메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

Recombinant Expression of Margatoxin and Agitoxin-2 in Pichia pastoris: An Efficient Method for Production of KV1.3 Channel Blockers

Author keywords

[No Author keywords available]

Indexed keywords

AGITOXIN 2; DISULFIDE; HYBRID PROTEIN; MARGATOXIN; POTASSIUM CHANNEL BLOCKING AGENT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84871548782     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052965     Document Type: Article
Times cited : (20)

References (50)
  • 3
    • 0035923519 scopus 로고    scopus 로고
    • Selective blockade of T lymphocyte K+ channels ameliorates experimental autoimmune encephalomyelitis, a model for multiple sclerosis
    • Beeton C, Wulff H, Barbaria J, Clot-Faybesse O, Pennington M, et al. (2001) Selective blockade of T lymphocyte K+ channels ameliorates experimental autoimmune encephalomyelitis, a model for multiple sclerosis. Proc Natl Acad Sci USA 98: 13942-13947.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13942-13947
    • Beeton, C.1    Wulff, H.2    Barbaria, J.3    Clot-Faybesse, O.4    Pennington, M.5
  • 4
    • 0142059887 scopus 로고    scopus 로고
    • Potassium channels as therapeutic targets for autoimmune disorders
    • Wulff H, Beeton C, Chandy KG, (2003) Potassium channels as therapeutic targets for autoimmune disorders. Curr Opin Drug Discov Dev 6: 640-647.
    • (2003) Curr Opin Drug Discov Dev , vol.6 , pp. 640-647
    • Wulff, H.1    Beeton, C.2    Chandy, K.G.3
  • 5
    • 27544460565 scopus 로고    scopus 로고
    • Potassium channels, memory T cells, and multiple sclerosis
    • Beeton C, Chandy KG, (2005) Potassium channels, memory T cells, and multiple sclerosis. Neuroscientist 11: 550-562.
    • (2005) Neuroscientist , vol.11 , pp. 550-562
    • Beeton, C.1    Chandy, K.G.2
  • 6
    • 34248599015 scopus 로고    scopus 로고
    • Targeting effector memory T cells with the small molecule Kv1.3 blocker PAP-1 suppresses allergic contact dermatitis
    • Azam P, Sankaranarayanan A, Homerick D, Griffey S, Wulff H, (2007) Targeting effector memory T cells with the small molecule Kv1.3 blocker PAP-1 suppresses allergic contact dermatitis. J Invest Dermatol 127: 1419-1429.
    • (2007) J Invest Dermatol , vol.127 , pp. 1419-1429
    • Azam, P.1    Sankaranarayanan, A.2    Homerick, D.3    Griffey, S.4    Wulff, H.5
  • 7
    • 35548988104 scopus 로고    scopus 로고
    • Pharmacokinetics, toxicity, and functional studies of the selective Kv1.3 channel blocker 5-(4-phenoxybutoxy)psoralen in rhesus macaques
    • Pereira LE, Villinger F, Wulff H, Sankaranarayanan A, Raman G, et al. (2007) Pharmacokinetics, toxicity, and functional studies of the selective Kv1.3 channel blocker 5-(4-phenoxybutoxy)psoralen in rhesus macaques. Exp Biol Med 232: 1338-1354.
    • (2007) Exp Biol Med , vol.232 , pp. 1338-1354
    • Pereira, L.E.1    Villinger, F.2    Wulff, H.3    Sankaranarayanan, A.4    Raman, G.5
  • 8
    • 53349102834 scopus 로고    scopus 로고
    • Imaging of effector memory T cells during a delayed-type hypersensitivity reaction and suppression by Kv1.3 channel block
    • Matheu MP, Beeton C, Garcia A, Chi V, Rangaraju S, et al. (2008) Imaging of effector memory T cells during a delayed-type hypersensitivity reaction and suppression by Kv1.3 channel block. Immunity 29: 602-614.
    • (2008) Immunity , vol.29 , pp. 602-614
    • Matheu, M.P.1    Beeton, C.2    Garcia, A.3    Chi, V.4    Rangaraju, S.5
  • 10
    • 80053645532 scopus 로고    scopus 로고
    • Venoms as a platform for human drugs: translating toxins into therapeutics
    • King GF, (2011) Venoms as a platform for human drugs: translating toxins into therapeutics. Expert Opin Biol Ther 11: 1469-1484.
    • (2011) Expert Opin Biol Ther , vol.11 , pp. 1469-1484
    • King, G.F.1
  • 11
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis RJ, Garcia ML, (2003) Therapeutic potential of venom peptides. Nat Rev Drug Discov 2: 790-802.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 12
    • 0026442383 scopus 로고
    • Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: mechanism of the antiproliferative effect of charybdotoxin
    • Leonard RJ, Garcia ML, Slaughter RS, Reuben JP, (1992) Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: mechanism of the antiproliferative effect of charybdotoxin. Proc Natl Acad Sci USA 89: 10094-10098.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10094-10098
    • Leonard, R.J.1    Garcia, M.L.2    Slaughter, R.S.3    Reuben, J.P.4
  • 13
    • 12744253747 scopus 로고    scopus 로고
    • K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom
    • Mouhat S, Visan V, Ananthakrishnan S, Wulff H, Andreotti N, et al. (2005) K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom. Biochem J 385: 95-104.
    • (2005) Biochem J , vol.385 , pp. 95-104
    • Mouhat, S.1    Visan, V.2    Ananthakrishnan, S.3    Wulff, H.4    Andreotti, N.5
  • 14
    • 6544281465 scopus 로고    scopus 로고
    • Structure and functions of scorpion toxins affecting K+ channels
    • Possani L, Selisko B, Gurrola G, (1999) Structure and functions of scorpion toxins affecting K+ channels. Perspect Drug Discov Design 15/16: 15-40.
    • (1999) Perspect Drug Discov Design , vol.15-16 , pp. 15-40
    • Possani, L.1    Selisko, B.2    Gurrola, G.3
  • 15
    • 0032753963 scopus 로고    scopus 로고
    • A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies
    • Tytgat J, Chandy KG, Garcia ML, Gutman GA, Martin-Eauclaire MF, et al. (1999) A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies. Trends Pharmacol Sci 20: 444-447.
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 444-447
    • Tytgat, J.1    Chandy, K.G.2    Garcia, M.L.3    Gutman, G.A.4    Martin-Eauclaire, M.F.5
  • 16
    • 0035854663 scopus 로고    scopus 로고
    • Functional significance of the β hairpin in the insecticidal neurotoxin ω-atracotoxin-Hv1a
    • Tedford HW, Fletcher JI, King GF, (2001) Functional significance of the β hairpin in the insecticidal neurotoxin ω-atracotoxin-Hv1a. J Biol Chem 276: 26568-26576.
    • (2001) J Biol Chem , vol.276 , pp. 26568-26576
    • Tedford, H.W.1    Fletcher, J.I.2    King, G.F.3
  • 17
    • 80054777668 scopus 로고    scopus 로고
    • A dynamic pharmacophore drives the interaction between psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a
    • Saez NJ, Mobli M, Bieri M, Chassagnon IR, Malde AK, et al. (2011) A dynamic pharmacophore drives the interaction between psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a. Mol Pharmacol 80: 796-808.
    • (2011) Mol Pharmacol , vol.80 , pp. 796-808
    • Saez, N.J.1    Mobli, M.2    Bieri, M.3    Chassagnon, I.R.4    Malde, A.K.5
  • 18
    • 78751585262 scopus 로고    scopus 로고
    • Venomics: a new paradigm for natural products-based drug discovery
    • Vetter I, Davis JL, Rash LD, Anangi R, Mobli M, et al. (2011) Venomics: a new paradigm for natural products-based drug discovery. Amino Acids 40: 15-28.
    • (2011) Amino Acids , vol.40 , pp. 15-28
    • Vetter, I.1    Davis, J.L.2    Rash, L.D.3    Anangi, R.4    Mobli, M.5
  • 19
    • 79959554744 scopus 로고    scopus 로고
    • Functional expression of spider neurotoxic peptide huwentoxin-I in E. coli
    • Meng E, Cai TF, Li WY, Zhang H, Liu YB, et al. (2011) Functional expression of spider neurotoxic peptide huwentoxin-I in E. coli. PloS ONE 6: e21608.
    • (2011) PloS ONE , vol.6
    • Meng, E.1    Cai, T.F.2    Li, W.Y.3    Zhang, H.4    Liu, Y.B.5
  • 20
    • 0028651908 scopus 로고
    • Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy
    • Johnson BA, Stevens SP, Williamson JM, (1994) Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 33: 15061-15070.
    • (1994) Biochemistry , vol.33 , pp. 15061-15070
    • Johnson, B.A.1    Stevens, S.P.2    Williamson, J.M.3
  • 21
    • 0029113242 scopus 로고
    • Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry
    • Krezel AM, Kasibhatla C, Hidalgo P, MacKinnon R, Wagner G, (1995) Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry. Protein Sci 4: 1478-1489.
    • (1995) Protein Sci , vol.4 , pp. 1478-1489
    • Krezel, A.M.1    Kasibhatla, C.2    Hidalgo, P.3    MacKinnon, R.4    Wagner, G.5
  • 22
    • 0027320629 scopus 로고
    • Purification, characterization, and biosynthesis of margatoxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels
    • Garcia-Calvo M, Leonard RJ, Novick J, Stevens SP, Schmalhofer W, et al. (1993) Purification, characterization, and biosynthesis of margatoxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels. J Biol Chem 268: 18866-18874.
    • (1993) J Biol Chem , vol.268 , pp. 18866-18874
    • Garcia-Calvo, M.1    Leonard, R.J.2    Novick, J.3    Stevens, S.P.4    Schmalhofer, W.5
  • 23
    • 30344446652 scopus 로고    scopus 로고
    • Preparation of amino-acid-type selective isotope labeling of protein expressed in Pichia pastoris
    • Chen CY, Cheng CH, Chen YC, Lee JC, Chou SH, et al. (2006) Preparation of amino-acid-type selective isotope labeling of protein expressed in Pichia pastoris. Proteins 62: 279-287.
    • (2006) Proteins , vol.62 , pp. 279-287
    • Chen, C.Y.1    Cheng, C.H.2    Chen, Y.C.3    Lee, J.C.4    Chou, S.H.5
  • 25
    • 77958486556 scopus 로고    scopus 로고
    • Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3
    • Anangi R, Chen CC, Lin YW, Cheng YR, Cheng CH, et al. (2010) Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3. Toxicon 56: 1388-1397.
    • (2010) Toxicon , vol.56 , pp. 1388-1397
    • Anangi, R.1    Chen, C.C.2    Lin, Y.W.3    Cheng, Y.R.4    Cheng, C.H.5
  • 26
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G, (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 27
    • 0028228251 scopus 로고
    • Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines
    • Grissmer S, Nguyen AN, Aiyar J, Hanson DC, Mather RJ, et al. (1994) Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol 45: 1227-1234.
    • (1994) Mol Pharmacol , vol.45 , pp. 1227-1234
    • Grissmer, S.1    Nguyen, A.N.2    Aiyar, J.3    Hanson, D.C.4    Mather, R.J.5
  • 28
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion D, Wüthrich K, (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem Biophys Res Comm 113: 967-974.
    • (1983) Biochem Biophys Res Comm , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 30
    • 0028335105 scopus 로고
    • Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom
    • Garcia ML, Garcia-Calvo M, Hidalgo P, Lee A, MacKinnon R, (1994) Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry 33: 6834-6839.
    • (1994) Biochemistry , vol.33 , pp. 6834-6839
    • Garcia, M.L.1    Garcia-Calvo, M.2    Hidalgo, P.3    Lee, A.4    MacKinnon, R.5
  • 32
    • 70349162817 scopus 로고    scopus 로고
    • The functional network of ion channels in T lymphocytes
    • Cahalan MD, Chandy KG, (2009) The functional network of ion channels in T lymphocytes. Immunol Rev 231: 59-87.
    • (2009) Immunol Rev , vol.231 , pp. 59-87
    • Cahalan, M.D.1    Chandy, K.G.2
  • 33
    • 0033591223 scopus 로고    scopus 로고
    • hSK4/hIK1, a calmodulin-binding KCa channel in human T lymphocytes. Roles in proliferation and volume regulation
    • Khanna R, Chang MC, Joiner WJ, Kaczmarek LK, Schlichter LC, (1999) hSK4/hIK1, a calmodulin-binding KCa channel in human T lymphocytes. Roles in proliferation and volume regulation. J Biol Chem 274: 14838-14849.
    • (1999) J Biol Chem , vol.274 , pp. 14838-14849
    • Khanna, R.1    Chang, M.C.2    Joiner, W.J.3    Kaczmarek, L.K.4    Schlichter, L.C.5
  • 35
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • Lange A, Giller K, Hornig S, Martin-Eauclaire MF, Pongs O, et al. (2006) Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR. Nature 440: 959-962.
    • (2006) Nature , vol.440 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.F.4    Pongs, O.5
  • 36
    • 0030064382 scopus 로고    scopus 로고
    • Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis
    • Ranganathan R, Lewis JH, MacKinnon R, (1996) Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. Neuron 16: 131-139.
    • (1996) Neuron , vol.16 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    MacKinnon, R.3
  • 37
    • 77956064356 scopus 로고    scopus 로고
    • NMR methods for determining disulfide-bond connectivities
    • Mobli M, King GF, (2010) NMR methods for determining disulfide-bond connectivities. Toxicon 56: 849-854.
    • (2010) Toxicon , vol.56 , pp. 849-854
    • Mobli, M.1    King, G.F.2
  • 38
    • 33751232672 scopus 로고    scopus 로고
    • Kv1.3 channels are a therapeutic target for T cell-mediated autoimmune diseases
    • Beeton C, Wulff H, Standifer NE, Azam P, Mullen KM, et al. (2006) Kv1.3 channels are a therapeutic target for T cell-mediated autoimmune diseases. Proc Natl Acad Sci USA 103: 17414-17419.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17414-17419
    • Beeton, C.1    Wulff, H.2    Standifer, N.E.3    Azam, P.4    Mullen, K.M.5
  • 39
    • 80052852577 scopus 로고    scopus 로고
    • Analogs of the sea anemone potassium channel blocker ShK for the treatment of autoimmune diseases
    • Beeton C, Pennington MW, Norton RS, (2011) Analogs of the sea anemone potassium channel blocker ShK for the treatment of autoimmune diseases. Inflamm Allergy Drug Targets 10: 313-321.
    • (2011) Inflamm Allergy Drug Targets , vol.10 , pp. 313-321
    • Beeton, C.1    Pennington, M.W.2    Norton, R.S.3
  • 40
    • 66949176303 scopus 로고    scopus 로고
    • Venomics as a drug discovery platform
    • Escoubas P, King GF, (2009) Venomics as a drug discovery platform. Expert Rev Proteomics 6: 221-224.
    • (2009) Expert Rev Proteomics , vol.6 , pp. 221-224
    • Escoubas, P.1    King, G.F.2
  • 41
    • 67349092459 scopus 로고    scopus 로고
    • Calibrating the chelicerate clock: a paleontological reply to Jeyaprakash and Hoy
    • Dunlop JA, Selden PA, (2009) Calibrating the chelicerate clock: a paleontological reply to Jeyaprakash and Hoy. Exp Appl Acarol 48: 183-197.
    • (2009) Exp Appl Acarol , vol.48 , pp. 183-197
    • Dunlop, J.A.1    Selden, P.A.2
  • 42
    • 17744406515 scopus 로고    scopus 로고
    • Current views on scorpion toxins specific for K+ channels
    • Rodriguez de la Vega RC, Possani LD, (2004) Current views on scorpion toxins specific for K+ channels. Toxicon 43: 865-875.
    • (2004) Toxicon , vol.43 , pp. 865-875
    • Rodriguez de la Vega, R.C.1    Possani, L.D.2
  • 44
    • 49649113677 scopus 로고    scopus 로고
    • Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease
    • Han S, Yi H, Yin SJ, Chen ZY, Liu H, et al. (2008) Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease. J Biol Chem 283: 19058-19065.
    • (2008) J Biol Chem , vol.283 , pp. 19058-19065
    • Han, S.1    Yi, H.2    Yin, S.J.3    Chen, Z.Y.4    Liu, H.5
  • 45
    • 66949177983 scopus 로고    scopus 로고
    • Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3
    • Jensen JE, Durek T, Alewood PF, Adams DJ, King GF, et al. (2009) Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon 54: 56-61.
    • (2009) Toxicon , vol.54 , pp. 56-61
    • Jensen, J.E.1    Durek, T.2    Alewood, P.F.3    Adams, D.J.4    King, G.F.5
  • 46
    • 0036709419 scopus 로고    scopus 로고
    • Role of the structurally disordered N- and C-terminal residues in the Janus-faced atracotoxins
    • Maggio F, King GF, (2002) Role of the structurally disordered N- and C-terminal residues in the Janus-faced atracotoxins. Toxicon 40: 1355-1361.
    • (2002) Toxicon , vol.40 , pp. 1355-1361
    • Maggio, F.1    King, G.F.2
  • 47
    • 6344287807 scopus 로고    scopus 로고
    • Scanning mutagenesis of ω-atracotoxin-Hv1a reveals a spatially restricted epitope that confers selective activity against insect calcium channels
    • Tedford HW, Gilles N, Menez A, Doering CJ, Zamponi GW, et al. (2004) Scanning mutagenesis of ω-atracotoxin-Hv1a reveals a spatially restricted epitope that confers selective activity against insect calcium channels. J Biol Chem 279: 44133-44140.
    • (2004) J Biol Chem , vol.279 , pp. 44133-44140
    • Tedford, H.W.1    Gilles, N.2    Menez, A.3    Doering, C.J.4    Zamponi, G.W.5
  • 48
    • 0031172171 scopus 로고    scopus 로고
    • In vitro folding and functional analysis of an anti-insect selective scorpion depressant neurotoxin produced in Escherichia coli
    • Turkov M, Rashi S, Noam Z, Gordon D, Ben Khalifa R, et al. (1997) In vitro folding and functional analysis of an anti-insect selective scorpion depressant neurotoxin produced in Escherichia coli. Protein Expr Purif 10: 123-131.
    • (1997) Protein Expr Purif , vol.10 , pp. 123-131
    • Turkov, M.1    Rashi, S.2    Noam, Z.3    Gordon, D.4    Ben Khalifa, R.5
  • 49
    • 0037634059 scopus 로고    scopus 로고
    • Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels
    • Escoubas P, Bernard C, Lambeau G, Lazdunski M, Darbon H, (2003) Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels. Protein Sci 12: 1332-1343.
    • (2003) Protein Sci , vol.12 , pp. 1332-1343
    • Escoubas, P.1    Bernard, C.2    Lambeau, G.3    Lazdunski, M.4    Darbon, H.5
  • 50
    • 84860521762 scopus 로고    scopus 로고
    • Charybdotoxin and margatoxin acting on the human voltage-gated potassium channel hKv1.3 and its H399N mutant: an experimental and computational comparison
    • Nikouee A, Khabiri M, Grissmer S, Ettrich R, (2012) Charybdotoxin and margatoxin acting on the human voltage-gated potassium channel hKv1.3 and its H399N mutant: an experimental and computational comparison. J Phys Chem B 116: 5132-5140.
    • (2012) J Phys Chem B , vol.116 , pp. 5132-5140
    • Nikouee, A.1    Khabiri, M.2    Grissmer, S.3    Ettrich, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.