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Volumn 28, Issue 12, 1998, Pages 1013-1023

Spruce budworm elastase precipitates Bacillus thuringiensis δ-endotoxin by specifically recognizing the C-terminal region

Author keywords

Bacillus thuringiensis; Choristoneura fumiferana; Delta endotoxin; Elastase; Gut juice; Resistance; Spruce budworm; Toxin precipitation

Indexed keywords

BACILLUS THURINGIENSIS CRYSTAL PROTEIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; CARBON; DODECYL SULFATE SODIUM; ELASTASE; ENDOTOXIN; INSECT PROTEIN; PANCREATIC ELASTASE; SEPHAROSE;

EID: 0032407476     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00090-3     Document Type: Article
Times cited : (18)

References (38)
  • 1
    • 0027328978 scopus 로고
    • Structural stability of Bacillus thuringiensis delta-endotoxin homolog-scanning mutants determined by susceptibility to proteases
    • Almond B., Dean D.H. Structural stability of Bacillus thuringiensis delta-endotoxin homolog-scanning mutants determined by susceptibility to proteases. Appl. Environ. Microbiol. 59:1993;2442-2448.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2442-2448
    • Almond, B.1    Dean, D.H.2
  • 2
    • 0000205368 scopus 로고
    • Extraction purification and properties of Bacillus sotto toxin
    • Angus T.A. Extraction purification and properties of Bacillus sotto toxin. Can. J. Microbiol. 2:1956;416-426.
    • (1956) Can. J. Microbiol. , vol.2 , pp. 416-426
    • Angus, T.A.1
  • 3
    • 0002896738 scopus 로고
    • Peritrophic envelope permeability in herbivorous insects
    • Barbehenn R.V., Martin M.M. Peritrophic envelope permeability in herbivorous insects. J. Insect Physiol. 41:1995;303-311.
    • (1995) J. Insect Physiol. , vol.41 , pp. 303-311
    • Barbehenn, R.V.1    Martin, M.M.2
  • 4
    • 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
  • 8
    • 0013533441 scopus 로고
    • The insecticidal specificity and toxicity of Bacillus thuringiensis delta-endotoxins may be determined respectively by an initial binding to membrane-specific receptors followed by a common mechanism of cytolysis
    • In: Samson, R.A. (Ed.)
    • Ellar, D., Knowles, B., Drobniewski, F., Haider, M., 1986. The insecticidal specificity and toxicity of Bacillus thuringiensis delta-endotoxins may be determined respectively by an initial binding to membrane-specific receptors followed by a common mechanism of cytolysis. In: Samson, R.A. (Ed.), Fundamental and Applied Aspects of Invertebrate Pathology. Foundation of the Fourth Intl Colloquim of Invertebrate Pathology, pp. 7-10.
    • (1986) Fundamental and Applied Aspects of Invertebrate Pathology. Foundation of the Fourth Intl Colloquim of Invertebrate Pathology , pp. 7-10
    • Ellar, D.1    Knowles, B.2    Drobniewski, F.3    Haider, M.4
  • 9
    • 0002223959 scopus 로고
    • The crystal toxin of Bacillus thuringiensis
    • In: Burges, H.D. (Ed.), Academic Press, New York
    • Fast, P.G., 1981. The crystal toxin of Bacillus thuringiensis. In: Burges, H.D. (Ed.), Microbial Control of Pests and Plant Diseases 1970-1980. Academic Press, New York, pp. 223-248.
    • (1981) Microbial Control of Pests and Plant Diseases 1970-1980 , pp. 223-248
    • Fast, P.G.1
  • 10
    • 0030612375 scopus 로고    scopus 로고
    • Further characterization of BT-R-1, the cadherin-like receptor for Cry1Ab toxin in tobacco hornworm (Manduca sexta) midguts
    • Francis B.R., Bulla L.A.J. Further characterization of BT-R-1, the cadherin-like receptor for Cry1Ab toxin in tobacco hornworm (Manduca sexta) midguts. Insect Biochem. Molec. Biol. 27:1997;541-550.
    • (1997) Insect Biochem. Molec. Biol. , vol.27 , pp. 541-550
    • Francis, B.R.1    Bulla, L.A.J.2
  • 11
    • 0025949194 scopus 로고
    • Functional domains of bacillus thuringiensis insecticidal crystal proteins
    • Ge A.Z., Rivers D., Milne R., Dean D. Functional domains of bacillus thuringiensis insecticidal crystal proteins. J. Biol. Chem. 266:1991;17954-17958.
    • (1991) J. Biol. Chem , vol.266 , pp. 17954-17958
    • Ge, A.Z.1    Rivers, D.2    Milne, R.3    Dean, D.4
  • 12
    • 0024687823 scopus 로고
    • Location of the Bombyx mori specificity domain on a Bacillus thuringiensis δ-endotoxin protein
    • Ge A.Z., Shivarova N.I., Dean D.H. Location of the Bombyx mori specificity domain on a Bacillus thuringiensis δ-endotoxin protein. Proc. Natl. Acad. Sci. 86:1989;4037-4041.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 4037-4041
    • Ge, A.Z.1    Shivarova, N.I.2    Dean, D.H.3
  • 13
    • 0001276188 scopus 로고
    • A laboratory method for mass rearing the eastern spruce budworm, Choristoneura fumiferana
    • In: King, E.G., Leppla, N.C. (Eds.), U.S.D.A. Technical Bulletin
    • Grisdale, D.G. (1984) A laboratory method for mass rearing the eastern spruce budworm, Choristoneura fumiferana. In: King, E.G., Leppla, N.C. (Eds.), Advances and Challenges in Insect Rearing. U.S.D.A. Technical Bulletin, pp. 223-231.
    • (1984) Advances and Challenges in Insect Rearing , pp. 223-231
    • Grisdale, D.G.1
  • 15
    • 0001247484 scopus 로고
    • Inhibition of the proteinase and esterase activity of trypsin and chymotrypsin by diisopropyl fluorophosphate: Crystallization of the inhibited chymotrypsin
    • Jansen, E., Fellows-Nutting, M., Jang, Balls, A., 1949. Inhibition of the proteinase and esterase activity of trypsin and chymotrypsin by diisopropyl fluorophosphate: crystallization of the inhibited chymotrypsin. J. Biol. Chem. 179, 189-199.
    • (1949) J. Biol. Chem. , vol.179 , pp. 189-199
    • Jansen, E.1    Fellows-Nutting, M.2    Jang Balls, A.3
  • 16
    • 0028291484 scopus 로고
    • The receptor for bacillus thuringiensis Cry1A(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N
    • Knight P.K., Crickmore N., Ellar D.J. The receptor for bacillus thuringiensis Cry1A(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N. Molec. Microbiol. 11(3):1994;429-436.
    • (1994) Molec. Microbiol. , vol.11 , Issue.3 , pp. 429-436
    • Knight, P.K.1    Crickmore, N.2    Ellar, D.J.3
  • 17
    • 0025871617 scopus 로고
    • N-acetyl galactosamine is part of the receptor in the insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis
    • Knowles B.H., Knight P.K., Ellar D.J. N-acetyl galactosamine is part of the receptor in the insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis. Proc. R. Soc. Lond. B. 245:1991;31-35.
    • (1991) Proc. R. Soc. Lond. B , vol.245 , pp. 31-35
    • Knowles, B.H.1    Knight, P.K.2    Ellar, D.J.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0028846881 scopus 로고
    • Domain III exchanges of Bacillus thuringiensis CryIA toxins affect binding to different gypsy moth midgut receptors
    • Lee M.K., Young B.A., And Dean D.H. Domain III exchanges of Bacillus thuringiensis CryIA toxins affect binding to different gypsy moth midgut receptors. Biochem. Biophys. Res. Comm. 216:1995;306-312.
    • (1995) Biochem. Biophys. Res. Comm. , vol.216 , pp. 306-312
    • Lee, M.K.1    Young, B.A.2    Dean, D.H.3
  • 20
    • 0030059352 scopus 로고    scopus 로고
    • Conversion of Bacillus thuringiensis Cry1ac-binding aminopeptidase to a soluble form by endogenous phosphatidylinositol phospholipase c
    • Lu Y., Adang M.J. Conversion of Bacillus thuringiensis Cry1ac-binding aminopeptidase to a soluble form by endogenous phosphatidylinositol phospholipase c. Insect Biochem. Mol. Biol. 26:1996;33-40.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 33-40
    • Lu, Y.1    Adang, M.J.2
  • 21
    • 0029017728 scopus 로고
    • Kinetics of Bacillus thuringiensis toxin binding with brush border membrane vesicles from susceptible and resistant larvae of Plutella xylostella
    • Masson L., Mazza A., Brousseau R., Tabashnik B. Kinetics of Bacillus thuringiensis toxin binding with brush border membrane vesicles from susceptible and resistant larvae of Plutella xylostella. J. Biol. Chem. 270:1995;11887-11896.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11887-11896
    • Masson, L.1    Mazza, A.2    Brousseau, R.3    Tabashnik, B.4
  • 23
    • 0027661652 scopus 로고
    • Purification and characterization of trypsin-like digestive enzyme from spruce budworm Choristoneura fumiferana responsible for the activation of delta endotoxin from Bacillus thuringiensis
    • Milne R., Kaplan H. Purification and characterization of trypsin-like digestive enzyme from spruce budworm Choristoneura fumiferana responsible for the activation of delta endotoxin from Bacillus thuringiensis. Insect Biochem. Mol. Biol. 23:1993;663-673.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 663-673
    • Milne, R.1    Kaplan, H.2
  • 24
    • 0029582685 scopus 로고
    • A protein complex from Choristoneura fumiferana gut-juice involved in the precipitation of delta-endotoxin from Bacillus thuringiensis subsp. sotto
    • Milne R.E., Pang A.S.D., Kaplan H. A protein complex from Choristoneura fumiferana gut-juice involved in the precipitation of delta-endotoxin from Bacillus thuringiensis subsp. sotto. Insect Biochem. Molec. Biol. 25:1995;1101-1114.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 1101-1114
    • Milne, R.E.1    Pang, A.S.D.2    Kaplan, H.3
  • 25
    • 0025933034 scopus 로고
    • Identification and characterization of Heliothis virescens midgut membrane proteins binding Bacillus thuringiensis
    • Oddou P., Hartman H., Geiser M. Identification and characterization of Heliothis virescens midgut membrane proteins binding Bacillus thuringiensis. Eur. J. Biochem. 202:1991;673-680.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 673-680
    • Oddou, P.1    Hartman, H.2    Geiser, M.3
  • 26
    • 0026033079 scopus 로고
    • Peptide mapping of different Bacillus thuringiensis toxin gene products by CNBr cleavage in SDS-PAGE gels
    • Pang A.D., Mathieson B. Peptide mapping of different Bacillus thuringiensis toxin gene products by CNBr cleavage in SDS-PAGE gels. J. Invertebr. Pathol. 57:1991;82-93.
    • (1991) J. Invertebr. Pathol. , vol.57 , pp. 82-93
    • Pang, A.D.1    Mathieson, B.2
  • 27
    • 0000787375 scopus 로고
    • The serological properties of simple substances. VI. The precipitation of a mixture of two specific antisera by a dihaptenic substance containing the two corresponding haptenic groups; evidence for the framework theory of serological precipitation
    • Pauling, L., Pressman, D., Campbell, 1944. The serological properties of simple substances. VI. The precipitation of a mixture of two specific antisera by a dihaptenic substance containing the two corresponding haptenic groups; evidence for the framework theory of serological precipitation. J. Am. Chem. Soc. 66, 330-336.
    • (1944) J. Am. Chem. Soc. , vol.66 , pp. 330-336
    • Pauling, L.1    Pressman, D.2    Campbell3
  • 28
    • 0027393296 scopus 로고
    • Identification and partial purification of a Bacillus thuringiensis Cry1C delta-endotoxin binding protein from Spodoptera littoralis gut membranes
    • Sanchis V., Ellar D.J. Identification and partial purification of a Bacillus thuringiensis Cry1C delta-endotoxin binding protein from Spodoptera littoralis gut membranes. FEBS. Lett. 316:1993;264-268.
    • (1993) FEBS. Lett. , vol.316 , pp. 264-268
    • Sanchis, V.1    Ellar, D.J.2
  • 29
    • 0028177991 scopus 로고
    • A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal Cry1A(c) toxin binding and 86Rb-K efflux in vitro
    • Sangadala S., Walters F., English L.H., Adang M.J. A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal Cry1A(c) toxin binding and 86Rb-K efflux in vitro. J. Biol. Chem. 269:1994;10088-10092.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10088-10092
    • Sangadala, S.1    Walters, F.2    English, L.H.3    Adang, M.J.4
  • 30
    • 0000170190 scopus 로고
    • Distribution and characterization of the oligomeric digestive enzymes from Erinnyis ello larvae and inferences concerning secretory mechanisms and permeability of the peritrophic membrane
    • Santos C.D., Terra W.R. Distribution and characterization of the oligomeric digestive enzymes from Erinnyis ello larvae and inferences concerning secretory mechanisms and permeability of the peritrophic membrane. Insect Biochem. 16:1986;691-700.
    • (1986) Insect Biochem. , vol.16 , pp. 691-700
    • Santos, C.D.1    Terra, W.R.2
  • 31
    • 0002900650 scopus 로고
    • Protease assay methods
    • In: Beynon, R.J., Bond, J.S. (Eds.), Oxford University Press, New York
    • Sarath, G., De La Motte, R.S., Wagner, F.W., 1989. Protease assay methods. In: Beynon, R.J., Bond, J.S. (Eds.), Proteolytic Enzymes. Oxford University Press, New York, pp. 25-55.
    • (1989) Proteolytic Enzymes , pp. 25-55
    • Sarath, G.1    De La Motte, R.S.2    Wagner, F.W.3
  • 32
    • 0343196687 scopus 로고    scopus 로고
    • Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors
    • Schwartz J., Lu Y., Sohnlein P., Brousseau R., Laprade R., Masson L., Adang M.J. Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors. FEBS. Lett. 412:1997;270-276.
    • (1997) FEBS. Lett. , vol.412 , pp. 270-276
    • Schwartz, J.1    Lu, Y.2    Sohnlein, P.3    Brousseau, R.4    Laprade, R.5    Masson, L.6    Adang, M.J.7
  • 33
    • 0027258633 scopus 로고
    • A specific binding protein from Manduca sexta for the insecticidal toxin of Bacillus thuringiensis subsp. berliner
    • Vadlamudi R.K., Tae H.J., Bulla L.A. A specific binding protein from Manduca sexta for the insecticidal toxin of Bacillus thuringiensis subsp. berliner. J. Biol. Chem. 268:1993;12334-12340.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12334-12340
    • Vadlamudi, R.K.1    Tae, H.J.2    Bulla, L.A.3
  • 34
    • 0028907322 scopus 로고
    • Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis
    • Vadlamudi R.K., Weber E., Ji I., Ji T.H., Bulla L.A. Jr. Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis. J. Biol. Chem. 270:1995;5490-5494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5490-5494
    • Vadlamudi, R.K.1    Weber, E.2    Ji, I.3    Ji, T.H.4    Bulla L.A., Jr.5
  • 35
    • 0029584379 scopus 로고
    • Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as the receptor for the Cry1A(c) delta-endotoxin of Bacillus thuringiensis
    • Valaitis A.P., Lee M.K., Rajamohan F., Dean D.H. Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as the receptor for the Cry1A(c) delta-endotoxin of Bacillus thuringiensis. Insect Biochem. Molec. Biol. 25:1995;1143-1151.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 1143-1151
    • Valaitis, A.P.1    Lee, M.K.2    Rajamohan, F.3    Dean, D.H.4
  • 36
    • 0030022109 scopus 로고    scopus 로고
    • Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin Cry1Aa affect is ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles
    • Wolfersberger M.G., Chen X.J., Dean D.H. Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin Cry1Aa affect is ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles. Appl. Environ. Microbiol. 62:1996;279-282.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 279-282
    • Wolfersberger, M.G.1    Chen, X.J.2    Dean, D.H.3
  • 37
    • 0013538319 scopus 로고
    • Permeability of the peritrophic membrane of the tobacco hornworm larval midgut
    • Wolfersberger M.G., Spaeth D.D., Dow J.A.T. Permeability of the peritrophic membrane of the tobacco hornworm larval midgut. Amer. Zool. 26:1986;74A.
    • (1986) Amer. Zool. , vol.26
    • Wolfersberger, M.G.1    Spaeth, D.D.2    Dow, J.A.T.3
  • 38
    • 0030902706 scopus 로고    scopus 로고
    • A change in a single midgut receptor in the diamondback moth (Plutella xylostella) is only in part responsible for field resistance to Bacillus thuringiensis subsp. kurstaki and B. thuringiensis subsp. aizawai
    • Wright D.J., Iqbal M., Granero F., Ferre J. A change in a single midgut receptor in the diamondback moth (Plutella xylostella) is only in part responsible for field resistance to Bacillus thuringiensis subsp. kurstaki and B. thuringiensis subsp. aizawai. Appl. Environ. Microbiol. 63:1997;1814-1819.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1814-1819
    • Wright, D.J.1    Iqbal, M.2    Granero, F.3    Ferre, J.4


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