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Volumn 287, Issue 3, 2012, Pages 1657-1661

Beltless translocation domain of botulinum neurotoxin A embodies a minimum ion-conductive channel

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM NEUROTOXINS; CATALYTIC DOMAINS; CAUSATIVE AGENTS; CHANNEL FORMATION; CONFORMATIONAL CHANGE; HEAVY CHAIN; ION CONDUCTION; LIGHT CHAIN; PH GRADIENTS; RECEPTOR-BINDING DOMAINS; RECEPTOR-MEDIATED ENDOCYTOSIS; SECONDARY STRUCTURES; STRUCTURAL REARRANGEMENT; TRANSMEMBRANES;

EID: 84855837031     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C111.319400     Document Type: Article
Times cited : (27)

References (45)
  • 1
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • DOI 10.1038/2338
    • 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 (Pubitemid 28467413)
    • (1998) Nature Structural Biology , vol.5 , Issue.10 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    DasGupta, B.R.4    Stevens, R.C.5
  • 3
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • DOI 10.1038/78005
    • Swaminathan, S., and Eswaramoorthy, S. (2000) Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7, 693-699 (Pubitemid 30636683)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 4
    • 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
  • 5
    • 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
  • 6
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the major steps in botulinum toxin action
    • Simpson, L. L. (2004) Identification of the major steps in botulinum toxin action. Annu. Rev. Pharmacol. Toxicol. 44, 167-193
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 167-193
    • Simpson, L.L.1
  • 8
    • 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. J., 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.J.4    Baldwin, M.R.5
  • 9
    • 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
  • 10
    • 0141641129 scopus 로고    scopus 로고
    • Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells
    • DOI 10.1083/jcb.200305098
    • Dong, M., Richards, D. A., Goodnough, M. C., Tepp, W. H., Johnson, E. A., and Chapman, E. R. (2003) Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells. J. Cell Biol. 162, 1293-1303 (Pubitemid 37210885)
    • (2003) Journal of Cell Biology , vol.162 , Issue.7 , pp. 1293-1303
    • Dong, M.1    Richards, D.A.2    Goodnough, M.C.3    Tepp, W.H.4    Johnson, E.A.5    Chapman, E.R.6
  • 13
    • 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 (Pubitemid 26015975)
    • (1995) Quarterly Reviews of Biophysics , vol.28 , Issue.4 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 14
    • 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 utilizing the three isoforms of SV2 as second receptor
    • Rummel, A., Häfner, K., Mahrhold, S., Darashchonak, N., Holt, M., Jahn, R., Beermann, S., Karnath, T., Bigalke, H., and Binz, T. (2009) Botulinum neurotoxins C, E, and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilizing 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    Beermann, S.7    Karnath, T.8    Bigalke, H.9    Binz, T.10
  • 15
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • DOI 10.1038/nsb879
    • 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 (Pubitemid 36034171)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 16
  • 17
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • DOI 10.1038/26412
    • Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Åresolution. Nature 395, 347-353 (Pubitemid 28450677)
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 19
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for butulinum neurotoxin serotype A
    • DOI 10.1038/nature03123
    • Breidenbach, M. A., and Brunger, A. T. (2004) Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 432, 925-929 (Pubitemid 40037157)
    • (2004) Nature , vol.432 , Issue.7019 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 20
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • DOI 10.1111/j.1365-2958.1994.tb00396.x
    • Montecucco, C., and Schiavo, G. (1994) Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 13, 1-8 (Pubitemid 24220537)
    • (1994) Molecular Microbiology , vol.13 , Issue.1 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 22
    • 80054105849 scopus 로고    scopus 로고
    • Double anchorage to the membrane and intact interchain disulfide bond are required for the low pH-induced entry of tetanus and botulinum neurotoxins into neurons
    • Pirazzini, M., Rossetto, O., Bolognese, P., Shone, C. C., and Montecucco, C. (2011) Double anchorage to the membrane and intact interchain disulfide bond are required for the low pH-induced entry of tetanus and botulinum neurotoxins into neurons. Cell Microbiol. 13, 1731-1743
    • (2011) Cell Microbiol. , vol.13 , pp. 1731-1743
    • Pirazzini, M.1    Rossetto, O.2    Bolognese, P.3    Shone, C.C.4    Montecucco, C.5
  • 23
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J. A., and Collier, R. J. (2007) Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 24
    • 55549106809 scopus 로고    scopus 로고
    • Membrane interaction of botulinum neurotoxinAtranslocation (T) domain: The belt region is a regulatory loop for membrane interaction
    • Galloux, M., Vitrac, H., Montagner, C., Raffestin, S., Popoff, M. R., Chenal, A., Forge, V., and Gillet, D. (2008) Membrane interaction of botulinum neurotoxinAtranslocation (T) domain: the belt region is a regulatory loop for membrane interaction. J. Biol. Chem. 283, 27668-27676
    • (2008) J. Biol. Chem. , vol.283 , pp. 27668-27676
    • Galloux, M.1    Vitrac, H.2    Montagner, C.3    Raffestin, S.4    Popoff, M.R.5    Chenal, A.6    Forge, V.7    Gillet, D.8
  • 25
    • 78650214996 scopus 로고    scopus 로고
    • Low pH-induced pore formation by the T domain of botulinum toxin type A is dependent upon NaCl concentration
    • Lai, B., Agarwal, R., Nelson, L. D., Swaminathan, S., and London, E. (2010) Low pH-induced pore formation by the T domain of botulinum toxin type A is dependent upon NaCl concentration. J. Membr. Biol. 236, 191-201
    • (2010) J. Membr. Biol. , vol.236 , pp. 191-201
    • Lai, B.1    Agarwal, R.2    Nelson, L.D.3    Swaminathan, S.4    London, E.5
  • 26
    • 79960693436 scopus 로고    scopus 로고
    • Studies of the mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes
    • Mushrush, D. J., Koteiche, H. A., Sammons, M. A., Link, A. J., McHaourab, H. S., and Lacy, D. B. (2011) Studies of the mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes. J. Biol. Chem. 286, 27011-27018
    • (2011) J. Biol. Chem. , vol.286 , pp. 27011-27018
    • Mushrush, D.J.1    Koteiche, H.A.2    Sammons, M.A.3    Link, A.J.4    McHaourab, H.S.5    Lacy, D.B.6
  • 27
    • 67650283952 scopus 로고    scopus 로고
    • Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F
    • Agarwal, R., Schmidt, J. J., Stafford, R. G., and Swaminathan, S. (2009) Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F. Nat. Struct. Mol. Biol. 16, 789-794
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 789-794
    • Agarwal, R.1    Schmidt, J.J.2    Stafford, R.G.3    Swaminathan, S.4
  • 28
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • DOI 10.1371/journal.ppat.0020113
    • Brunger, A. T., Breidenbach, M. A., Jin, R., Fischer, A., Santos, J. S., and Montal, M. (2007) Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog. 3, 1191-1194 (Pubitemid 47510272)
    • (2007) PLoS Pathogens , vol.3 , Issue.9 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 29
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • DOI 10.1006/jmbi.1999.2945
    • Lacy, D. B., and Stevens, R. C. (1999) Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 291, 1091-1104 (Pubitemid 29423772)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.5 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 30
    • 0029047219 scopus 로고
    • Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain
    • Lebeda, F. J., and Olson, M. A. (1995) Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain. Toxicon 33, 559-567
    • (1995) Toxicon , vol.33 , pp. 559-567
    • Lebeda, F.J.1    Olson, M.A.2
  • 31
    • 0026448842 scopus 로고
    • Identification of an ion channel-forming motif in the primary structure of tetanus and botulinum neurotoxins
    • Montal, M. S., Blewitt, R., Tomich, J. M., and Montal, M. (1992) Identification of an ion channel-forming motif in the primary structure of tetanus and botulinum neurotoxins. FEBS Lett. 313, 12-18
    • (1992) FEBS Lett. , vol.313 , pp. 12-18
    • Montal, M.S.1    Blewitt, R.2    Tomich, J.M.3    Montal, M.4
  • 32
    • 0029115961 scopus 로고
    • Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A
    • Oblatt-Montal, M., Yamazaki, M., Nelson, R., and Montal, M. (1995) Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A. Protein Sci. 4, 1490-1497
    • (1995) Protein Sci. , vol.4 , pp. 1490-1497
    • Oblatt-Montal, M.1    Yamazaki, M.2    Nelson, R.3    Montal, M.4
  • 33
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • DOI 10.1074/jbc.M703619200
    • Fischer, A., and Montal, M. (2007) Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes. J. Biol. Chem. 282, 29604-29611 (Pubitemid 350043363)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 35
    • 0032972388 scopus 로고    scopus 로고
    • Chloride channels activated by hypotonicity in N2A neuroblastoma cell line
    • DOI 10.1007/s002210050614
    • Carpaneto, A., Accardi, A., Pisciotta, M., and Gambale, F. (1999) Chloride channels activated by hypotonicity in N2A neuroblastoma cell line. Exp. Brain Res. 124, 193-199 (Pubitemid 29134419)
    • (1999) Experimental Brain Research , vol.124 , Issue.2 , pp. 193-199
    • Carpaneto, A.1    Accardi, A.2    Pisciotta, M.3    Gambale, F.4
  • 37
    • 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
  • 38
    • 10644230055 scopus 로고    scopus 로고
    • Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
    • DOI 10.1111/j.1471-4159.2004.02844.x
    • Bade, S., Rummel, A., Reisinger, C., Karnath, T., Ahnert-Hilger, G., Bigalke, H., and Binz, T. (2004) Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurons via unfolded translocation intermediates. J. Neurochem. 91, 1461-1472 (Pubitemid 39658572)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.6 , pp. 1461-1472
    • Bade, S.1    Rummel, A.2    Reisinger, C.3    Karnath, T.4    Ahnert-Hilger, G.5    Bigalke, H.6    Binz, T.7
  • 39
    • 64549164100 scopus 로고    scopus 로고
    • Evidence for a proton-protein symport mechanism in the anthrax toxin channel
    • Basilio, D., Juris, S. J., Collier, R. J., and Finkelstein, A. (2009) Evidence for a proton-protein symport mechanism in the anthrax toxin channel. J. Gen. Physiol. 133, 307-314
    • (2009) J. Gen. Physiol. , vol.133 , pp. 307-314
    • Basilio, D.1    Juris, S.J.2    Collier, R.J.3    Finkelstein, A.4
  • 40
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • DOI 10.1016/j.jmb.2005.11.030, PII S0022283605014166
    • Krantz, B. A., Finkelstein, A., and Collier, R. J. (2006) Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J. Mol. Biol. 355, 968-979 (Pubitemid 43012140)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 41
    • 18144441577 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin: Low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells
    • DOI 10.1074/jbc.M305849200
    • Blöcker, D., Pohlmann, K., Haug, G., Bachmeyer, C., Benz, R., Aktories, K., and Barth, H. (2003) Clostridium botulinum C2 toxin: low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells. J. Biol. Chem. 278, 37360-37367 (Pubitemid 37175254)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37360-37367
    • Blocker, D.1    Pohlmann, K.2    Haug, G.3    Bachmeyer, C.4    Benz, R.5    Aktories, K.6    Barth, H.7
  • 42
    • 0346333312 scopus 로고    scopus 로고
    • Cellular Uptake of Clostridium botulinum C2 Toxin: Membrane Translocation of a Fusion Toxin Requires Unfolding of Its Dihydrofolate Reductase Domain
    • DOI 10.1021/bi0354278
    • Haug, G., Wilde, C., Leemhuis, J., Meyer, D. K., Aktories, K., and Barth, H. (2003) Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain. Biochemistry 42, 15284-15291 (Pubitemid 38031727)
    • (2003) Biochemistry , vol.42 , Issue.51 , pp. 15284-15291
    • Haug, G.1    Wilde, C.2    Leemhuis, J.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 43
    • 0033532355 scopus 로고    scopus 로고
    • Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
    • DOI 10.1126/science.284.5416.955
    • Ren, J., Kachel, K., Kim, H., Malenbaum, S. E., Collier, R. J., and London, E. (1999) Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation. Science 284, 955-957 (Pubitemid 29288432)
    • (1999) Science , vol.284 , Issue.5416 , pp. 955-957
    • Ren, J.1    Kachel, K.2    Kim, H.3    Malenbaum, S.E.4    Collier, R.J.5    London, E.6
  • 44
    • 55249092457 scopus 로고    scopus 로고
    • Formation of an unfolding intermediate state of soluble chloride intracellular channel protein CLIC1 at acidic pH
    • Fanucchi, S., Adamson, R. J., and Dirr, H. W. (2008) Formation of an unfolding intermediate state of soluble chloride intracellular channel protein CLIC1 at acidic pH. Biochemistry 47, 11674-11681
    • (2008) Biochemistry , vol.47 , pp. 11674-11681
    • Fanucchi, S.1    Adamson, R.J.2    Dirr, H.W.3
  • 45
    • 84855839513 scopus 로고    scopus 로고
    • YASARA Biosciences, Vienna, Austria
    • Krieger, E. (2011) YASARA, YASARA Biosciences, Vienna, Austria
    • (2011) YASARA
    • Krieger, E.1


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