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Volumn 7, Issue , 2017, Pages

Neuronal entry and high neurotoxicity of botulinum neurotoxin A require its N-terminal binding sub-domain

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; BOTULINUM TOXIN A; MEMBRANE PROTEIN; MUTANT PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 85015340807     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep44474     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 81555195210 scopus 로고    scopus 로고
    • Novel therapeutics based on recombinant botulinum neurotoxins to normalize the release of transmitters and pain mediators
    • Dolly, J. O., Wang, J., Zurawski, T. H. & Meng, J. Novel therapeutics based on recombinant botulinum neurotoxins to normalize the release of transmitters and pain mediators. FEBS J 278, 4454-66 (2011).
    • (2011) FEBS J , vol.278 , pp. 4454-4466
    • Dolly, J.O.1    Wang, J.2    Zurawski, T.H.3    Meng, J.4
  • 2
    • 84888183341 scopus 로고    scopus 로고
    • Aesthetic uses of the botulinum toxin
    • Dorizas, A., Krueger, N. & Sadick, N. S. Aesthetic uses of the botulinum toxin. Dermatol Clin 32, 23-36 (2014).
    • (2014) Dermatol Clin , vol.32 , pp. 23-36
    • Dorizas, A.1    Krueger, N.2    Sadick, N.S.3
  • 4
    • 84880941444 scopus 로고    scopus 로고
    • Botulinum toxin A and headache treatment
    • Gady, J. & Ferneini, E. M. Botulinum toxin A and headache treatment. Conn Med 77, 165-6 (2013).
    • (2013) Conn Med , vol.77 , pp. 165-166
    • Gady, J.1    Ferneini, E.M.2
  • 5
    • 0033991246 scopus 로고    scopus 로고
    • Sensitivity of embryonic rat dorsal root ganglia neurons to Clostridium botulinum neurotoxins
    • Welch, M. J., Purkiss, J. R. & Foster, K. A. Sensitivity of embryonic rat dorsal root ganglia neurons to Clostridium botulinum neurotoxins. Toxicon 38, 245-58 (2000).
    • (2000) Toxicon , vol.38 , pp. 245-258
    • Welch, M.J.1    Purkiss, J.R.2    Foster, K.A.3
  • 6
    • 34548567008 scopus 로고    scopus 로고
    • Synaptobrevin i mediates exocytosis of CGRP from sensory neurons and inhibition by botulinum toxins reflects their anti-nociceptive potential
    • Meng, J., Wang, J., Lawrence, G. & Dolly, J. O. Synaptobrevin I mediates exocytosis of CGRP from sensory neurons and inhibition by botulinum toxins reflects their anti-nociceptive potential. J Cell Sci 120, 2864-74 (2007).
    • (2007) J Cell Sci , vol.120 , pp. 2864-2874
    • Meng, J.1    Wang, J.2    Lawrence, G.3    Dolly, J.O.4
  • 7
    • 1642568305 scopus 로고    scopus 로고
    • Regulation of calcitonin gene-related peptide secretion from trigeminal nerve cells by botulinum toxin type A: Implications for migraine therapy
    • discussion 42-3
    • Durham, P. L., Cady, R. & Cady, R. Regulation of calcitonin gene-related peptide secretion from trigeminal nerve cells by botulinum toxin type A: implications for migraine therapy. Headache 44, 35-42, discussion 42-3 (2004).
    • (2004) Headache , vol.44 , pp. 35-42
    • Durham, P.L.1    Cady, R.2    Cady, R.3
  • 8
    • 84959018159 scopus 로고    scopus 로고
    • TNFalpha induces co-trafficking of TRPV1/TRPA1 in VAMP1-containing vesicles to the plasmalemma via Munc18-1/syntaxin1/SNAP-25 mediated fusion
    • 21226
    • Meng, J., Wang, J., Steinhoff, M. & Dolly, J. O. TNFalpha induces co-trafficking of TRPV1/TRPA1 in VAMP1-containing vesicles to the plasmalemma via Munc18-1/syntaxin1/SNAP-25 mediated fusion. Sci Rep 6, 21226, 1-15 (2016).
    • (2016) Sci Rep , vol.6 , pp. 1-15
    • Meng, J.1    Wang, J.2    Steinhoff, M.3    Dolly, J.O.4
  • 9
    • 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. & Stevens, R. C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat Struct Biol 5, 898-902 (1998).
    • (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
  • 10
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in Clostridium botulinum neurotoxin type e is unique: Its implication in faster translocation
    • Kumaran, D. et al. Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J Mol Biol 386, 233-45 (2009).
    • (2009) J Mol Biol , vol.386 , pp. 233-245
    • Kumaran, D.1
  • 11
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S. & Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat Struct Biol 7, 693-9 (2000).
    • (2000) Nat Struct Biol , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 12
    • 0021243873 scopus 로고
    • Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization
    • Dolly, J. O., Black, J., Williams, R. S. & Melling, J. Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization. Nature 307, 457-60 (1984).
    • (1984) Nature , vol.307 , pp. 457-460
    • Dolly, J.O.1    Black, J.2    Williams, R.S.3    Melling, J.4
  • 13
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • Jin, R., Rummel, A., Binz, T. & Brunger, A. T. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444, 1092-5 (2006).
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 14
    • 33845885528 scopus 로고    scopus 로고
    • Structural basis of cell surface receptor recognition by botulinum neurotoxin B
    • Chai, Q. et al. Structural basis of cell surface receptor recognition by botulinum neurotoxin B. Nature 444, 1096-100 (2006).
    • (2006) Nature , vol.444 , pp. 1096-1100
    • Chai, Q.1
  • 15
    • 0022556314 scopus 로고
    • Interaction of 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiographic localization and quantitation of distinct membrane acceptors for types A and B on motor nerves
    • Black, J. D. & Dolly, J. O. Interaction of 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiographic localization and quantitation of distinct membrane acceptors for types A and B on motor nerves. J Cell Biol 103, 521-34 (1986).
    • (1986) J Cell Biol , vol.103 , pp. 521-534
    • Black, J.D.1    Dolly, J.O.2
  • 16
    • 84881141444 scopus 로고    scopus 로고
    • Molecular components required for resting and stimulated endocytosis of botulinum neurotoxins by glutamatergic and peptidergic neurons
    • Meng, J., Wang, J., Lawrence, G. W. & Dolly, J. O. Molecular components required for resting and stimulated endocytosis of botulinum neurotoxins by glutamatergic and peptidergic neurons. FASEB J 27, 3167-80 (2013).
    • (2013) FASEB J , vol.27 , pp. 3167-3180
    • Meng, J.1    Wang, J.2    Lawrence, G.W.3    Dolly, J.O.4
  • 17
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: A marvel of protein design
    • Montal, M. Botulinum neurotoxin: a marvel of protein design. Annu Rev Biochem 79, 591-617 (2010).
    • (2010) Annu Rev Biochem , vol.79 , pp. 591-617
    • Montal, M.1
  • 18
    • 84907398838 scopus 로고    scopus 로고
    • Thioredoxin and its reductase are present on synaptic vesicles, and their inhibition prevents the paralysis induced by botulinum neurotoxins
    • Pirazzini, M. et al. Thioredoxin and its reductase are present on synaptic vesicles, and their inhibition prevents the paralysis induced by botulinum neurotoxins. Cell Rep 8, 1870-8 (2014).
    • (2014) Cell Rep , vol.8 , pp. 1870-1878
    • Pirazzini, M.1
  • 19
    • 79953184288 scopus 로고    scopus 로고
    • A dileucine in the protease of botulinum toxin A underlies its long-lived neuroparalysis: Transfer of longevity to a novel potential therapeutic
    • Wang, J. et al. A dileucine in the protease of botulinum toxin A underlies its long-lived neuroparalysis: transfer of longevity to a novel potential therapeutic. J Biol Chem 286, 6375-85 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 6375-6385
    • Wang, J.1
  • 20
    • 84878505471 scopus 로고    scopus 로고
    • Identification of fibroblast growth factor receptor 3 (FGFR3) as a protein receptor for botulinum neurotoxin serotype A (BoNT/A)
    • Jacky, B. P. et al. Identification of fibroblast growth factor receptor 3 (FGFR3) as a protein receptor for botulinum neurotoxin serotype A (BoNT/A). PLoS Pathog 9, e1003369 (2013).
    • (2013) PLoS Pathog , vol.9 , pp. e1003369
    • Jacky, B.P.1
  • 21
    • 80052994116 scopus 로고    scopus 로고
    • Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly
    • Sun, S. et al. Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly. Cell Host Microbe 10, 237-47 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 237-247
    • Sun, S.1
  • 22
    • 84892372004 scopus 로고    scopus 로고
    • Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
    • Benoit, R. M. et al. Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A. Nature 505, 108-11 (2014).
    • (2014) Nature , vol.505 , pp. 108-111
    • Benoit, R.M.1
  • 23
    • 84977603945 scopus 로고    scopus 로고
    • N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A
    • Yao, G. et al. N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Nat Struct Mol Biol (2016).
    • (2016) Nat Struct Mol Biol
    • Yao, G.1
  • 24
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy, D. B. & Stevens, R. C. Sequence homology and structural analysis of the clostridial neurotoxins. J Mol Biol 291, 1091-104 (1999).
    • (1999) J Mol Biol , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 25
    • 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. & Montecucco, C. 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).
    • (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
  • 26
    • 84878530224 scopus 로고    scopus 로고
    • Structural insights into the functional role of the Hcn sub-domain of the receptor-binding domain of the botulinum neurotoxin mosaic serotype C/D
    • Zhang, Y. et al. Structural insights into the functional role of the Hcn sub-domain of the receptor-binding domain of the botulinum neurotoxin mosaic serotype C/D. Biochimie 95, 1379-85 (2013).
    • (2013) Biochimie , vol.95 , pp. 1379-1385
    • Zhang, Y.1
  • 27
    • 12144291021 scopus 로고    scopus 로고
    • Plasma membrane localization signals in the light chain of botulinum neurotoxin
    • Fernandez-Salas, E. et al. Plasma membrane localization signals in the light chain of botulinum neurotoxin. Proc Natl Acad Sci USA 101, 3208-13 (2004).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3208-3213
    • Fernandez-Salas, E.1
  • 28
    • 47749084648 scopus 로고    scopus 로고
    • Novel chimeras of botulinum neurotoxins A and e unveil contributions from the binding, translocation, and protease domains to their functional characteristics
    • Wang, J. et al. Novel chimeras of botulinum neurotoxins A and E unveil contributions from the binding, translocation, and protease domains to their functional characteristics. J Biol Chem 283, 16993-7002 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 16993-17002
    • Wang, J.1
  • 29
    • 0034797114 scopus 로고    scopus 로고
    • A comparison of the safety margins of botulinum neurotoxin serotypes A, B, and F in mice
    • Aoki, K. R. A comparison of the safety margins of botulinum neurotoxin serotypes A, B, and F in mice. Toxicon 39, 1815-20 (2001).
    • (2001) Toxicon , vol.39 , pp. 1815-1820
    • Aoki, K.R.1
  • 30
    • 33646248918 scopus 로고    scopus 로고
    • SV2 is the protein receptor for botulinum neurotoxin A
    • Dong, M. et al. SV2 is the protein receptor for botulinum neurotoxin A. Science 312, 592-6 (2006).
    • (2006) Science , vol.312 , pp. 592-596
    • Dong, M.1
  • 31
    • 58549094719 scopus 로고    scopus 로고
    • Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin e into neurons
    • Dong, M. et al. Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons. Mol Biol Cell 19, 5226-37 (2008).
    • (2008) Mol Biol Cell , vol.19 , pp. 5226-5237
    • Dong, M.1
  • 32
    • 65549142642 scopus 로고    scopus 로고
    • Activation of TRPV1 mediates calcitonin gene-related peptide release, which excites trigeminal sensory neurons and is attenuated by a retargeted botulinum toxin with anti-nociceptive potential
    • Meng, J. et al. Activation of TRPV1 mediates calcitonin gene-related peptide release, which excites trigeminal sensory neurons and is attenuated by a retargeted botulinum toxin with anti-nociceptive potential. J Neurosci 29, 4981-92 (2009).
    • (2009) J Neurosci , vol.29 , pp. 4981-4992
    • Meng, J.1
  • 33
    • 0020621268 scopus 로고
    • Radioiodination of botulinum neurotoxin type A with retention of biological activity and its binding to brain synaptosomes
    • Williams, R. S., Tse, C. K., Dolly, J. O., Hambleton, P. & Melling, J. Radioiodination of botulinum neurotoxin type A with retention of biological activity and its binding to brain synaptosomes. Eur J Biochem 131, 437-45 (1983).
    • (1983) Eur J Biochem , vol.131 , pp. 437-445
    • Williams, R.S.1    Tse, C.K.2    Dolly, J.O.3    Hambleton, P.4    Melling, J.5
  • 34
    • 0033800350 scopus 로고    scopus 로고
    • A conjugate composed of nerve growth factor coupled to a non-toxic derivative of Clostridium botulinum neurotoxin type A can inhibit neurotransmitter release in vitro
    • Chaddock, J. A. et al. A conjugate composed of nerve growth factor coupled to a non-toxic derivative of Clostridium botulinum neurotoxin type A can inhibit neurotransmitter release in vitro. Growth Factors 18, 147-55 (2000).
    • (2000) Growth Factors , vol.18 , pp. 147-155
    • Chaddock, J.A.1
  • 35
    • 0037144403 scopus 로고    scopus 로고
    • Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin
    • Duggan, M. J. et al. Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin. J Biol Chem 277, 34846-52 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 34846-34852
    • Duggan, M.J.1
  • 36
    • 84879939934 scopus 로고    scopus 로고
    • Stapling of the botulinum type A protease to growth factors and neuropeptides allows selective targeting of neuroendocrine cells
    • Arsenault, J. et al. Stapling of the botulinum type A protease to growth factors and neuropeptides allows selective targeting of neuroendocrine cells. J Neurochem 126, 223-33 (2013).
    • (2013) J Neurochem , vol.126 , pp. 223-233
    • Arsenault, J.1
  • 38
    • 84865975652 scopus 로고    scopus 로고
    • A botulinum toxin-derived targeted secretion inhibitor downregulates the GH/IGF1 axis
    • Somm, E. et al. A botulinum toxin-derived targeted secretion inhibitor downregulates the GH/IGF1 axis. J Clin Invest 122, 3295-306 (2012).
    • (2012) J Clin Invest , vol.122 , pp. 3295-3306
    • Somm, E.1
  • 39
    • 0036044484 scopus 로고    scopus 로고
    • Clinical features of antibody-induced complete secondary failure of botulinum toxin therapy
    • Dressler, D. Clinical features of antibody-induced complete secondary failure of botulinum toxin therapy. Eur Neurol 48, 26-9 (2002).
    • (2002) Eur Neurol , vol.48 , pp. 26-29
    • Dressler, D.1
  • 41
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41, 207-34 (2005).
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1


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