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Volumn 58, Issue 1, 2011, Pages 93-100

Recombinant conotoxin, TxVIA, produced in yeast has insecticidal activity

Author keywords

Deroceras reticulatum; Ion channel; Mamestra brassicae; Musca domestica; Neurotoxin; Pichia pastoris; Pro peptide

Indexed keywords

CONOTOXIN; TXVIA TOXIN; UNCLASSIFIED DRUG;

EID: 79959373747     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2011.05.009     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0028504107 scopus 로고
    • Laboratory evaluation of six species of entomopathogenic fungi for the control of the house fly (Musca domestica L.), a pest of intensive animal units
    • Barson G., Renn N., Bywater A.F. Laboratory evaluation of six species of entomopathogenic fungi for the control of the house fly (Musca domestica L.), a pest of intensive animal units. J. Invertebr. Pathol. 1994, 64:107-113.
    • (1994) J. Invertebr. Pathol. , vol.64 , pp. 107-113
    • Barson, G.1    Renn, N.2    Bywater, A.F.3
  • 3
    • 0031177988 scopus 로고    scopus 로고
    • Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families
    • Bown D.P., Wilkinson H.S., Gatehouse J.A. Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families. Insect Biochem. Mol. Biol. 1997, 27:625-638.
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 625-638
    • Bown, D.P.1    Wilkinson, H.S.2    Gatehouse, J.A.3
  • 4
    • 0942279699 scopus 로고    scopus 로고
    • Propeptide does not act as a molecular chaperone but facilitates protein disulphide isomerase-assisted folding of a conotoxin precursor
    • Buczec O., Olivera B.M., Bulaj G. Propeptide does not act as a molecular chaperone but facilitates protein disulphide isomerase-assisted folding of a conotoxin precursor. Biochemistry 2004, 43:1093-1101.
    • (2004) Biochemistry , vol.43 , pp. 1093-1101
    • Buczec, O.1    Olivera, B.M.2    Bulaj, G.3
  • 6
    • 40449127990 scopus 로고    scopus 로고
    • Toxins from cone snails: properties, applications and biotechnological production
    • Becker S., Terlau H. Toxins from cone snails: properties, applications and biotechnological production. Appl. Microbiol. Biotechnol. 2008, 79:1-9.
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 1-9
    • Becker, S.1    Terlau, H.2
  • 8
    • 0141650651 scopus 로고    scopus 로고
    • Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease
    • Cabral K.M.S., Almeida M.S., Valente A.P., Almeida F.C.L., Kurtenback E. Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease. Protein Expr. Purif. 2003, 31:115-122.
    • (2003) Protein Expr. Purif. , vol.31 , pp. 115-122
    • Cabral, K.M.S.1    Almeida, M.S.2    Valente, A.P.3    Almeida, F.C.L.4    Kurtenback, E.5
  • 9
    • 0037929460 scopus 로고    scopus 로고
    • Cloning and expression of biologically active Plantago lanceolata pollen allergen Pla l 1 in the yeast Pichia pastoris
    • Calabozo B., Díaz-Perales A., Salcedo G., Barber D., Polo F. Cloning and expression of biologically active Plantago lanceolata pollen allergen Pla l 1 in the yeast Pichia pastoris. Biochem. J. 2003, 372:889-896.
    • (2003) Biochem. J. , vol.372 , pp. 889-896
    • Calabozo, B.1    Díaz-Perales, A.2    Salcedo, G.3    Barber, D.4    Polo, F.5
  • 11
    • 14744285206 scopus 로고    scopus 로고
    • Review: expression of heterologous proteins in Pichia pastoris: a useful tool in protein engineering and production
    • Daly R., Hearn M.T.W. Review: expression of heterologous proteins in Pichia pastoris: a useful tool in protein engineering and production. J. Mol. Recognit. 2005, 18:119-138.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 12
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: quality control in the secretory pathway
    • Ellgaard L., Molinari M., Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999, 286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 13
    • 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. Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels. Protein Sci. 2003, 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
  • 15
    • 0028049479 scopus 로고
    • A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in mollusks and acts as an antagonist in rat brain
    • Fainzibler M., Kofman O., Zlotkin E., Gordon D. A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in mollusks and acts as an antagonist in rat brain. J. Biol. Chem. 1994, 269:2574-2580.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2574-2580
    • Fainzibler, M.1    Kofman, O.2    Zlotkin, E.3    Gordon, D.4
  • 16
    • 1642568734 scopus 로고    scopus 로고
    • Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused spider venom toxin to insect haemolymph following oral ingestion
    • Fitches E., Edwards M.G., Mee C., Grisham E., Gatehouse A.M.R., Edwards J.P., Gatehouse J.A. Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused spider venom toxin to insect haemolymph following oral ingestion. J. Insect Physiol. 2004, 50:61-71.
    • (2004) J. Insect Physiol. , vol.50 , pp. 61-71
    • Fitches, E.1    Edwards, M.G.2    Mee, C.3    Grisham, E.4    Gatehouse, A.M.R.5    Edwards, J.P.6    Gatehouse, J.A.7
  • 17
    • 0031728454 scopus 로고    scopus 로고
    • A comparison of the short and long term effects of insecticidal lectins on the activities of soluble and brush border enzymes of the tomato moth larvae (Lacanobia oleracea)
    • Fitches E., Gatehouse J.A. A comparison of the short and long term effects of insecticidal lectins on the activities of soluble and brush border enzymes of the tomato moth larvae (Lacanobia oleracea). J. Insect Physiol. 1998, 44:1213-1224.
    • (1998) J. Insect Physiol. , vol.44 , pp. 1213-1224
    • Fitches, E.1    Gatehouse, J.A.2
  • 18
    • 0002037385 scopus 로고    scopus 로고
    • The usage of molluscicides in agriculture and horticulture in Great Britain over the past 30 years
    • In: Slug and Snail Pests in Agriculture, BCPC Monograph No 66, Canterbury, UK,
    • Garthwaite, D.G., Thomas, M.R., 1996. The usage of molluscicides in agriculture and horticulture in Great Britain over the past 30 years. In: Slug and Snail Pests in Agriculture, BCPC Monograph No 66, Canterbury, UK, pp. 39-46.
    • (1996) , pp. 39-46
    • Garthwaite, D.G.1    Thomas, M.R.2
  • 19
    • 0027479426 scopus 로고
    • Alteration of sodium currents by new peptide toxins from the venom of a molluscivorous Conus snail
    • Hasson A., Fainzibler M., Gordon D., Zlotkin E., Spira M.E. Alteration of sodium currents by new peptide toxins from the venom of a molluscivorous Conus snail. Eur. J. Neurosci. 1993, 5:56-64.
    • (1993) Eur. J. Neurosci. , vol.5 , pp. 56-64
    • Hasson, A.1    Fainzibler, M.2    Gordon, D.3    Zlotkin, E.4    Spira, M.E.5
  • 21
    • 0037184042 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the sodium channel agonist/antagonist δ-conotoxin TxVIA
    • Kohno T., Sasaki T., Kobayashi K., Fainzibler M., Sato K. Three-dimensional solution structure of the sodium channel agonist/antagonist δ-conotoxin TxVIA. J. Biol. Chem. 2002, 277:36387-36391.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36387-36391
    • Kohno, T.1    Sasaki, T.2    Kobayashi, K.3    Fainzibler, M.4    Sato, K.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0142245696 scopus 로고    scopus 로고
    • High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2
    • Lehmann K., Hoffman S., Neudecker P., Suhr M., Becker W.M., Rosch P. High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2. Protein Expr. Purif. 2003, 31:250-259.
    • (2003) Protein Expr. Purif. , vol.31 , pp. 250-259
    • Lehmann, K.1    Hoffman, S.2    Neudecker, P.3    Suhr, M.4    Becker, W.M.5    Rosch, P.6
  • 25
    • 0030729069 scopus 로고    scopus 로고
    • Conus venom peptides, receptor and ion channel targets and drug design: 50 million years of neuropharmacology (EE Just Lecture, 1996)
    • Olivera B.M. Conus venom peptides, receptor and ion channel targets and drug design: 50 million years of neuropharmacology (EE Just Lecture, 1996). Mol. Biol. Cell 1997, 8:2101-2109.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2101-2109
    • Olivera, B.M.1
  • 26
    • 0033029128 scopus 로고    scopus 로고
    • Homogeneous sample preparation for automated high throughput analysis with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Rapid Commun
    • Onnerfjord P., Ekström S., Bergquist J., Nilsson J., Laurell T., Marko-Varga G. Homogeneous sample preparation for automated high throughput analysis with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 1999, 13:315-322.
    • (1999) Mass Spectrom. , vol.13 , pp. 315-322
    • Onnerfjord, P.1    Ekström, S.2    Bergquist, J.3    Nilsson, J.4    Laurell, T.5    Marko-Varga, G.6
  • 27
    • 33845761868 scopus 로고    scopus 로고
    • Soluble expression, purification and identification of a disulphide-rich conotoxin derived from Conus litteratus
    • Pi C., Liu J., Wang L., Jiang X., Liu Y., Peng C., Chen S., Xu A. Soluble expression, purification and identification of a disulphide-rich conotoxin derived from Conus litteratus. J. Biotechnol. 2007, 128:184-193.
    • (2007) J. Biotechnol. , vol.128 , pp. 184-193
    • Pi, C.1    Liu, J.2    Wang, L.3    Jiang, X.4    Liu, Y.5    Peng, C.6    Chen, S.7    Xu, A.8
  • 28
    • 0029856411 scopus 로고    scopus 로고
    • Folding of ω-conotoxins. 2. Influence of precursor sequences and protein disulphide isomerase
    • Price-Carter M., Gray W.M., Goldenberg D.P. Folding of ω-conotoxins. 2. Influence of precursor sequences and protein disulphide isomerase. Biochemistry 1996, 35:15547-15557.
    • (1996) Biochemistry , vol.35 , pp. 15547-15557
    • Price-Carter, M.1    Gray, W.M.2    Goldenberg, D.P.3
  • 29
    • 0030046574 scopus 로고    scopus 로고
    • Review: in vitro folding of inclusion body proteins
    • Rudolph R., Lilie H. Review: in vitro folding of inclusion body proteins. FASEB J. 1996, 10:49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 31
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau H., Shon K.J., Grilley M., Stocker M., Stuhmer W., Olivera B.M. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature 1996, 381:148-151.
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 32
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: a rich source of novel ion channel-targeted peptides
    • Terlau H., Olivera B.M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol. Rev. 2004, 84:41-68.
    • (2004) Physiol. Rev. , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 33
    • 33646561868 scopus 로고    scopus 로고
    • A fusion protein containing a lepidopteran-specific toxin from the South Indian red scorpion (Mesobuthus tamulus) and snowdrop lectin shows oral toxicity to target insects
    • Trung N.P., Fitches E., Gatehouse J.A. A fusion protein containing a lepidopteran-specific toxin from the South Indian red scorpion (Mesobuthus tamulus) and snowdrop lectin shows oral toxicity to target insects. BMC Biotechnol. 2006, 6:18.
    • (2006) BMC Biotechnol. , vol.6 , pp. 18
    • Trung, N.P.1    Fitches, E.2    Gatehouse, J.A.3
  • 34
    • 15444362099 scopus 로고    scopus 로고
    • Conus peptides - a rich pharmaceutical treasure
    • Wang C.Z., Chi C.W. Conus peptides - a rich pharmaceutical treasure. Acta Biochim. Biophys. Sin. 2004, 36:713-723.
    • (2004) Acta Biochim. Biophys. Sin. , vol.36 , pp. 713-723
    • Wang, C.Z.1    Chi, C.W.2
  • 35
    • 57849140606 scopus 로고    scopus 로고
    • Identification and characterization of a novel O-superfamily conotoxin from Conus litteratus
    • Wang L., Pi C., Liu J., Chen S., Peng C., Sun D., Zhou M., Xiang H., Ren Z., Xu A. Identification and characterization of a novel O-superfamily conotoxin from Conus litteratus. J. Pept. Sci. 2008, 14:1077-1083.
    • (2008) J. Pept. Sci. , vol.14 , pp. 1077-1083
    • Wang, L.1    Pi, C.2    Liu, J.3    Chen, S.4    Peng, C.5    Sun, D.6    Zhou, M.7    Xiang, H.8    Ren, Z.9    Xu, A.10
  • 36
    • 0028774540 scopus 로고
    • Expression of highly disulphide-bonded proteins in Pichia pastoris
    • White C.E., Kempi N.M., Komives E.A. Expression of highly disulphide-bonded proteins in Pichia pastoris. Structure 1994, 2:1003-1005.
    • (1994) Structure , vol.2 , pp. 1003-1005
    • White, C.E.1    Kempi, N.M.2    Komives, E.A.3
  • 37
    • 0031791992 scopus 로고    scopus 로고
    • Omega-toxins affect Na+ currents in neurosecretory insect neurons
    • Wicher D., Penzlin H. Omega-toxins affect Na+ currents in neurosecretory insect neurons. Receptors Channels 1998, 5:355-366.
    • (1998) Receptors Channels , vol.5 , pp. 355-366
    • Wicher, D.1    Penzlin, H.2
  • 38
    • 33749667367 scopus 로고    scopus 로고
    • Recombinant omega-conotoxin MVIIA possesses strong analgesic activity
    • Xia Z., Chen Y., Zhu Y., Wang F., Xu X., Zhan J. Recombinant omega-conotoxin MVIIA possesses strong analgesic activity. BioDrugs 2006, 20:275-281.
    • (2006) BioDrugs , vol.20 , pp. 275-281
    • Xia, Z.1    Chen, Y.2    Zhu, Y.3    Wang, F.4    Xu, X.5    Zhan, J.6


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