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Volumn 74, Issue 3, 2000, Pages 1279-1289

Recombinant expression of α-bungarotoxin in Pichia pastoris facilitates identification of mutant toxins engineered to recognize neuronal nicotinic acetylcholine receptors

Author keywords

Nicotinic acetylcholine receptors; Pharmacology; Pichia pastoris; Bungarotoxin

Indexed keywords

ALPHA BUNGAROTOXIN; NEUROTOXIN; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT;

EID: 0033968089     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.741279.x     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 0030696883 scopus 로고    scopus 로고
    • Nonidentity of the α-neurotoxin binding sites on the nicotinic acetylcholine receptor revealed by modification in α-neurotoxin and receptor structures
    • Ackermann E. J. and Taylor P. (1997) Nonidentity of the α-neurotoxin binding sites on the nicotinic acetylcholine receptor revealed by modification in α-neurotoxin and receptor structures. Biochemistry 36, 12836-12844.
    • (1997) Biochemistry , vol.36 , pp. 12836-12844
    • Ackermann, E.J.1    Taylor, P.2
  • 2
    • 0032079868 scopus 로고    scopus 로고
    • Identification of pairwise interactions in the α-neurotoxin-nicotinic acetylcholine receptor complex through double mutant cycles
    • Ackermann E. J., Ang E. T.-H., Kanter J. R., Tsigelny I., and Taylor P. (1998) Identification of pairwise interactions in the α-neurotoxin-nicotinic acetylcholine receptor complex through double mutant cycles. J. Biol. Chem. 273, 10958-10964.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10958-10964
    • Ackermann, E.J.1    Ang, E.T.-H.2    Kanter, J.R.3    Tsigelny, I.4    Taylor, P.5
  • 4
    • 85013526554 scopus 로고
    • Electrophysiology of neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes following injection of genes or cDNAs
    • Bertrand D., Cooper E., Valera S., Rungger D., and Ballivet M. (1991) Electrophysiology of neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes following injection of genes or cDNAs. Methods Neurosci. 4, 174-193.
    • (1991) Methods Neurosci. , vol.4 , pp. 174-193
    • Bertrand, D.1    Cooper, E.2    Valera, S.3    Rungger, D.4    Ballivet, M.5
  • 5
    • 0033596746 scopus 로고    scopus 로고
    • X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32
    • Bewley M. C., Tam B. M., Grewal J., He S., Shewry S., Murphy M. E., Mason A. B., Woodworth R. C., Baker E. N., and MacGillivray R. T. (1999) X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry 38, 2535-2541.
    • (1999) Biochemistry , vol.38 , pp. 2535-2541
    • Bewley, M.C.1    Tam, B.M.2    Grewal, J.3    He, S.4    Shewry, S.5    Murphy, M.E.6    Mason, A.B.7    Woodworth, R.C.8    Baker, E.N.9    MacGillivray, R.T.10
  • 6
    • 0030980834 scopus 로고    scopus 로고
    • The molecular biology of neuronal nicotinic acetylcholine receptors
    • Boyd R. T. (1997) The molecular biology of neuronal nicotinic acetylcholine receptors. Crit. Rev. Toxicol. 27, 299-318.
    • (1997) Crit. Rev. Toxicol. , vol.27 , pp. 299-318
    • Boyd, R.T.1
  • 8
    • 0014877189 scopus 로고
    • Use of snake venom toxin to characterize the cholinergic receptor protein
    • Changeux J.-P., Kasai M., and Lee C.-Y. (1970) Use of snake venom toxin to characterize the cholinergic receptor protein. Proc. Natl. Acad. Sci. USA 67, 1241-1247.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 1241-1247
    • Changeux, J.-P.1    Kasai, M.2    Lee, C.-Y.3
  • 9
    • 0002117263 scopus 로고
    • Neurotoxins acting on acetylcholine receptors
    • (Harvey A., ed), Academic Press, San Diego
    • Chiappinelli V. A. (1995) Neurotoxins acting on acetylcholine receptors, in Natural and Synthetic Neurotoxins (Harvey A., ed), pp. 65-128. Academic Press, San Diego.
    • (1995) Natural and Synthetic Neurotoxins , pp. 65-128
    • Chiappinelli, V.A.1
  • 10
    • 0030293804 scopus 로고    scopus 로고
    • Binding of native κ-bungarotoxin and site-directed mutants to nicotinic acetylcholine receptors
    • Chiappinelli V. A., Weaver W. R., McLane K. E., Conti-Fine B. M., Fiordalisi J. J., and Grant G. A. (1996) Binding of native κ-bungarotoxin and site-directed mutants to nicotinic acetylcholine receptors. Toxicon 34, 1243-1256.
    • (1996) Toxicon , vol.34 , pp. 1243-1256
    • Chiappinelli, V.A.1    Weaver, W.R.2    McLane, K.E.3    Conti-Fine, B.M.4    Fiordalisi, J.J.5    Grant, G.A.6
  • 11
    • 0029953564 scopus 로고    scopus 로고
    • Molecular and cellular aspects of nicotine abuse
    • Dani J. A. and Heinemann S. (1996) Molecular and cellular aspects of nicotine abuse. Neuron 16, 905-908.
    • (1996) Neuron , vol.16 , pp. 905-908
    • Dani, J.A.1    Heinemann, S.2
  • 13
    • 0024784407 scopus 로고
    • Direct expression in E. coli of a functionally active protein A-snake toxin fusion protein
    • Ducancel F., Boulain J. C., Tremeau O., and Ménez A. (1989) Direct expression in E. coli of a functionally active protein A-snake toxin fusion protein. Protein Eng. 3, 139-143.
    • (1989) Protein Eng. , vol.3 , pp. 139-143
    • Ducancel, F.1    Boulain, J.C.2    Tremeau, O.3    Ménez, A.4
  • 14
    • 0002687075 scopus 로고
    • Structure-function relationships of postsynaptic neurotoxins from snake venoms
    • (Harvey A. L., ed), Pergamon Press, New York
    • Endo T. and Tamiya N. (1991) Structure-function relationships of postsynaptic neurotoxins from snake venoms, in Snake Toxins (Harvey A. L., ed), pp. 165-222, Pergamon Press, New York.
    • (1991) Snake Toxins , pp. 165-222
    • Endo, T.1    Tamiya, N.2
  • 15
    • 0027265201 scopus 로고
    • Evidence for a fast-exchange conformational process in α-bungarotoxin
    • Fiordalisi J. J. and Grant G. A. (1993) Evidence for a fast-exchange conformational process in α-bungarotoxin. Toxicon 31, 767-775.
    • (1993) Toxicon , vol.31 , pp. 767-775
    • Fiordalisi, J.J.1    Grant, G.A.2
  • 16
    • 0028179132 scopus 로고
    • Site-directed mutagenesis of κ-bungarotoxin: Implications for neuronal receptor specificity
    • Fiordalisi J. J., Al-Rabiee R., Chiappinelli V. A., and Grant G. A. (1994) Site-directed mutagenesis of κ-bungarotoxin: implications for neuronal receptor specificity. Biochemistry 33, 3872-3877.
    • (1994) Biochemistry , vol.33 , pp. 3872-3877
    • Fiordalisi, J.J.1    Al-Rabiee, R.2    Chiappinelli, V.A.3    Grant, G.A.4
  • 17
    • 0030026194 scopus 로고    scopus 로고
    • Facile production of native-like κ-bungarotoxin in yeast: An enhanced system for the production of a neuronal nicotinic acetylcholine receptor probe
    • Fiordalisi J. J., James P. L., Zhang Y., and Grant G. A. (1996) Facile production of native-like κ-bungarotoxin in yeast: an enhanced system for the production of a neuronal nicotinic acetylcholine receptor probe. Toxicon 34, 213-224.
    • (1996) Toxicon , vol.34 , pp. 213-224
    • Fiordalisi, J.J.1    James, P.L.2    Zhang, Y.3    Grant, G.A.4
  • 18
    • 0032168390 scopus 로고    scopus 로고
    • Differential roles for disulfide bonds in the structural integrity and biological activity of κ-bungarotoxin, a nicotinic acetylcholine receptor antagonist
    • Grant G. A., Luetje C. W., Summers R., and Xu X. L. (1998) Differential roles for disulfide bonds in the structural integrity and biological activity of κ-bungarotoxin, a nicotinic acetylcholine receptor antagonist. Biochemistry 37, 12166-12171.
    • (1998) Biochemistry , vol.37 , pp. 12166-12171
    • Grant, G.A.1    Luetje, C.W.2    Summers, R.3    Xu, X.L.4
  • 21
    • 0033543759 scopus 로고    scopus 로고
    • Chimeric analysis of a neuronal nicotinic acetylcholine receptor reveals amino acids conferring sensitivity to α-bungarotoxin
    • Levandoski M. M., Lin Y., Moise L., McLaughlin J., Cooper E., and Hawrot E. (1999) Chimeric analysis of a neuronal nicotinic acetylcholine receptor reveals amino acids conferring sensitivity to α-bungarotoxin. J. Biol. Chem. 274, 26113-26119.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26113-26119
    • Levandoski, M.M.1    Lin, Y.2    Moise, L.3    McLaughlin, J.4    Cooper, E.5    Hawrot, E.6
  • 23
    • 0022943266 scopus 로고
    • The crystal structure of α-bungarotoxin at 2.5 Å resolution: Relation to solution structure and binding to acetylcholine receptor
    • Love R. A. and Stroud R. M. (1986) The crystal structure of α-bungarotoxin at 2.5 Å resolution: relation to solution structure and binding to acetylcholine receptor. Protein Eng. 1, 37-46.
    • (1986) Protein Eng. , vol.1 , pp. 37-46
    • Love, R.A.1    Stroud, R.M.2
  • 24
    • 0032213318 scopus 로고    scopus 로고
    • α-Conotoxin AuIB selectively blocks α3β4 nicotinic acetylcholine receptors and nicotine-evoked norepinephrine release
    • Luo S., Kulak J. M., Cartier G. E., Jacobsen R. B., Yoshikami D., Olivera B. M., and McIntosh J. M. (1998) α-Conotoxin AuIB selectively blocks α3β4 nicotinic acetylcholine receptors and nicotine-evoked norepinephrine release. J. Neurosci. 18, 8571-8579.
    • (1998) J. Neurosci. , vol.18 , pp. 8571-8579
    • Luo, S.1    Kulak, J.M.2    Cartier, G.E.3    Jacobsen, R.B.4    Yoshikami, D.5    Olivera, B.M.6    McIntosh, J.M.7
  • 25
    • 0031761951 scopus 로고    scopus 로고
    • NMR analysis of the N-terminal SRCR domain of human CD5: Engineering of a glycoprotein for superior characteristics in NMR experiments
    • McAlister M. S., Davis B., Pfuhl M., and Driscoll P. C. (1998) NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments. Protein Eng. 11, 847-853.
    • (1998) Protein Eng. , vol.11 , pp. 847-853
    • McAlister, M.S.1    Davis, B.2    Pfuhl, M.3    Driscoll, P.C.4
  • 26
    • 0028965629 scopus 로고
    • Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons
    • McGehee D. S. and Role L. W. (1995) Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons. Annu. Rev. Physiol. 57, 521-546.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 521-546
    • McGehee, D.S.1    Role, L.W.2
  • 27
    • 0015292318 scopus 로고
    • Purification, properties and amino acid sequence of α-bungarotoxin from the venom of Bungarus multicinctus
    • Mebs D., Narite K., Iwanaga S., Samejima Y., and Lee C.-Y. (1972) Purification, properties and amino acid sequence of α-bungarotoxin from the venom of Bungarus multicinctus. Hoppe Seylers Z. Physiol. Chem. 353, 243-262.
    • (1972) Hoppe Seylers Z. Physiol. Chem. , vol.353 , pp. 243-262
    • Mebs, D.1    Narite, K.2    Iwanaga, S.3    Samejima, Y.4    Lee, C.-Y.5
  • 28
    • 0027396750 scopus 로고
    • Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis
    • Pillet L., Tremeau O., Ducancel F., Drevet P., Zinn-Justin S., Pinkasfeld S., Boulain J. C., and Ménez A. (1993) Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis. J. Biol. Chem. 268, 909-916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 909-916
    • Pillet, L.1    Tremeau, O.2    Ducancel, F.3    Drevet, P.4    Zinn-Justin, S.5    Pinkasfeld, S.6    Boulain, J.C.7    Ménez, A.8
  • 31
    • 0033564929 scopus 로고    scopus 로고
    • The functional role of positively charged amino acid side chains in α-bungarotoxin revealed by site-directed mutagenesis of a His-tagged recombinant α-bungarotoxin
    • Rosenthal J. A., Levandoski M. M., Chang B., Potts J. F., Shi Q.-L., and Hawrot E. (1999) The functional role of positively charged amino acid side chains in α-bungarotoxin revealed by site-directed mutagenesis of a His-tagged recombinant α-bungarotoxin. Biochemistry 38, 7847-7855.
    • (1999) Biochemistry , vol.38 , pp. 7847-7855
    • Rosenthal, J.A.1    Levandoski, M.M.2    Chang, B.3    Potts, J.F.4    Shi, Q.-L.5    Hawrot, E.6
  • 32
    • 0027398069 scopus 로고
    • The diversity of neuronal nicotinic acetylcholine receptors
    • Sargent P. B. (1993) The diversity of neuronal nicotinic acetylcholine receptors. Annu. Rev. Neurosci. 16, 403-443.
    • (1993) Annu. Rev. Neurosci. , vol.16 , pp. 403-443
    • Sargent, P.B.1
  • 33
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range 1 to 100 kDa
    • Schagger H. and von Jagow G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 34
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins. The functional site of erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues
    • Tremeau O., Lemaire C., Drevet P., Pinkasfeld S., Ducancel F., Boulain J. C., and Ménez A. (1995) Genetic engineering of snake toxins. The functional site of erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. J. Biol. Chem. 270, 9362-9369.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9362-9369
    • Tremeau, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.C.6    Ménez, A.7
  • 35
    • 0022531880 scopus 로고
    • Purification and characterization of a nicotinic acetylcholine receptor from chick brain
    • Whiting P. and Lindstrom J. (1986) Purification and characterization of a nicotinic acetylcholine receptor from chick brain. Biochemistry 25, 2082-2093.
    • (1986) Biochemistry , vol.25 , pp. 2082-2093
    • Whiting, P.1    Lindstrom, J.2
  • 36
    • 1642617187 scopus 로고
    • Purification and characterization of a nicotinic acetylcholine receptor from rat brain
    • Whiting P. and Lindstrom J. (1987) Purification and characterization of a nicotinic acetylcholine receptor from rat brain. Proc. Natl. Acad. Sci. USA 84, 595-599.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 595-599
    • Whiting, P.1    Lindstrom, J.2


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