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Volumn 145, Issue 3, 2010, Pages 215-221

Variant Cry1Ia toxins generated by DNA shuffling are active against sugarcane giant borer

Author keywords

Bacillus thuringiensis; Brush Border Midgut Vesicles; Molecular modelling; Phage display; Saccharum officinarum; Telchin licus licus

Indexed keywords

BACTERIOLOGY; MOLECULAR MODELING; PROTEINS; TOXICITY;

EID: 74149084627     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.11.011     Document Type: Article
Times cited : (37)

References (38)
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 51249121783 scopus 로고    scopus 로고
    • How to cope with insect resistance to Bt toxins?
    • Bravo A., and Soberón M. How to cope with insect resistance to Bt toxins?. Trends Biotechnol. 26 (2008) 573-579
    • (2008) Trends Biotechnol. , vol.26 , pp. 573-579
    • Bravo, A.1    Soberón, M.2
  • 5
    • 0028905149 scopus 로고
    • Mutations in Domain I of Bacillus thuringiensis δ-Endotoxin CryIAb reduce the irreversible binding of toxin to Manduca sexta brush border membrane vesicles
    • Chen X.J., Curtiss A., Alcantara E., and Dean D.H. Mutations in Domain I of Bacillus thuringiensis δ-Endotoxin CryIAb reduce the irreversible binding of toxin to Manduca sexta brush border membrane vesicles. J. Biol. Chem. 270 (1995) 6412-6419
    • (1995) J. Biol. Chem. , vol.270 , pp. 6412-6419
    • Chen, X.J.1    Curtiss, A.2    Alcantara, E.3    Dean, D.H.4
  • 8
    • 0029930607 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition
    • de Maagd R.A., Kwa M.S.G., Klei V.D., Yamamoto T., Schipper B., Vlak J.M., Stiekema W.J., and Bosch D. Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition. Appl. Environ. Microbiol. 62 (1996) 1537-1543
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1537-1543
    • de Maagd, R.A.1    Kwa, M.S.G.2    Klei, V.D.3    Yamamoto, T.4    Schipper, B.5    Vlak, J.M.6    Stiekema, W.J.7    Bosch, D.8
  • 9
    • 0030574275 scopus 로고    scopus 로고
    • Probing the mechanism of action of Bacillus thuringiensis insecticidal proteins by site-directed mutagenesis-a minireview
    • Dean D.H., Rajamohan F., Lee M.K., Wu S.-J., Chen X.J., Alcantara E., and Hussain S.R. Probing the mechanism of action of Bacillus thuringiensis insecticidal proteins by site-directed mutagenesis-a minireview. Gene 179 (1996) 111-117
    • (1996) Gene , vol.179 , pp. 111-117
    • Dean, D.H.1    Rajamohan, F.2    Lee, M.K.3    Wu, S.-J.4    Chen, X.J.5    Alcantara, E.6    Hussain, S.R.7
  • 11
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32 (2004) 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 12
    • 0031559920 scopus 로고    scopus 로고
    • Isolated domain II and III from the Bacillus thuringiensis Cry1Ab delta-endotoxin binds to lepidopteran midgut membranes
    • Flores H., Soberón X., Sánches J., and Bravo A. Isolated domain II and III from the Bacillus thuringiensis Cry1Ab delta-endotoxin binds to lepidopteran midgut membranes. FEBS Lett. 414 (1997) 313-318
    • (1997) FEBS Lett. , vol.414 , pp. 313-318
    • Flores, H.1    Soberón, X.2    Sánches, J.3    Bravo, A.4
  • 14
    • 59449090348 scopus 로고    scopus 로고
    • Chemical modification of Bacillus thuringiensis Cry1Aa toxin single-cysteine mutants reveals the importance of domain I structural elements in the mechanism or pore formation
    • Girade F., Vachon V., Lebel G., Préfontaine G., Scgwartz J.-L., Masson L., and Laprade R. Chemical modification of Bacillus thuringiensis Cry1Aa toxin single-cysteine mutants reveals the importance of domain I structural elements in the mechanism or pore formation. Biochim. Biophys. Acta. 1788 (2009) 575-580
    • (2009) Biochim. Biophys. Acta. , vol.1788 , pp. 575-580
    • Girade, F.1    Vachon, V.2    Lebel, G.3    Préfontaine, G.4    Scgwartz, J.-L.5    Masson, L.6    Laprade, R.7
  • 16
    • 70349617068 scopus 로고    scopus 로고
    • Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela
    • Guo S., Ye S., Liu Y., Wei L., Xue J., Wu H., Song F., Zhang J., Wu X., Huang D., and Rao Z. Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela. J. Struct. Biol. 168 (2009) 259-266
    • (2009) J. Struct. Biol. , vol.168 , pp. 259-266
    • Guo, S.1    Ye, S.2    Liu, Y.3    Wei, L.4    Xue, J.5    Wu, H.6    Song, F.7    Zhang, J.8    Wu, X.9    Huang, D.10    Rao, Z.11
  • 17
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Höfte H., and Whiteley H.R. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53 (1989) 242-255
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 19
  • 20
    • 0035118386 scopus 로고    scopus 로고
    • Directed molecular evolution in plant improvement
    • Lassner M., and Bedbrook J. Directed molecular evolution in plant improvement. Curr. Opin. Plant Biol. 4 (2001) 152-156
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 152-156
    • Lassner, M.1    Bedbrook, J.2
  • 23
    • 74149086604 scopus 로고    scopus 로고
    • A broca gigante da cana-de-açúcar, Castnia licus Drury, 1770 (Lep.: Castniidae)
    • Cia, Maceió, pp
    • Mendonça, A.F., Viveiros, A.J.A., Sampaio, F.F., 1996. A broca gigante da cana-de-açúcar, Castnia licus Drury, 1770 (Lep.: Castniidae). Pragas da cana-de-açúcar. Insetos, Cia., Maceió., pp. 133-167.
    • (1996) Pragas da cana-de-açúcar. Insetos , pp. 133-167
    • Mendonça, A.F.1    Viveiros, A.J.A.2    Sampaio, F.F.3
  • 25
    • 0030722164 scopus 로고    scopus 로고
    • Applications of DNA shuffling to pharmaceuticals and vaccines
    • Patten P.A., Howard R.J., and Stemmer W.P.C. Applications of DNA shuffling to pharmaceuticals and vaccines. Curr. Opin. Biotechnol. 8 (1997) 724-733
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 724-733
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.C.3
  • 26
    • 2942510818 scopus 로고    scopus 로고
    • Selection from Antibody Libraries
    • Barbas III C.F., Burton D.R., Scott J.K., and Silverman G.J. (Eds), Cold Spring Harbor Laboratory Press, New York
    • Rader C., Steinberger P., and Barbas III C.F. Selection from Antibody Libraries. In: Barbas III C.F., Burton D.R., Scott J.K., and Silverman G.J. (Eds). Phage Display: A laboratory manual (2001), Cold Spring Harbor Laboratory Press, New York 10.1-10.20
    • (2001) Phage Display: A laboratory manual
    • Rader, C.1    Steinberger, P.2    Barbas III, C.F.3
  • 27
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 18244408982 scopus 로고    scopus 로고
    • Phage-display Vectors
    • Barbas III C.F., Burton D.R., Scott J.K., and Silverman G.J. (Eds), Cold Spring Harbor Laboratory Press, New York
    • Scott J.K., and Barbas III C.F. Phage-display Vectors. In: Barbas III C.F., Burton D.R., Scott J.K., and Silverman G.J. (Eds). Phage Display: A laboratory manual (2001), Cold Spring Harbor Laboratory Press, New York 2.1-2.19
    • (2001) Phage Display: A laboratory manual
    • Scott, J.K.1    Barbas III, C.F.2
  • 30
    • 45849086558 scopus 로고    scopus 로고
    • Characterization of a novel Cry9Bb d-endotoxin from Bacillus thuringiensis
    • Silva-Werneck J.O., and Ellar D.J. Characterization of a novel Cry9Bb d-endotoxin from Bacillus thuringiensis. J. Invertebr. Pathol. 98 (2008) 320-328
    • (2008) J. Invertebr. Pathol. , vol.98 , pp. 320-328
    • Silva-Werneck, J.O.1    Ellar, D.J.2
  • 31
    • 0030158571 scopus 로고    scopus 로고
    • The staden sequence analysis package
    • Staden R. The staden sequence analysis package. Mol. Biotechnol. 5 (1996) 233-241
    • (1996) Mol. Biotechnol. , vol.5 , pp. 233-241
    • Staden, R.1
  • 32
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Lett. Nat. 370 (1994) 389-391
    • (1994) Lett. Nat. , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0036921994 scopus 로고    scopus 로고
    • Phage display: practicalities and prospects
    • Willats W.G.T. Phage display: practicalities and prospects. Plant Mol. Biol. 50 (2002) 837-854
    • (2002) Plant Mol. Biol. , vol.50 , pp. 837-854
    • Willats, W.G.T.1
  • 35
    • 45949125218 scopus 로고
    • Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae)
    • Wolfersberger M., Luethy P., Maurer A., Parenti P., Sacchi F.V., Giordana B., and Hanozet G.M. Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae). Comp. Biochem. Phisiol. 86 (1987) 301-308
    • (1987) Comp. Biochem. Phisiol. , vol.86 , pp. 301-308
    • Wolfersberger, M.1    Luethy, P.2    Maurer, A.3    Parenti, P.4    Sacchi, F.V.5    Giordana, B.6    Hanozet, G.M.7
  • 36
    • 67349279272 scopus 로고    scopus 로고
    • N546 in β18-β19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin
    • Xiang W.F., Qiu X.L., Zhi D.X., and Min Z.X. N546 in β18-β19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin. J. Invertebr. Pathol 101 (2009) 119-123
    • (2009) J. Invertebr. Pathol , vol.101 , pp. 119-123
    • Xiang, W.F.1    Qiu, X.L.2    Zhi, D.X.3    Min, Z.X.4
  • 37
    • 33745597608 scopus 로고    scopus 로고
    • A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis
    • Zhang X., Candas M., Griko N.B., Taussig R., and Bulla Jr. L.A. A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 9897-9902
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9897-9902
    • Zhang, X.1    Candas, M.2    Griko, N.B.3    Taussig, R.4    Bulla Jr., L.A.5
  • 38
    • 0030754926 scopus 로고    scopus 로고
    • Opmitization for DNA shuffling for high fidelity recombination
    • Zhao H., and Arnold F.H. Opmitization for DNA shuffling for high fidelity recombination. Nucleic Acids Res. 25 (1997) 1307-1308
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.H.2


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