotoxin. Proteins 61: 288-295.
    • (2005) Proteins , vol.61 , pp. 288-295
    • Jayaraman, S.1    Eswaramoorthy, S.2    Kumaran, D.3    Swaminathan, S.4
  • 29
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • Jin, R., Rummel, A., Binz, T., and Brunger, A.T. (2006) Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444: 1092-1095.
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 31
    • 77956591091 scopus 로고    scopus 로고
    • Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA
    • Karalewitz, A.P., Kroken, A.R., Fu, Z., Baldwin, M.R., Kim, J.P., and Barbieri, J.T. (2010) Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA. Biochemistry 49: 8117-8126.
    • (2010) Biochemistry , vol.49 , pp. 8117-8126
    • Karalewitz, A.P.1    Kroken, A.R.2    Fu, Z.3    Baldwin, M.R.4    Kim, J.P.5    Barbieri, J.T.6
  • 32
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • Keller, J.E., Neale, E.A., Oyler, G., and Adler, M. (1999) Persistence of botulinum neurotoxin action in cultured spinal cord cells. FEBS Lett 456: 137-142.
    • (1999) FEBS Lett , vol.456 , pp. 137-142
    • Keller, J.E.1    Neale, E.A.2    Oyler, G.3    Adler, M.4
  • 33
    • 0027136038 scopus 로고
    • Disulfide formation in reduced tetanus toxin by thioredoxin: the pharmacological role of interchain covalent and noncovalent bonds
    • Kistner, A., Sanders, D., and Habermann, E. (1993) Disulfide formation in reduced tetanus toxin by thioredoxin: the pharmacological role of interchain covalent and noncovalent bonds. Toxicon 31: 1423-1434.
    • (1993) Toxicon , vol.31 , pp. 1423-1434
    • Kistner, A.1    Sanders, D.2    Habermann, E.3
  • 34
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova, L.K., and Montal, M. (2003) Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat Struct Biol 10: 13-18.
    • (2003) Nat Struct Biol , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 35
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in clostridium botulinum neurotoxin type E is unique: its implication in faster translocation
    • Kumaran, D., Eswaramoorthy, S., Furey, W., Navaza, J., Sax, M., and Swaminathan, S. (2009) Domain organization in clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J Mol Biol 386: 233-245.
    • (2009) J Mol Biol , vol.386 , pp. 233-245
    • Kumaran, D.1    Eswaramoorthy, S.2    Furey, W.3    Navaza, J.4    Sax, M.5    Swaminathan, S.6
  • 36
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy, D.B., and Stevens, R.C. (1999) Sequence homology and structural analysis of the clostridial neurotoxins. J Mol Biol 291: 1091-1104.
    • (1999) J Mol Biol , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 37
    • 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
  • 38
    • 0032842847 scopus 로고    scopus 로고
    • Functional characterisation of tetanus and botulinum neurotoxins binding domains
    • Lalli, G., Herreros, J., Osborne, S.L., Montecucco, C., Rossetto, O., and Schiavo, G. (1999) Functional characterisation of tetanus and botulinum neurotoxins binding domains. J Cell Sci 112: 2715-2724.
    • (1999) J Cell Sci , vol.112 , pp. 2715-2724
    • Lalli, G.1    Herreros, J.2    Osborne, S.L.3    Montecucco, C.4    Rossetto, O.5    Schiavo, G.6
  • 39
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pka values
    • Li, H., Robertson, A.D., and Jensen, J.H. (2005) Very fast empirical prediction and rationalization of protein pka values. Proteins 61: 704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 40
    • 79551494442 scopus 로고    scopus 로고
    • Embryonic stem cell-derived neurons are a novel, highly sensitive tissue culture platform for botulinum research
    • McNutt, P., Celver, J., Hamilton, T., and Mesngon, M. (2011) Embryonic stem cell-derived neurons are a novel, highly sensitive tissue culture platform for botulinum research. Biochem Biophys Res Commun 405: 85-90.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 85-90
    • McNutt, P.1    Celver, J.2    Hamilton, T.3    Mesngon, M.4
  • 41
    • 33645212684 scopus 로고    scopus 로고
    • The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves
    • Mahrhold, S., Rummel, A., Bigalke, H., Davletov, B., and Binz, T. (2006) The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves. FEBS Lett 580: 2011-2014.
    • (2006) FEBS Lett , vol.580 , pp. 2011-2014
    • Mahrhold, S.1    Rummel, A.2    Bigalke, H.3    Davletov, B.4    Binz, T.5
  • 42
    • 0024599014 scopus 로고
    • Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charge, and transmembrane potential on the kinetics of channel formation
    • Menestrina, G., Forti, S., and Gambale, F. (1989) Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charge, and transmembrane potential on the kinetics of channel formation. Biophys J 55: 393-405.
    • (1989) Biophys J , vol.55 , pp. 393-405
    • Menestrina, G.1    Forti, S.2    Gambale, F.3
  • 43
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenböck, G., De Angelis, D.A., and Rothman, J.E. (1998) Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394: 192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenböck, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 44
    • 68849127717 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel
    • Montal, M. (2009) Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel. Toxicon 54: 565-569.
    • (2009) Toxicon , vol.54 , pp. 565-569
    • Montal, M.1
  • 45
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: a marvel of protein design
    • Montal, M. (2010) Botulinum neurotoxin: a marvel of protein design. Annu Rev Biochem 79: 591-617.
    • (2010) Annu Rev Biochem , vol.79 , pp. 591-617
    • Montal, M.1
  • 46
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco, C. (1986) How do tetanus and botulinum toxins bind to neuronal membranes? Trends biochem sci 11: 314-317.
    • (1986) Trends biochem sci , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 47
    • 18744410709 scopus 로고    scopus 로고
    • Botulinal neurotoxins: revival of an old killer
    • Montecucco, C., and Molgó, J. (2005) Botulinal neurotoxins: revival of an old killer. Curr Opin Pharmacol 5: 274-279.
    • (2005) Curr Opin Pharmacol , vol.5 , pp. 274-279
    • Montecucco, C.1    Molgó, J.2
  • 48
    • 0024506750 scopus 로고
    • Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes
    • Montecucco, C., Schiavo, G., and Dasgupta, B.R. (1989) Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes. Biochem J 259: 47-53.
    • (1989) Biochem J , vol.259 , pp. 47-53
    • Montecucco, C.1    Schiavo, G.2    Dasgupta, B.R.3
  • 49
    • 4644364793 scopus 로고    scopus 로고
    • Presynaptic receptor arrays for clostridial neurotoxins
    • Montecucco, C., Rossetto, O., and Schiavo, G. (2004) Presynaptic receptor arrays for clostridial neurotoxins. Trends Microbiol 12: 442-446.
    • (2004) Trends Microbiol , vol.12 , pp. 442-446
    • Montecucco, C.1    Rossetto, O.2    Schiavo, G.3
  • 50
    • 0029954333 scopus 로고    scopus 로고
    • Mosaic structures of neurotoxins produced from clostridium botulinum types C and D organisms
    • Moriishi, K., Koura, M., Abe, N., Fujii, N., Fujinaga, Y., Inoue, K., etal. (1996) Mosaic structures of neurotoxins produced from clostridium botulinum types C and D organisms. Biochim Biophys Acta 1307: 123-126.
    • (1996) Biochim Biophys Acta , vol.1307 , pp. 123-126
    • Moriishi, K.1    Koura, M.2    Abe, N.3    Fujii, N.4    Fujinaga, Y.5    Inoue, K.6
  • 51
    • 59649101806 scopus 로고    scopus 로고
    • The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
    • Muraro, L., Tosatto, S., Motterlini, L., Rossetto, O., and Montecucco, C. (2009) The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane. Biochem Biophys Res Commun 380: 76-80.
    • (2009) Biochem Biophys Res Commun , vol.380 , pp. 76-80
    • Muraro, L.1    Tosatto, S.2    Motterlini, L.3    Rossetto, O.4    Montecucco, C.5
  • 52
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides gt1b/gd1a
    • Nishiki, T., Tokuyama, Y., Kamata, Y., Nemoto, Y., Yoshida, A., Sato, K., etal. (1996) The high-affinity binding of clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides gt1b/gd1a. FEBS Lett 378: 253-257.
    • (1996) FEBS Lett , vol.378 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sato, K.6
  • 53
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: consistent treatment of internal and surface residues in empirical pka predictions
    • Olsson, M.H.M., Søndergaard, C.R., Rostkowski, M., and Jensen, J.H. (2011) PROPKA3: consistent treatment of internal and surface residues in empirical pka predictions. J Chem Theory Comput 7: 525-537.
    • (2011) J Chem Theory Comput , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 54
    • 79953289881 scopus 로고    scopus 로고
    • Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors
    • Peng, L., Tepp, W.H., Johnson, E.A., and Dong, M. (2011) Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors. PLoS Pathog 7: e1002008.
    • (2011) PLoS Pathog , vol.7
    • Peng, L.1    Tepp, W.H.2    Johnson, E.A.3    Dong, M.4
  • 55
    • 34548283134 scopus 로고    scopus 로고
    • Concerted protonation of key histidines triggers membrane interaction of the diphtheria toxin t domain
    • Perier, A., Chassaing, A., Raffestin, S., Pichard, S., Masella, M., Ménez, A., etal. (2007) Concerted protonation of key histidines triggers membrane interaction of the diphtheria toxin t domain. J Biol Chem 282: 24239-24245.
    • (2007) J Biol Chem , vol.282 , pp. 24239-24245
    • Perier, A.1    Chassaing, A.2    Raffestin, S.3    Pichard, S.4    Masella, M.5    Ménez, A.6
  • 56
    • 2442719960 scopus 로고    scopus 로고
    • Comparison of the pH-induced conformational change of different clostridial neurotoxins
    • Puhar, A., Johnson, E.A., Rossetto, O., and Montecucco, C. (2004) Comparison of the pH-induced conformational change of different clostridial neurotoxins. Biochem Biophys Res Commun 319: 66-71.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 66-71
    • Puhar, A.1    Johnson, E.A.2    Rossetto, O.3    Montecucco, C.4
  • 57
    • 4444338184 scopus 로고    scopus 로고
    • Snake presynaptic neurotoxins with phospholipase A2 activity induce punctate swellings of neurites and exocytosis of synaptic vesicles
    • Rigoni, M., Schiavo, G., Weston, A.E., Caccin, P., Allegrini, F., Pennuto, M., etal. (2004) Snake presynaptic neurotoxins with phospholipase A2 activity induce punctate swellings of neurites and exocytosis of synaptic vesicles. J Cell Sci 117: 3561-3570.
    • (2004) J Cell Sci , vol.117 , pp. 3561-3570
    • Rigoni, M.1    Schiavo, G.2    Weston, A.E.3    Caccin, P.4    Allegrini, F.5    Pennuto, M.6
  • 60
    • 0037459107 scopus 로고    scopus 로고
    • Two carbohydrate binding sites in the H(Cc)-domain of tetanus neurotoxin are required for toxicity
    • Rummel, A., Bade, S., Alves, J., Bigalke, H., and Binz, T. (2003) Two carbohydrate binding sites in the H(Cc)-domain of tetanus neurotoxin are required for toxicity. J Mol Biol 326: 835-847.
    • (2003) J Mol Biol , vol.326 , pp. 835-847
    • Rummel, A.1    Bade, S.2    Alves, J.3    Bigalke, H.4    Binz, T.5
  • 61
    • 1242320307 scopus 로고    scopus 로고
    • The Hcc-domain of botulinum neurotoxins A and B exhibits a singular ganglioside binding site displaying serotype specific carbohydrate interaction
    • Rummel, A., Mahrhold, S., Bigalke, H., and Binz, T. (2004a) The Hcc-domain of botulinum neurotoxins A and B exhibits a singular ganglioside binding site displaying serotype specific carbohydrate interaction. Mol Microbiol 51: 631-643.
    • (2004) Mol Microbiol , vol.51 , pp. 631-643
    • Rummel, A.1    Mahrhold, S.2    Bigalke, H.3    Binz, T.4
  • 62
    • 3142735021 scopus 로고    scopus 로고
    • Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G
    • Rummel, A., Karnath, T., Henke, T., Bigalke, H., and Binz, T. (2004b) Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J Biol Chem 279: 30865-30870.
    • (2004) J Biol Chem , vol.279 , pp. 30865-30870
    • Rummel, A.1    Karnath, T.2    Henke, T.3    Bigalke, H.4    Binz, T.5
  • 63
    • 33846096319 scopus 로고    scopus 로고
    • Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept
    • Rummel, A., Eichner, T., Weil, T., Karnath, T., Gutcaits, A., Mahrhold, S., etal. (2007) Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept. Proc Natl Acad Sci USA 104: 359-364.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 359-364
    • Rummel, A.1    Eichner, T.2    Weil, T.3    Karnath, T.4    Gutcaits, A.5    Mahrhold, S.6
  • 64
    • 69949182315 scopus 로고    scopus 로고
    • Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor
    • Rummel, A., Häfner, K., Mahrhold, S., Darashchonak, N., Holt, M., Jahn, R., etal. (2009) Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor. J Neurochem 110: 1942-1954.
    • (2009) J Neurochem , vol.110 , pp. 1942-1954
    • Rummel, A.1    Häfner, K.2    Mahrhold, S.3    Darashchonak, N.4    Holt, M.5    Jahn, R.6
  • 65
    • 0024564474 scopus 로고
    • Studies on the intoxication pathway of tetanus toxin in the rat pheochromocytoma (PC12) cell line. Binding, internalization, and inhibition of acetylcholine release
    • Sandberg, K., Berry, C.J., and Rogers, T.B. (1989) Studies on the intoxication pathway of tetanus toxin in the rat pheochromocytoma (PC12) cell line. Binding, internalization, and inhibition of acetylcholine release. J Biol Chem 264: 5679-5686.
    • (1989) J Biol Chem , vol.264 , pp. 5679-5686
    • Sandberg, K.1    Berry, C.J.2    Rogers, T.B.3
  • 66
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig, K., and Olsnes, S. (1980) Diphtheria toxin entry into cells is facilitated by low pH. J Cell Biol 87: 828-832.
    • (1980) J Cell Biol , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 67
    • 0033786834 scopus 로고    scopus 로고
    • Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system
    • Sankaranarayanan, S., and Ryan, T.A. (2000) Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system. Nat Cell Biol 2: 197-204.
    • (2000) Nat Cell Biol , vol.2 , pp. 197-204
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 68
    • 0025648954 scopus 로고
    • An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin
    • Schiavo, G., Papini, E., Genna, G., and Montecucco, C. (1990) An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin. Infect Immun 58: 4136-4141.
    • (1990) Infect Immun , vol.58 , pp. 4136-4141
    • Schiavo, G.1    Papini, E.2    Genna, G.3    Montecucco, C.4
  • 69
    • 0025879549 scopus 로고
    • On the role of polysialoglycosphingolipids as tetanus toxin receptors. A study with lipid monolayers
    • Schiavo, G., Demel, R., and Montecucco, C. (1991) On the role of polysialoglycosphingolipids as tetanus toxin receptors. A study with lipid monolayers. Eur J Biochem 199: 705-711.
    • (1991) Eur J Biochem , vol.199 , pp. 705-711
    • Schiavo, G.1    Demel, R.2    Montecucco, C.3
  • 70
    • 0028355349 scopus 로고
    • Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroexocytosis apparatus
    • Schiavo, G., Rossetto, O., Benfenati, F., Poulain, B., and Montecucco, C. (1994) Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroexocytosis apparatus. Ann N Y Acad Sci 710: 65-75.
    • (1994) Ann N Y Acad Sci , vol.710 , pp. 65-75
    • Schiavo, G.1    Rossetto, O.2    Benfenati, F.3    Poulain, B.4    Montecucco, C.5
  • 71
    • 0031840854 scopus 로고    scopus 로고
    • Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes
    • Sheridan, R.E. (1998) Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes. Toxicon 36: 703-717.
    • (1998) Toxicon , vol.36 , pp. 703-717
    • Sheridan, R.E.1
  • 72
    • 67749111568 scopus 로고    scopus 로고
    • TCEP treatment reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells
    • Shi, X., Garcia, G.E., Neill, R.J., and Gordon, R.K. (2009) TCEP treatment reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells. J Cell Biochem 107: 1021-1030.
    • (2009) J Cell Biochem , vol.107 , pp. 1021-1030
    • Shi, X.1    Garcia, G.E.2    Neill, R.J.3    Gordon, R.K.4
  • 73
    • 0029161741 scopus 로고
    • Growth of clostridia and preparation of their neurotoxins
    • Shone, C.C., and Tranter, H.S. (1995) Growth of clostridia and preparation of their neurotoxins. Curr Top Microbiol Immunol 195: 143-160.
    • (1995) Curr Top Microbiol Immunol , vol.195 , pp. 143-160
    • Shone, C.C.1    Tranter, H.S.2
  • 74
    • 0023658427 scopus 로고
    • A 50-kDa fragment from the NH2-terminus of the heavy subunit of clostridium botulinum type A neurotoxin forms channels in lipid vesicles
    • Shone, C.C., Hambleton, P., and Melling, J. (1987) A 50-kDa fragment from the NH2-terminus of the heavy subunit of clostridium botulinum type A neurotoxin forms channels in lipid vesicles. Eur J Biochem 167: 175-180.
    • (1987) Eur J Biochem , vol.167 , pp. 175-180
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 75
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson, L.L., Coffield, J.A., and Bakry, N. (1994) Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J Pharmacol Exp Ther 269: 256-262.
    • (1994) J Pharmacol Exp Ther , vol.269 , pp. 256-262
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 76
    • 1342344554 scopus 로고    scopus 로고
    • The role of the interchain disulfide bond in governing the pharmacological actions of botulinum toxin
    • Simpson, L.L., Maksymowych, A.B., Park, J., and Bora, R.S. (2004) The role of the interchain disulfide bond in governing the pharmacological actions of botulinum toxin. J Pharmacol Exp Ther 308: 857-864.
    • (2004) J Pharmacol Exp Ther , vol.308 , pp. 857-864
    • Simpson, L.L.1    Maksymowych, A.B.2    Park, J.3    Bora, R.S.4
  • 77
    • 34047147339 scopus 로고    scopus 로고
    • Primary cultures of embryonic chicken neurons for sensitive cell-based assay of botulinum neurotoxin: implications for therapeutic discovery
    • Stahl, A.M., Ruthel, G., Torres-Melendez, E., Kenny, T.A., Panchal, R.G., and Bavari, S. (2007) Primary cultures of embryonic chicken neurons for sensitive cell-based assay of botulinum neurotoxin: implications for therapeutic discovery. J Biomol Screen 12: 370-377.
    • (2007) J Biomol Screen , vol.12 , pp. 370-377
    • Stahl, A.M.1    Ruthel, G.2    Torres-Melendez, E.3    Kenny, T.A.4    Panchal, R.G.5    Bavari, S.6
  • 78
    • 77957906825 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner
    • Strotmeier, J., Lee, K., Völker, A.K., Mahrhold, S., Zong, Y., Zeiser, J., etal. (2010) Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner. Biochem J 431: 207-216.
    • (2010) Biochem J , vol.431 , pp. 207-216
    • Strotmeier, J.1    Lee, K.2    Völker, A.K.3    Mahrhold, S.4    Zong, Y.5    Zeiser, J.6
  • 79
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S., and Eswaramoorthy, S. (2000) Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat Struct Biol 7: 617-619.
    • (2000) Nat Struct Biol , vol.7 , pp. 617-619
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 80
    • 0033037446 scopus 로고    scopus 로고
    • Internalization and proteolytic action of botulinum toxins in CNS neurons and astrocytes
    • Verderio, C., Coco, S., Rossetto, O., Montecucco, C., and Matteoli, M. (1999) Internalization and proteolytic action of botulinum toxins in CNS neurons and astrocytes. J Neurochem 73: 372-379.
    • (1999) J Neurochem , vol.73 , pp. 372-379
    • Verderio, C.1    Coco, S.2    Rossetto, O.3    Montecucco, C.4    Matteoli, M.5
  • 81
    • 0027946632 scopus 로고
    • Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture
    • Williamson, L.C., and Neale, E.A. (1994) Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture. J Neurochem 63: 2342-2345.
    • (1994) J Neurochem , vol.63 , pp. 2342-2345
    • Williamson, L.C.1    Neale, E.A.2
  • 82
    • 79251482759 scopus 로고    scopus 로고
    • SV2 mediates entry of tetanus neurotoxin into central neurons
    • Yeh, F.L., Dong, M., Yao, J., Tepp, W.H., Lin, G., Johnson, E.A., etal. (2010) SV2 mediates entry of tetanus neurotoxin into central neurons. PLoS Pathog 6: e1001207.
    • (2010) PLoS Pathog , vol.6
    • Yeh, F.L.1    Dong, M.2    Yao, J.3    Tepp, W.H.4    Lin, G.5    Johnson, E.A.6
  • 83
    • 78650892621 scopus 로고    scopus 로고
    • Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions
    • Zhang, Y., Buchko, G.W., Qin, L., Robinson, H., and Varnum, S.M. (2011) Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions. Biochem Biophys Res Commun 404: 407-412.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 407-412
    • Zhang, Y.1    Buchko, G.W.2    Qin, L.3    Robinson, H.4    Varnum, S.M.5


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