메뉴 건너뛰기




Volumn 72, Issue 1, 2006, Pages 506-515

Protease inhibitors fail to prevent pore formation by the activated Bacillus thuringiensis toxin Cry1Aa in insect brush border membrane vesicles

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; ENZYMES; LIGHT SCATTERING; PH EFFECTS; TOXIC MATERIALS;

EID: 33644860854     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.1.506-515.2006     Document Type: Article
Times cited : (28)

References (69)
  • 1
    • 0022386469 scopus 로고
    • Protease activation of the entomocidal protoxin of Bacillus thuringiensis subsp. kurstaki
    • Andrews, R. E., Jr., M. M. Bibilos, and L. A, Bulla, Jr. 1985. Protease activation of the entomocidal protoxin of Bacillus thuringiensis subsp. kurstaki. Appl. Environ. Microbiol. 50:737-742.
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 737-742
    • Andrews Jr., R.E.1    Bibilos, M.M.2    Bulla Jr., L.A.3
  • 2
    • 0027264640 scopus 로고
    • Effects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB δ-endotoxin
    • Angsuthanasombat, C., N. Crickmore, and D. J. Ellar. 1993. Effects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB δ-endotoxin. FEMS Microbiol. Lett. 111:255-262.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 255-262
    • Angsuthanasombat, C.1    Crickmore, N.2    Ellar, D.J.3
  • 3
    • 0032877662 scopus 로고    scopus 로고
    • Production of chymotrypsin-resistant Bacillus thuringiensis Cry2Aa1 δ-endotoxin by protein engineering
    • Audtho, M., A. P. Valaitis, O. Alzate, and D. H. Dean. 1999. Production of chymotrypsin-resistant Bacillus thuringiensis Cry2Aa1 δ-endotoxin by protein engineering. Appl. Environ. Microbiol. 65:4601-4605.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4601-4605
    • Audtho, M.1    Valaitis, A.P.2    Alzate, O.3    Dean, D.H.4
  • 4
    • 16544393124 scopus 로고    scopus 로고
    • The Bacillus thuringiensis Cry1Aa toxin: Effects of trypsin and chymotrypsin site mutations on toxicity and stability
    • Bah, A., K. van Frankenhuyzen, R. Brousseau, and L. Massen. 2004. The Bacillus thuringiensis Cry1Aa toxin: effects of trypsin and chymotrypsin site mutations on toxicity and stability. J. Invertebr. Pathol. 85:120-127.
    • (2004) J. Invertebr. Pathol. , vol.85 , pp. 120-127
    • Bah, A.1    Van Frankenhuyzen, K.2    Brousseau, R.3    Massen, L.4
  • 5
    • 0028673152 scopus 로고
    • Classification of peptidases
    • Barrett, A. J. 1994. Classification of peptidases. Methods Enzymol 244:1-15.
    • (1994) Methods Enzymol , vol.244 , pp. 1-15
    • Barrett, A.J.1
  • 6
    • 0024328328 scopus 로고
    • Facile preparation and characterization of the toxin from Bacillus thuringiensis var. kurslaki
    • Bietlot, H., P. R. Carey, C. Choma, H. Kaplan, T. Lessard, and M. Pozsgay. 1989. Facile preparation and characterization of the toxin from Bacillus thuringiensis var. kurslaki. Biochem. J. 260:87-91.
    • (1989) Biochem. J. , vol.260 , pp. 87-91
    • Bietlot, H.1    Carey, P.R.2    Choma, C.3    Kaplan, H.4    Lessard, T.5    Pozsgay, M.6
  • 7
    • 16244392435 scopus 로고    scopus 로고
    • Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications
    • Boonserm, P., P. Davis, D. J. Ellar, and J. Li. 2005. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J. MoI. Biol. 348:363-382.
    • (2005) J. MoI. Biol. , vol.348 , pp. 363-382
    • Boonserm, P.1    Davis, P.2    Ellar, D.J.3    Li, J.4
  • 8
    • 7744222624 scopus 로고    scopus 로고
    • Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains
    • Bravo, A., I. Gomez, J. Conde, C. Muñoz-Garay, J. Sánchez, R. Miranda, M. Zhuang, S. S. Gill, and M. Soberón. 2004. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. Biochim. Biophys. Acta 1667:38-46.
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 38-46
    • Bravo, A.1    Gomez, I.2    Conde, J.3    Muñoz-Garay, C.4    Sánchez, J.5    Miranda, R.6    Zhuang, M.7    Gill, S.S.8    Soberón, M.9
  • 10
    • 0031182629 scopus 로고    scopus 로고
    • Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A δ-endotoxin may facilitate its coleopteran toxicity
    • Carroll, J., D. Convents, J. Van Damme, A. Boets, J. Van Rie, and D. J. Ellar. 1997. Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A δ-endotoxin may facilitate its coleopteran toxicity. J. Invertebr. Pathol. 70:41-49.
    • (1997) J. Invertebr. Pathol. , vol.70 , pp. 41-49
    • Carroll, J.1    Convents, D.2    Van Damme, J.3    Boets, A.4    Van Rie, J.5    Ellar, D.J.6
  • 11
    • 0027314529 scopus 로고
    • An analysis of Bacillus thuringiensis δ-endotoxin action on insect-midgut-membrane permeability using a light-scattering assay
    • Carroll, J., and D. J. Ellar. 1993. An analysis of Bacillus thuringiensis δ-endotoxin action on insect-midgut-membrane permeability using a light-scattering assay. Eur. J. Biochem. 214:771-778.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 771-778
    • Carroll, J.1    Ellar, D.J.2
  • 12
    • 0024320570 scopus 로고
    • Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis
    • Carroll, J., J. Li, and D. J. Ellar. 1989. Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis. Biochem. J. 261:99-105.
    • (1989) Biochem. J. , vol.261 , pp. 99-105
    • Carroll, J.1    Li, J.2    Ellar, D.J.3
  • 13
    • 0025337108 scopus 로고
    • Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis. Structural implications
    • Choma, C. T., W. K. Surewicz, P. R. Carey, M. Pozsgay, T. Raynor, and H. Kaplan. 1990. Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis. Structural implications. Eur. J. Biochem. 189:523-527.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 523-527
    • Choma, C.T.1    Surewicz, W.K.2    Carey, P.R.3    Pozsgay, M.4    Raynor, T.5    Kaplan, H.6
  • 14
    • 0026031259 scopus 로고
    • Two structural domains as a general fold of the toxic fragment of the Bacillus thuringiensis δ-endotoxins
    • Convents, D., M. Cherlet, J. Van Damme, I. Lasters, and M. Lauwereys. 1991. Two structural domains as a general fold of the toxic fragment of the Bacillus thuringiensis δ-endotoxins. Eur. J. Biochem. 195:631-635.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 631-635
    • Convents, D.1    Cherlet, M.2    Van Damme, J.3    Lasters, I.4    Lauwereys, M.5
  • 16
    • 0024052158 scopus 로고
    • Barium and calcium block Bacillus thuringiensis subspecies kurstaki δ-endotoxin inhibition of potassium current across isolated midgut of larval Manduca sexta
    • Crawford, D. N., and W. R. Harvey. 1988. Barium and calcium block Bacillus thuringiensis subspecies kurstaki δ-endotoxin inhibition of potassium current across isolated midgut of larval Manduca sexta. J. Exp. Biol. 137:277-286.
    • (1988) J. Exp. Biol. , vol.137 , pp. 277-286
    • Crawford, D.N.1    Harvey, W.R.2
  • 17
    • 0027562745 scopus 로고
    • In vitro and in vivo proteolysis of the Bacillus thuringiensis subsp. israelensis CryIVD protein by Culex quinquefasciatus larval midgut proteases
    • Dai, S.-M., and S. S. Gill. 1993. In vitro and in vivo proteolysis of the Bacillus thuringiensis subsp. israelensis CryIVD protein by Culex quinquefasciatus larval midgut proteases. Insect Biochem. Mol. Biol. 23:273-283.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 273-283
    • Dai, S.-M.1    Gill, S.S.2
  • 18
    • 0021417293 scopus 로고
    • Extremely high pH in biological systems: A model for carbonate transport
    • Dow, J. A. T. 1984. Extremely high pH in biological systems: a model for carbonate transport. Am. J. Physiol. 246:R633-R635.
    • (1984) Am. J. Physiol. , vol.246
    • Dow, J.A.T.1
  • 19
    • 0001087630 scopus 로고
    • pH gradients in lepidopteran midgut
    • Dow, J. A. T. 1992. pH gradients in lepidopteran midgut. J. Exp. Biol. 172:355-375.
    • (1992) J. Exp. Biol. , vol.172 , pp. 355-375
    • Dow, J.A.T.1
  • 20
    • 0342697515 scopus 로고
    • Chemical additives that affect the potency of endotoxin of Bacillus thuringiensis against Plodia interpunctella
    • El-Moursy, A., R. Aboul-Ela, H. S. Salama, and A. Abdel-Razek. 1992. Chemical additives that affect the potency of endotoxin of Bacillus thuringiensis against Plodia interpunctella. Insect Sci. Applic. 13:775-779.
    • (1992) Insect Sci. Applic. , vol.13 , pp. 775-779
    • El-Moursy, A.1    Aboul-Ela, R.2    Salama, H.S.3    Abdel-Razek, A.4
  • 22
    • 0001688230 scopus 로고
    • Sulfonyl fluorides as inhibitors of esterases. III. Identification of serine as the site of sulfonylation in phenylmethanesulfonyl α-chymotrypsin
    • Gold, A. M. 1965. Sulfonyl fluorides as inhibitors of esterases. III. Identification of serine as the site of sulfonylation in phenylmethanesulfonyl α-chymotrypsin. Biochemistry 4:897-901.
    • (1965) Biochemistry , vol.4 , pp. 897-901
    • Gold, A.M.1
  • 23
    • 0037181168 scopus 로고    scopus 로고
    • Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin
    • Gómez, I., J. Sánchez, R. Miranda, A. Bravo, and M. Soberón. 2002. Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin. FEBS Lett. 513:242-246.
    • (2002) FEBS Lett. , vol.513 , pp. 242-246
    • Gómez, I.1    Sánchez, J.2    Miranda, R.3    Bravo, A.4    Soberón, M.5
  • 25
    • 0025045696 scopus 로고
    • Effects of Bacillus thuringiensis delta-endotoxin on the permeability of brush border membrane vesicles from tobacco hornworm (Manduca sexta) midgut
    • Hendrickx, K., A. De Loof, and H. Van Mellaert. 1990. Effects of Bacillus thuringiensis delta-endotoxin on the permeability of brush border membrane vesicles from tobacco hornworm (Manduca sexta) midgut. Comp. Biochem. Physiol. 95C:241-245.
    • (1990) Comp. Biochem. Physiol. , vol.95 , pp. 241-245
    • Hendrickx, K.1    De Loof, A.2    Van Mellaert, H.3
  • 26
    • 4143130999 scopus 로고    scopus 로고
    • Characterization of a novel plasma membrane protein, expressed in the midgut epithelia of Bombyx mori, that binds to Cry1A toxins
    • Hossain, D. M., Y. Shitomi, K. Moriyama, M. Higuchi, T. Hayakawa, T. Mitsui, R. Sato, and H. Hori. 2004. Characterization of a novel plasma membrane protein, expressed in the midgut epithelia of Bombyx mori, that binds to Cry1A toxins. Appl. Environ. Microbiol. 70:4604-4612.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 4604-4612
    • Hossain, D.M.1    Shitomi, Y.2    Moriyama, K.3    Higuchi, M.4    Hayakawa, T.5    Mitsui, T.6    Sato, R.7    Hori, H.8
  • 27
    • 0032473877 scopus 로고    scopus 로고
    • Characterization of aminopeptidase N from the brush border membrane of the larvae midgut of silkworm, Bombyx mori as a zinc enzyme
    • Hua, G., K. Tsukamoto, R. Taguchi, M. Tomita, S. Miyajima, and H. Ikezawa. 1998. Characterization of aminopeptidase N from the brush border membrane of the larvae midgut of silkworm, Bombyx mori as a zinc enzyme. Biochim. Biophys. Acta 1383:301-310.
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 301-310
    • Hua, G.1    Tsukamoto, K.2    Taguchi, R.3    Tomita, M.4    Miyajima, S.5    Ikezawa, H.6
  • 28
    • 0018130363 scopus 로고
    • Inactivation of the protease inhibitor phenylmethylsulfonyl fluoride in buffers
    • James, G. T. 1978. Inactivation of the protease inhibitor phenylmethylsulfonyl fluoride in buffers. Anal. Biochem. 86:574-579.
    • (1978) Anal. Biochem. , vol.86 , pp. 574-579
    • James, G.T.1
  • 29
    • 0030114708 scopus 로고    scopus 로고
    • Digestion of δ-entotoxin by gut proteases may explain reduced sensitivity of advanced instar larvae of Spodoptera littoralis to Cry1C
    • Keller, M., B. Sneh, N. Strizhov, E. Prudovsky, A. Regev, C. Koncz, J. Schell, and A. Zilberstein. 1996. Digestion of δ-entotoxin by gut proteases may explain reduced sensitivity of advanced instar larvae of Spodoptera littoralis to Cry1C. Insect Biochem. Mol. Biol. 26:365-373.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 365-373
    • Keller, M.1    Sneh, B.2    Strizhov, N.3    Prudovsky, E.4    Regev, A.5    Koncz, C.6    Schell, J.7    Zilberstein, A.8
  • 30
    • 0037066630 scopus 로고    scopus 로고
    • Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles
    • Kirouac, M., V. Vachon, J.-F. Noël, F. Girard, J.-L. Schwartz, and R. Laprade. 2002. Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles. Biochim. Biophys. Acta 1561:171-179.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 171-179
    • Kirouac, M.1    Vachon, V.2    Noël, J.-F.3    Girard, F.4    Schwartz, J.-L.5    Laprade, R.6
  • 31
    • 0344628681 scopus 로고    scopus 로고
    • Analysis of the properties of Bacillus thuringiensis insecticidal toxins using a potential-sensitive fluorescent probe
    • Kirouac, M., V. Vachon, S. Rivest, J.-L. Schwartz, and R. Laprade. 2003. Analysis of the properties of Bacillus thuringiensis insecticidal toxins using a potential-sensitive fluorescent probe. J. Membr. Biol. 196:51-59.
    • (2003) J. Membr. Biol. , vol.196 , pp. 51-59
    • Kirouac, M.1    Vachon, V.2    Rivest, S.3    Schwartz, J.-L.4    Laprade, R.5
  • 33
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li, J., J. Carroll, and D. J. Ellar. 1991. Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353:815-821.
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 34
    • 0034859678 scopus 로고    scopus 로고
    • Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms
    • Li, J., D. J. Derbyshire, B. Promdonkoy, and D. J. Ellar. 2001. Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms. Biochem. Soc. Trans. 29:571-577.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 571-577
    • Li, J.1    Derbyshire, D.J.2    Promdonkoy, B.3    Ellar, D.J.4
  • 35
    • 0034467902 scopus 로고    scopus 로고
    • Role of proteolysis in determining potency of Bacillus thuringiensis Cry1Ac δ-endotoxin
    • Lightwood, D. J., D. J. Ellar, and P. Jarrett. 2000. Role of proteolysis in determining potency of Bacillus thuringiensis Cry1Ac δ-endotoxin. Appl. Environ. Microbiol 66:5174-5181.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 5174-5181
    • Lightwood, D.J.1    Ellar, D.J.2    Jarrett, P.3
  • 36
    • 0008153028 scopus 로고    scopus 로고
    • Synergism of Bacillus thuringiensis by ethylenediamine tetraacetate in susceptible and resistant larvae of diamond-back moth (Lepidoptera: Plutellidae)
    • Liu, Y.-B., and B. E. Tabashnik. 1997. Synergism of Bacillus thuringiensis by ethylenediamine tetraacetate in susceptible and resistant larvae of diamond-back moth (Lepidoptera: Plutellidae). J. Econ. Entomol. 90:287-292.
    • (1997) J. Econ. Entomol. , vol.90 , pp. 287-292
    • Liu, Y.-B.1    Tabashnik, B.E.2
  • 37
    • 0031559895 scopus 로고    scopus 로고
    • Aminopeptidase dependent pore formation of Bacillus thuringiensis Cry1Ac toxin on Trichoplusia ni membranes
    • Lorence, A., A. Darszon, and A. Bravo. 1997. Aminopeptidase dependent pore formation of Bacillus thuringiensis Cry1Ac toxin on Trichoplusia ni membranes. FEBS Lett. 414:303-307.
    • (1997) FEBS Lett. , vol.414 , pp. 303-307
    • Lorence, A.1    Darszon, A.2    Bravo, A.3
  • 38
    • 0028986449 scopus 로고
    • Endotoxins induce cation channels in Spodoptera frugiperda brush border membranes in suspension and in planar lipid bilayers
    • Lorence, A., A. Darszon, C. Diaz, A. Liévano, R. Quintero, and A. Bravo. 1995. δ-Endotoxins induce cation channels in Spodoptera frugiperda brush border membranes in suspension and in planar lipid bilayers. FEBS Lett. 360:217-222.
    • (1995) FEBS Lett. , vol.360 , pp. 217-222
    • Lorence, A.1    Darszon, A.2    Diaz, C.3    Liévano, A.4    Quintero, R.5    Bravo, A.6
  • 40
    • 0028239097 scopus 로고
    • Ligand blot identification of a Manduca sexta midgut binding protein specific to three Bacillus thuringiensis CryIA-type ICPs
    • Martínez-Ramírez, A. C., S. González-Nebauer, B. Escriche, and M. D. Real. 1994. Ligand blot identification of a Manduca sexta midgut binding protein specific to three Bacillus thuringiensis CryIA-type ICPs. Biochem. Biophys. Res. Commun. 201:782-787.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 782-787
    • Martínez-Ramírez, A.C.1    González-Nebauer, S.2    Escriche, B.3    Real, M.D.4
  • 41
    • 0028150717 scopus 로고
    • Specificity domain localization of Bacillus thuringiensis insecticidal toxins is highly dependent on the bioassay system
    • Masson, L., A. Mazza, L. Gringorten, D. Baines, V. Aneliunas, and R. Brousseau. 1994. Specificity domain localization of Bacillus thuringiensis insecticidal toxins is highly dependent on the bioassay system. Mol. Microbiol. 14:851-860.
    • (1994) Mol. Microbiol. , vol.14 , pp. 851-860
    • Masson, L.1    Mazza, A.2    Gringorten, L.3    Baines, D.4    Aneliunas, V.5    Brousseau, R.6
  • 42
    • 0025281654 scopus 로고
    • Comparative analysis of the individual protoxin components in P1 crystals of Bacillus thuringiensis subsp. kurstaki isolates NRD-12 and HD-1
    • Masson, L., G. Préfontaine, L. Péloquin, P. C. K. Lau, and R. Brousseau. 1989. Comparative analysis of the individual protoxin components in P1 crystals of Bacillus thuringiensis subsp. kurstaki isolates NRD-12 and HD-1. Biochem. J. 269:507-512.
    • (1989) Biochem. J. , vol.269 , pp. 507-512
    • Masson, L.1    Préfontaine, G.2    Péloquin, L.3    Lau, P.C.K.4    Brousseau, R.5
  • 43
    • 0035498897 scopus 로고    scopus 로고
    • Processing of Cry1Ab δ-endotoxin from Bacillus thuringiensis by Manduca sexta and Spodoptera frugiperda midgut proteases: Role in protoxin activation and toxin inactivation
    • Miranda, R., F. Z. Zamudio, and A. Bravo. 2001. Processing of Cry1Ab δ-endotoxin from Bacillus thuringiensis by Manduca sexta and Spodoptera frugiperda midgut proteases: role in protoxin activation and toxin inactivation. Insect Biochem. Mol. Biol. 31:1155-1163.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 1155-1163
    • Miranda, R.1    Zamudio, F.Z.2    Bravo, A.3
  • 44
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • Morse, R. J., T. Yamamoto, and R. M. Stroud. 2001. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure 9:409-417.
    • (2001) Structure , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 45
    • 0024722507 scopus 로고
    • Evidence for two different types of insecticidal P2 toxins with dual specificity in Bacillus thuringiensis subspecies
    • Nichols, C. N., W. Ahmad, and D. J. Ellar. 1989. Evidence for two different types of insecticidal P2 toxins with dual specificity in Bacillus thuringiensis subspecies. J. Bacteriol. 171:5141-5147.
    • (1989) J. Bacteriol. , vol.171 , pp. 5141-5147
    • Nichols, C.N.1    Ahmad, W.2    Ellar, D.J.3
  • 46
    • 0026914204 scopus 로고
    • Processing of δ-endotoxin from Bacillus thuringiensis subsp. kurstaki HD-1 and HD-73 by gut juices of various insect larvae
    • Ogiwara, K., L. S. Indrasith, S. Asano, and H. Hori. 1992. Processing of δ-endotoxin from Bacillus thuringiensis subsp. kurstaki HD-1 and HD-73 by gut juices of various insect larvae. J. Invertebr. Pathol. 60:121-126.
    • (1992) J. Invertebr. Pathol. , vol.60 , pp. 121-126
    • Ogiwara, K.1    Indrasith, L.S.2    Asano, S.3    Hori, H.4
  • 47
    • 0031725639 scopus 로고    scopus 로고
    • Degradation of Bacillus thuringiensis δ-endotoxin in host insect gut juice
    • Pang, A. S. D., and J. L. Gringorten. 1998. Degradation of Bacillus thuringiensis δ-endotoxin in host insect gut juice. FEMS Microbiol. Lett. 167:281-285.
    • (1998) FEMS Microbiol. Lett. , vol.167 , pp. 281-285
    • Pang, A.S.D.1    Gringorten, J.L.2
  • 48
    • 0033305864 scopus 로고    scopus 로고
    • Activation and fragmentation of Bacillus thuringiensis δ-endotoxin by high concentrations of proteolytic enzymes
    • Pang, A. S. D., J. L. Gringorten, and C. Bai. 1999. Activation and fragmentation of Bacillus thuringiensis δ-endotoxin by high concentrations of proteolytic enzymes. Can. J. Microbiol. 45:816-825.
    • (1999) Can. J. Microbiol. , vol.45 , pp. 816-825
    • Pang, A.S.D.1    Gringorten, J.L.2    Bai, C.3
  • 50
    • 11544370262 scopus 로고
    • Potentiation of Bacillus thuringiensis endotoxin against the greasy cutworm Agrotis ypsilon
    • Salama, H. S., M. S. Foda, and A. Sharaby. 1989. Potentiation of Bacillus thuringiensis endotoxin against the greasy cutworm Agrotis ypsilon. J. Appl. Entomol. 108:372-380.
    • (1989) J. Appl. Entomol. , vol.108 , pp. 372-380
    • Salama, H.S.1    Foda, M.S.2    Sharaby, A.3
  • 51
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • R. J. Beynon and J. S. Bond (ed.). IRL Press, Oxford, United Kingdom
    • Salvesen, G., and H. Nagase. 1989. Inhibition of proteolytic enzymes, pp. 83-104. In R. J. Beynon and J. S. Bond (ed.), Proteolytic enzymes: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Proteolytic Enzymes: A Practical Approach , pp. 83-104
    • Salvesen, G.1    Nagase, H.2
  • 53
    • 0001244705 scopus 로고
    • Direct evidence for the presence of histidine in the active center of chymotrypsin
    • Schoellmann, G., and E. Shaw. 1963. Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry 2:252-255.
    • (1963) Biochemistry , vol.2 , pp. 252-255
    • Schoellmann, G.1    Shaw, E.2
  • 55
    • 0032111202 scopus 로고    scopus 로고
    • Processing of δ-endotoxin of Bacillus thuringiensis subsp. kurstaki HD-1 in Heliothis armigera midgut juice and the effects of protease inhibitors
    • Shao, Z., Y. Cui, X. Liu, H. Yi, J. Ji, and Z. Yu. 1998. Processing of δ-endotoxin of Bacillus thuringiensis subsp. kurstaki HD-1 in Heliothis armigera midgut juice and the effects of protease inhibitors. J. Invertebr. Pathol. 72:73-81.
    • (1998) J. Invertebr. Pathol. , vol.72 , pp. 73-81
    • Shao, Z.1    Cui, Y.2    Liu, X.3    Yi, H.4    Ji, J.5    Yu, Z.6
  • 57
    • 0001199351 scopus 로고
    • Two protease inhibitors fail to synergize Bacillus thuringiensis in diamondback moth (Lepidoptera: Plutellidae)
    • Tabashnik, B. E., N. Finson, and M. W. Johnson. 1992. Two protease inhibitors fail to synergize Bacillus thuringiensis in diamondback moth (Lepidoptera: Plutellidae). J. Econ. Entomol. 85:2082-2087.
    • (1992) J. Econ. Entomol. , vol.85 , pp. 2082-2087
    • Tabashnik, B.E.1    Finson, N.2    Johnson, M.W.3
  • 58
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra, W. R., and C. Ferreira. 1994. Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109B:1-62.
    • (1994) Comp. Biochem. Physiol. , vol.109 , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 59
    • 0035486813 scopus 로고    scopus 로고
    • Differential effects of pH on the pore-forming properties of Bacillus thuringiensis insecticidal toxins
    • Tran, L. B., V. Vachon, J.-L. Schwartz, and R. Laprade. 2001. Differential effects of pH on the pore-forming properties of Bacillus thuringiensis insecticidal toxins. Appl. Environ. Microbiol. 67:4488-4494.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4488-4494
    • Tran, L.B.1    Vachon, V.2    Schwartz, J.-L.3    Laprade, R.4
  • 61
    • 0025688063 scopus 로고
    • A novel Bacillus thuringiensis gene encoding a Spodoptera exigua-specific crystal protein
    • Visser, B., E. Munsterman, A. Stoker, and W. G. Dirkse. 1990. A novel Bacillus thuringiensis gene encoding a Spodoptera exigua-specific crystal protein. J. Bacteriol. 172:6783-6788.
    • (1990) J. Bacteriol. , vol.172 , pp. 6783-6788
    • Visser, B.1    Munsterman, E.2    Stoker, A.3    Dirkse, W.G.4
  • 62
    • 0001382744 scopus 로고
    • Genes from Bacillus thuringiensis entomocidus 60.5 coding for insect-specific crystal proteins
    • Visser, B., T. Van der Salm, W. Van den Brink, and G. Folkers. 1988. Genes from Bacillus thuringiensis entomocidus 60.5 coding for insect-specific crystal proteins. Mol. Gen. Genet. 212:219-224.
    • (1988) Mol. Gen. Genet. , vol.212 , pp. 219-224
    • Visser, B.1    Van Der Salm, T.2    Van Den Brink, W.3    Folkers, G.4
  • 63
    • 84990462079 scopus 로고
    • Neither barium nor calcium prevents the inhibition by Bacillus thuringiensis δ-endotoxin of sodium- Or potassium gradient-dependent amino acid accumulation by tobacco hornworm midgut brush border membrane vesicles
    • Wolfersberger, M. G. 1989. Neither barium nor calcium prevents the inhibition by Bacillus thuringiensis δ-endotoxin of sodium- or potassium gradient-dependent amino acid accumulation by tobacco hornworm midgut brush border membrane vesicles. Arch. Insect Biochem. Physiol. 12:267-277.
    • (1989) Arch. Insect Biochem. Physiol. , vol.12 , pp. 267-277
    • Wolfersberger, M.G.1
  • 64
    • 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., P. Luethy, A. Maurer, P. Parenti, F. V. Sacchi, B. Giordana, and G. M. Hanozet. 1987. Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae). Comp. Biochem. Physiol. 86A:301-308.
    • (1987) Comp. Biochem. Physiol. , 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
  • 65
    • 0000128089 scopus 로고
    • Diversity in digestive proteinase activity among insects
    • Wolfson, J. L., and L. L. Murdock. 1990. Diversity in digestive proteinase activity among insects. J. Chem. Ecol. 16:1089-1102.
    • (1990) J. Chem. Ecol. , vol.16 , pp. 1089-1102
    • Wolfson, J.L.1    Murdock, L.L.2
  • 66
    • 0032793534 scopus 로고    scopus 로고
    • Activation process of dipteran-specific insecticidal protein produced by Bacillus thuringiensis subsp. israelensis
    • Yamagiwa, M., M. Esaki, K. Otake, M. Inagaki, T. Komano, T. Amachi, and H. Sakai. 1999. Activation process of dipteran-specific insecticidal protein produced by Bacillus thuringiensis subsp. israelensis. Appl. Environ. Microbiol. 65:3464-3469.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3464-3469
    • Yamagiwa, M.1    Esaki, M.2    Otake, K.3    Inagaki, M.4    Komano, T.5    Amachi, T.6    Sakai, H.7
  • 67
    • 0036490818 scopus 로고    scopus 로고
    • Active form of dipteran-specific insecticidal protein Cry11A produced by Bacillus thuringiensis subsp. israelensis
    • Yamagiwa, M., R. Ogawa, K. Yasuda, H. Natsuyama, K. Sen, and H. Sakai. 2002. Active form of dipteran-specific insecticidal protein Cry11A produced by Bacillus thuringiensis subsp. israelensis. Biosci. Biotechnol. Biochem. 66:516-522.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 516-522
    • Yamagiwa, M.1    Ogawa, R.2    Yasuda, K.3    Natsuyama, H.4    Sen, K.5    Sakai, H.6
  • 68
    • 0031826689 scopus 로고    scopus 로고
    • Limited proteolysis of Bacillus thuringiensis Cry1G and CryIVB δ-endotoxins leads to formation of active fragments that do not coincide with the structural domains
    • Zalunin, I. A., L. P. Revina, L. I. Kostina, G. G. Chestukhina, and V. M. Stepanov. 1998. Limited proteolysis of Bacillus thuringiensis Cry1G and CryIVB δ-endotoxins leads to formation of active fragments that do not coincide with the structural domains. J. Protein Chem. 17:463-471.
    • (1998) J. Protein Chem. , vol.17 , pp. 463-471
    • Zalunin, I.A.1    Revina, L.P.2    Kostina, L.I.3    Chestukhina, G.G.4    Stepanov, V.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.