참고문헌
-
Angsuthanasombat, C., Chungjatupornchai, W., Kertbundit, S., Luxananil, P., Settasatian, C., Wilairat, P. and Panyim, S. (1987) Cloning and expression of 130-kDa mosquito-larvicidal
$\delta$ -endotoxin gene of Bacillus thuringiensis var israelensis in Escherichia coli. Mol. Gen. Genet. 208, 384-389. https://doi.org/10.1007/BF00328128 - Angsuthanasombat, C., Crickmore, N. and Ellar, D. J. (1992) Comparison of Bacillus thuringiensis subsp. israelensis CryIVA and CryIVB cloned toxins reveals synergism in vivo. FEMS Microbiol. Lett. 94, 63-68. https://doi.org/10.1111/j.1574-6968.1992.tb05290.x
- Angsuthanasombat, C., Crickmore, N. and Ellar, D. J. (1993) Effects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB deltaendotoxin. FEMS Microbiol. Lett. 111, 255-261.
- Aronson, A. I., Beckman, W. and Dunn, P. (1986) Bacillus thuringiensis and related insect pathogens. Microbiol. Rev. 50, 1-24.
- Ballester, V., Granero, F., Tabashnik, B. E., Malvar, T. and Ferre, J. (1999) Integrative model for binding of Bacillus thuringiensis toxins in susceptible and resistant larvae of the diamondback moth (Plutella xylostella). Appl. Environ. Microbiol. 65, 2503-2507.
- Becker, N. and Margalit, J. (1993) Use of Bacillus thuringiensis subsp. israelensis against mosquitoes and black flies; in Bacillus thuringiensis, an Environmental Biopesticide: Theory and Practice, Entwistle, P. F., Cory, J. S., Bailey, M. J. and Higgs, S. (eds.), pp. 147-170, John Wiley and Sons, Chichester, UK.
- Burton, S. L., Ellar, D. J., Li, J. and Derbyshire, D. J. (1999) N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognized by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin. J. Mol. Biol. 287, 1101-1122.
- Carroll, J., Li, J. and Ellar, D. J. (1989) Proteolytic processing of a coleopteran-specific delta-endotoxin produced by Bacillus thuringiensis var. tenebrionis. Biochem. J. 261, 99-105.
- Chungjatupornchai, W., Hofte. H., Seurinck, J., Angsuthanasombat, C. and Vaeck, M. (1988) Common features of Bacillus thuringiensis toxins specific for Diptera and Lepidoptera. Eur. J. Biochem. 173, 9-16. https://doi.org/10.1111/j.1432-1033.1988.tb13960.x
- Crickmore, N., Zeigler, D. R., Feitelson, J., Schnepf, E., Van Rie, J., Lereclus, D., Baum, J. and Dean, D. H. (1998) Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62, 807-813.
- Derbyshire, D. J., Ellar, D. J. and Li, J. (2001) Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine. Acta Crystallogr. D. Biol. Crystallogr. 57, 1938-1944. https://doi.org/10.1107/S090744490101040X
- de Maagd, R. A., Bravo, A. and Crickmore, N. (2001) How Bacillus thuringiensis has evolved specific toxins to colonize the insect world. Trends Genet. 4, 193-199.
- Galitsky, N., Cody, V., Wojtczak, A., Ghosh, D., Luft, J. R., Pangborn, W. and English, L. (2001) Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis. Acta Crystallogr. D. Biol. Crystallogr. 57, 1101-1109. https://doi.org/10.1107/S0907444901008186
- Gazit, E., La Rocca, P., Sansom, M. S. and Shai, Y. (1998) The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an 'umbrella-like' structure of the pore. Proc. Natl. Acad. Sci. USA 95, 12289-12294. https://doi.org/10.1073/pnas.95.21.12289
- Gerber, D. and Shai, Y. (2000) Insertion and organization within membranes of the delta-endotoxin pore-forming domain, helix 4-loop-helix 5, and inhibition of its activity by a mutant helix 4 peptide. J. Biol. Chem. 275, 23602-23607. https://doi.org/10.1074/jbc.M002596200
- Gray, W. R. (1997) Disulphide bonds between cysteine residues; in Protein Structure (A Practical Approach). 2nd ed., Creighton, T. E. (ed.), pp. 165-186, Oxford University Press Inc, New York, USA.
- Grochulski, P., Masson, L., Borisova, S., Pusztai-Carey, M., Schwartz, J.-L., Brousseau, R. and Cygler, M. (1995) Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation. J. Mol. Biol. 254, 447-464. https://doi.org/10.1006/jmbi.1995.0630
- Hofte, H. and Whiteley, H. R. (1989) Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53, 242-255.
- Jurat-Fuentes, J.-L. and Adang, M. J. (2001) Importance of Cry1 delta-endotoxin domain II loops for binding specificity in Heliothis virescens (L.). Appl. Environ. Microbiol. 67, 323-329. https://doi.org/10.1128/AEM.67.1.323-329.2001
-
Kanintronkul, Y., Sramala, I., Katzenmeier, G., Panyim, S. and Angsuthanasombat, C. (2003) Specific mutations within the
$\alpha$ 4-$\alpha$ 5 loop of the Bacillus thuringiensis Cry4B toxin reveal a crucial role of Asn-166 and Tyr-170. Mol. Biotechnol. 24, 11-19. https://doi.org/10.1385/MB:24:1:11 -
Knowles, B. H. (1994) Mechanism of action of Bacillus thuringiensis insecticidal
$\delta$ -endotoxins. Adv. Insect. Physiol. 24, 275-308. https://doi.org/10.1016/S0065-2806(08)60085-5 - Knowles, B. H. and Ellar, D. J. (1987) Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis delta endotoxin with difference insect specificity. Biochim. Biophys. Acta 924, 509-518. https://doi.org/10.1016/0304-4165(87)90167-X
- Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291. https://doi.org/10.1107/S0021889892009944
-
Li, J., Carroll, J. and Ellar, D. J. (1991) Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5
${\AA}$ resolution. Nature 353, 815-821. https://doi.org/10.1038/353815a0 - Lee, M. K., Young, B. A. and Dean, D. H. (1995) Domain III exchanges of Bacillus thuringiensis CryIA toxins affect binding to different gypsy moth midgut receptors. Biochem. Biophys. Res. Commun. 216, 306-312. https://doi.org/10.1006/bbrc.1995.2625
- Manavalan, P. and Johnson, W. C. (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76-85. https://doi.org/10.1016/0003-2697(87)90135-7
- Masson, L., Tabashnik, B. E., Liu, Y. B., Brousseau, R. and Schwartz, J.-L. (1999) Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel. J. Biol. Chem. 274, 31996-32000. https://doi.org/10.1074/jbc.274.45.31996
- Masson, L., Tabashnik, B. E., Mazza, A., Prefontaine, G., Potvin, L., Brousseau, R. and Schwartz, J.-L. (2002) Mutagenic analysis of a conserved region of domain III in the Cry1Ac toxin of Bacillus thuringiensis. Appl. Environ. Microbiol. 68, 194-200. https://doi.org/10.1128/AEM.68.1.194-200.2002
- Morse, R. J., Yamamoto, T. and Stroud, R. M. (2001) Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure (Camb.) 9, 409-417. https://doi.org/10.1016/S0969-2126(01)00601-3
- Nicholls, C. N., Ahmad, W. and Ellar, D. J. (1989) Evidence for two different types of insecticidal P2 toxins with dual specificity in Bacillus thuringiensis subspecies. J. Bacteriol. 171, 5141-5147.
-
Nunez-Valdez, M.-E., Sanchez, J., Lina, L., Guereca, L. and Bravo, A. (2001) Structural and functional studies of
$\alpha$ -helix 5 region from Bacillus thuringiensis Cry1Ab$\delta$ -endotoxins. Biochim. Biophys. Acta 1546, 122-133. https://doi.org/10.1016/S0167-4838(01)00132-7 - Ponder, J. W. and Richards, F. M. (1987) An efficient Newton-like method for molecular mechanics energy minimization of large molecules. J. Comput. Chem. 8, 1016-24. https://doi.org/10.1002/jcc.540080710
-
Pornwiroon, W., Katzenmeier, G., Panyim, S. and Angsuthanasombat, C. (2004) Aromaticity of Tyr-202 in the
$\alpha$ 4-$\alpha$ 5 loop is essential for toxicity of the Bacillus thuringiensis Cry4A toxin. J. Biochem. Mol. Biol. 37, 292-297. https://doi.org/10.5483/BMBRep.2004.37.3.292 -
Puntheeranurak, T., Leetachewa, S., Katzenmeier, G., Krittanai, C., Panyim, S. and Angsuthanasombat, C. (2001) Expression and biochemical characterization of the Bacillus thuringiensis Cry4B
$\alpha$ 1-$\alpha$ 5 pore-forming fragment. J. Biochem. Mol. Biol. 34, 293-298. -
Puntheranurak, T., Uawithya, P., Potvin, L., Angsuthanasombat, C., and Schwartz, J.-L. (2004) Ion channels formed in planar lipid bilayers by the dipteran-specific Cry4B Bacillus thuringiensis toxin and its
$\alpha$ 1-$\alpha$ 5 fragment. Mol. Membr. Biol. 21, 67-74. https://doi.org/10.1080/09687680310001625792 - Rajamohan, F., Hussain, S. R., Cotrill, J. A., Gould, F. and Dean, D. H. (1996) Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts. J. Biol. Chem. 271, 25220-25226. https://doi.org/10.1074/jbc.271.41.25220
- Sander, C. and Schneider, R. (1991) Database of homologyderived protein structures and the structural meaning of sequence alignment. Proteins 9, 56-68. https://doi.org/10.1002/prot.340090107
- Schnepf, E., Crickmore, N., Van Rie, J., Lereclus, D., Baum, J., Feitelson, J., Zeigler, D. R. and Dean, D. H. (1998) Bacillus thuringiensis and its pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62, 775-806.
- Schwartz, J.-L., Juteau, M., Grochulski, P., Cygler, M., Prefontaine, G., Brousseau, R. and Masson, L. (1997) Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering. FEBS Lett. 410, 397-402. https://doi.org/10.1016/S0014-5793(97)00626-1
- Smedley, D. P. and Ellar, D. J. (1996) Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion. Microbiology 142, 1617-1624. https://doi.org/10.1099/13500872-142-7-1617
- Sramala, I., Uawithya, P., Chanama, U., Leetachewa, S., Krittanai, C., Katzenmeier, G., Panyim, S. and Angsuthanasombat, C. (2000) Single proline substitutions of selected helices of the Bacillus thuringiensis Cry4B toxin affect inclusion solubility and larvicidal activity. J. Biochem. Mol. Biol. Biophys. 4, 187- 193.
- Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. and Higgins, D. G. (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24, 4876-82.
- Uawithya, P., Tuntitippawan, T., Katzenmeier, G., Panyim, S. and Angsuthanasombat, C. (1998) Effects on larvicidal activity of single proline substitutions in alpha 3 or alpha 4 of the Bacillus thuringiensis Cry4B toxin. Biochem. Mol. Biol. Int. 44, 825-832.
- Von Tersch, M. A., Slatin, S. L., Kulesza, C. A. and English, L. H. (1994) Membrane-permeabilizing activities of Bacillus thuringiensis coleopteran-active toxin CryIIIB2 and CryIIIB2 domain I peptide. Appl. Environ. Microbiol. 60, 3711-3717.
- Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56. https://doi.org/10.1016/0263-7855(90)80070-V
- Walters, F. S., Slatin, S. L., Kulesza, C. A. and English, L. H. (1993) Ion channel activity of N-terminal fragments from CryIA(c) delta-endotoxin. Biochem. Biophys. Res. Commun. 196, 921-926. https://doi.org/10.1006/bbrc.1993.2337
- Ward, S. and Ellar, D. J. (1998) Cloning and expression of two homologous genes of Bacillus thuringiensis subsp. israelensis which encode 130-kilodalton mosquitocidal proteins. J. Bacteriol. 170, 727-735.
- Wynne, S. A., Crowther, R. A. and Leslie, A. G. W. (1999) The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3, 771-780. https://doi.org/10.1016/S1097-2765(01)80009-5
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