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Volumn 71, Issue 7, 2005, Pages 3966-3977

Location of the Bombyx mori aminopeptidase N type 1 binding site on Bacillus thuringiensis Cry1Aa toxin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; BACTERIA; BINDING ENERGY; MAPPING; MICROBIOLOGY;

EID: 22144493370     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.7.3966-3977.2005     Document Type: Article
Times cited : (51)

References (78)
  • 1
    • 0027328978 scopus 로고
    • Structural stability of Bacillus thuringiensis δ-endotoxin homolog-scanning mutants determined by susceptibility to proteases
    • Almond, B. D., and D. H. Dean. 1993. Structural stability of Bacillus thuringiensis δ-endotoxin homolog-scanning mutants determined by susceptibility to proteases. Appl. Environ. Microbiol. 59:2442-2448.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2442-2448
    • Almond, B.D.1    Dean, D.H.2
  • 2
    • 0029048940 scopus 로고
    • Mutagenesis of specificity and toxicity regions of a Bacillus thuringiensis protoxin gene
    • Aronson, A. I., D. Wu, and C. Zhang. 1995. Mutagenesis of specificity and toxicity regions of a Bacillus thuringiensis protoxin gene. J. Bacteriol. 177:4059-4065.
    • (1995) J. Bacteriol. , vol.177 , pp. 4059-4065
    • Aronson, A.I.1    Wu, D.2    Zhang, C.3
  • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0033574601 scopus 로고    scopus 로고
    • N-Acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin
    • Burton, S. L., D. J. Ellar, J. Li, and D. J. Derbyshire. 1999. N-Acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin. J. Mol. Biol. 287:1011-1022.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1011-1022
    • Burton, S.L.1    Ellar, D.J.2    Li, J.3    Derbyshire, D.J.4
  • 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., A. Curtiss, E. Alcantara, and D. H. Dean. 1995. 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. 270:6412-6419.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6412-6419
    • Chen, X.J.1    Curtiss, A.2    Alcantara, E.3    Dean, D.H.4
  • 6
    • 0027359047 scopus 로고
    • Site-directed mutations in a highly conserved region of Bacillus thuringiensis δ-endotoxin affect inhibition of short circuit current across Bombyx mori midguts
    • Chen, X. J., M. K. Lee, and D. H. Dean. 1993. Site-directed mutations in a highly conserved region of Bacillus thuringiensis δ-endotoxin affect inhibition of short circuit current across Bombyx mori midguts. Proc. Natl. Acad. Sci. USA 90:9041-9045.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9041-9045
    • Chen, X.J.1    Lee, M.K.2    Dean, D.H.3
  • 8
    • 0029930607 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis δ-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition
    • de Maagd, R. A., M. S. G. Kwa, H. van der Klei, T. Yamamoto, B. Schipper, and J. M. Vlak. 1996. Domain III substitution in Bacillus thuringiensis δ-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition. Appl. Environ. Microbiol. 62:1537-1543.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1537-1543
    • Maagd, R.A.1    Kwa, M.S.G.2    Van Der Klei, H.3    Yamamoto, T.4    Schipper, B.5    Vlak, J.M.6
  • 9
    • 0034114535 scopus 로고    scopus 로고
    • Bacillus thuringiensis δ-endotoxin Cry1C domain III can function as a specificity determinant for Spodoptera exigua in different, but not all, Cry1-Cry1C hybrids
    • de Maagd, R. A., M. Weemen-Hendriks, W. Stiekema, and D. Bosch. 2000. Bacillus thuringiensis δ-endotoxin Cry1C domain III can function as a specificity determinant for Spodoptera exigua in different, but not all, Cry1-Cry1C hybrids. Appl. Environ. Microbiol. 66:1559-1563.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1559-1563
    • De Maagd, R.A.1    Weemen-Hendriks, M.2    Stiekema, W.3    Bosch, D.4
  • 10
    • 0032937987 scopus 로고    scopus 로고
    • Domain III of the Bacillus thuringiensis δ-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N
    • de Maagd, R. A., P. L. Bakker, L. Masson, M. J. Adang, S. Sangadala, W. Stiekema, and D. Bosch. 1999. Domain III of the Bacillus thuringiensis δ-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N. Mol. Microbiol. 31:463-471.
    • (1999) Mol. Microbiol. , vol.31 , pp. 463-471
    • Maagd, R.A.1    Bakker, P.L.2    Masson, L.3    Adang, M.J.4    Sangadala, S.5    Stiekema, W.6    Bosch, D.7
  • 11
    • 0030767349 scopus 로고    scopus 로고
    • Cloning and characterization of Manduca sexta and Plutella xylostella midgut aminopeptidase N enzymes related to Bacillus thuringiensis toxin binding proteins
    • Denolf, P., K. Hendrickx, J. Vandamme, S. Jansens, M. Peferoen, D. Degheele, and J. van Rie. 1997. Cloning and characterization of Manduca sexta and Plutella xylostella midgut aminopeptidase N enzymes related to Bacillus thuringiensis toxin binding proteins. Eur. J. Biochem. 248:748-761.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 748-761
    • Denolf, P.1    Hendrickx, K.2    Vandamme, J.3    Jansens, S.4    Peferoen, M.5    Degheele, D.6    Van Rie, J.7
  • 12
    • 0035800472 scopus 로고    scopus 로고
    • Identification of a gene associated with Bt resistance in Heliothis virescens
    • Gahan, L. J., F. Gould, and D. G. Heckel. 2001. Identification of a gene associated with Bt resistance in Heliothis virescens. Science 293:857-860.
    • (2001) Science , vol.293 , pp. 857-860
    • Gahan, L.J.1    Gould, F.2    Heckel, D.G.3
  • 13
    • 0017769048 scopus 로고
    • Antibodies to major histocompatibility antigens produced by hybrid cell lines
    • Galfre, G., S. C. Howe, C. Milstein, G. W. Butcher, and J. C. Howard. 1977. Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature 266:550-552.
    • (1977) Nature , vol.266 , pp. 550-552
    • Galfre, G.1    Howe, S.C.2    Milstein, C.3    Butcher, G.W.4    Howard, J.C.5
  • 15
    • 0025948489 scopus 로고
    • Identification of putative insect brush border membrane-binding molecules specific to Bacillus thuringiensis δ-endotoxin by protein blot analysis
    • Garczynski, S. F., J. W. Crim, and M. J. Adang. 1991. Identification of putative insect brush border membrane-binding molecules specific to Bacillus thuringiensis δ-endotoxin by protein blot analysis. Appi. Environ. Microbiol. 57:2816-2820.
    • (1991) Appi. Environ. Microbiol. , vol.57 , pp. 2816-2820
    • Garczynski, S.F.1    Crim, J.W.2    Adang, M.J.3
  • 16
    • 0025949194 scopus 로고
    • Functional domains of Bacillus thuringiensis insecticidal crystal proteins
    • Ge, A. Z., D. Rivers, R. Milne, and D. H. Dean. 1991. Functional domains of Bacillus thuringiensis insecticidal crystal proteins. J. Biol. Chem. 266:17954-17958.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17954-17958
    • Ge, A.Z.1    Rivers, D.2    Milne, R.3    Dean, D.H.4
  • 17
    • 0022870838 scopus 로고
    • The hypervariable region in the genes coding for entomopathogenic crystal proteins of Bacillus thuringiensis: Nucleotide sequence of the kurhd1 gene of subsp. kurstaki HD1
    • Geiser, M., S. Schweitzer, and C. Grimm. 1986. The hypervariable region in the genes coding for entomopathogenic crystal proteins of Bacillus thuringiensis: nucleotide sequence of the kurhd1 gene of subsp. kurstaki HD1. Gene 48:109-118.
    • (1986) Gene , vol.48 , pp. 109-118
    • Geiser, M.1    Schweitzer, S.2    Grimm, C.3
  • 18
    • 0000951677 scopus 로고
    • Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
    • Geysen, H. M., R. H. Meloen, and S. J. Barteling. 1984. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. USA 81:3998-4002.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3998-4002
    • Geysen, H.M.1    Meloen, R.H.2    Barteling, S.J.3
  • 19
    • 0036899846 scopus 로고    scopus 로고
    • Transgenic Drosophila reveals a functional in vivo receptor for the Bacillus thuringiensis toxin Cry1Ac1
    • Gill, M., and D. J. Ellar. 2002. Transgenic Drosophila reveals a functional in vivo receptor for the Bacillus thuringiensis toxin Cry1Ac1. Insect Mol. Biol. 11:619-625.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 619-625
    • Gill, M.1    Ellar, D.J.2
  • 20
    • 0028875319 scopus 로고
    • Identification, isolation, and cloning of a Bacillus thuringiensis Cry1Ac toxin-binding protein from the midgut of the lepidopteran insect Heliothis virescens
    • Gill, S. S., E. A. Cowles, and V. Francis. 1995. Identification, isolation, and cloning of a Bacillus thuringiensis Cry1Ac toxin-binding protein from the midgut of the lepidopteran insect Heliothis virescens. J. Biol. Chem. 270:27277-27282.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27277-27282
    • Gill, S.S.1    Cowles, E.A.2    Francis, V.3
  • 21
    • 0026478141 scopus 로고
    • The mode of action of Bacillus thuringiensis endotoxins
    • Gill, S. S., E. A. Cowles, and P. V. Pietrantonio. 1992. The mode of action of Bacillus thuringiensis endotoxins. Annu. Rev. Entomol. 37:615-636.
    • (1992) Annu. Rev. Entomol. , vol.37 , pp. 615-636
    • Gill, S.S.1    Cowles, E.A.2    Pietrantonio, P.V.3
  • 22
    • 0019165436 scopus 로고
    • Antibody production by hybridomas
    • Goding, J. W. 1980. Antibody production by hybridomas. J. Immunol. Methods 39:285-308.
    • (1980) J. Immunol. Methods , vol.39 , pp. 285-308
    • Goding, J.W.1
  • 23
    • 0037119455 scopus 로고    scopus 로고
    • Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins
    • Gomez, I., J. Miranda-Rios, E. Rudido-Pinera, D. I. Oltean, S. S. Gill, A. Bravo, and M. Soberon. 2002. Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins. J. Biol. Chem. 277:30137-30143.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30137-30143
    • Gomez, I.1    Miranda-Rios, J.2    Rudido-Pinera, E.3    Oltean, D.I.4    Gill, S.S.5    Bravo, A.6    Soberon, M.7
  • 24
    • 0014118333 scopus 로고
    • Biphasic system for separation of spores and crystals of Bacillus thuringiensis
    • Goodman, N. S., R. J. Gottfried, and M. H. Rogoff. 1967. Biphasic system for separation of spores and crystals of Bacillus thuringiensis. J. Bacteriol. 94:485.
    • (1967) J. Bacteriol. , vol.94 , pp. 485
    • Goodman, N.S.1    Gottfried, R.J.2    Rogoff, M.H.3
  • 26
    • 0037434835 scopus 로고    scopus 로고
    • A cadherin-like protein functions as a receptor for Bacillus thuringiensis Cry1Aa and Cry1Ac toxins on midgut epithelial cells of Bombyx mori larvae
    • Hara, H., S. Atsumi, K. Yaoi, K. Nakanishi, S. Higurashi, N. Miura, H. Tabunoki, and R. Sato. 2003. A cadherin-like protein functions as a receptor for Bacillus thuringiensis Cry1Aa and Cry1Ac toxins on midgut epithelial cells of Bombyx mori larvae. FEBS Lett. 538:29-34.
    • (2003) FEBS Lett. , vol.538 , pp. 29-34
    • Hara, H.1    Atsumi, S.2    Yaoi, K.3    Nakanishi, K.4    Higurashi, S.5    Miura, N.6    Tabunoki, H.7    Sato, R.8
  • 27
    • 0025045696 scopus 로고
    • Effects of Bacillus thuringiensis δ-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 δ-endotoxin on the permeability of brush border membrane vesicles from tobacco hornworm (Manduca sexta) midgut. Comp. Biochem. Physiol. Part C 95:241-245.
    • (1990) Comp. Biochem. Physiol. Part C , vol.95 , pp. 241-245
    • Hendrickx, K.1    De Loof, A.2    Van Mellaert, H.3
  • 28
    • 0024278416 scopus 로고
    • Binding of the δ-endotoxin from Bacillus thuringiensis to brush-border membrane vesicles of the cabbage butterfly (Pieris brassicae)
    • Hofmann, C, P. Lüthy, R. Hütter, and V. Pliska. 1988. Binding of the δ-endotoxin from Bacillus thuringiensis to brush-border membrane vesicles of the cabbage butterfly (Pieris brassicae). Eur. J. Biochem. 173:85-91.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 85-91
    • Hofmann, C.1    Lüthy, P.2    Hütter, R.3    Pliska, V.4
  • 29
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Höfte, H., and H. R. Whiteley. 1989. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53:242-255.
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 30
    • 0040358826 scopus 로고    scopus 로고
    • Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor
    • Jenkins, J. L., M. K. Lee, A. P. Valaitis, A. Curtiss, and D. H. Dean. 2000. Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor. J. Biol. Chem. 275:14423-14431.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14423-14431
    • Jenkins, J.L.1    Lee, M.K.2    Valaitis, A.P.3    Curtiss, A.4    Dean, D.H.5
  • 31
    • 0032743862 scopus 로고    scopus 로고
    • Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity
    • Jenkins, J. L., M. K. Lee, S. Sangadala, M. J. Adang, and D. H. Dean. 1999. Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity. FEBS Lett. 462:373-376.
    • (1999) FEBS Lett. , vol.462 , pp. 373-376
    • Jenkins, J.L.1    Lee, M.K.2    Sangadala, S.3    Adang, M.J.4    Dean, D.H.5
  • 32
    • 0004072904 scopus 로고    scopus 로고
    • Oxford University Press, Oxford, England
    • Kleanthous, C. 2000. Protein-protein recognition, p. 20-21. Oxford University Press, Oxford, England.
    • (2000) Protein-protein Recognition , pp. 20-21
    • Kleanthous, C.1
  • 33
    • 0029027032 scopus 로고
    • Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin
    • Knight, P. J. K., B. H. Knowles, and D. J. Ellar. 1995. Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin. J. Biol. Chem. 270:17765-17770.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17765-17770
    • Knight, P.J.K.1    Knowles, B.H.2    Ellar, D.J.3
  • 34
    • 0028291484 scopus 로고
    • The receptor for Bacillus thuringiensis CryIAc δ-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N
    • Knight, P. J. K., N. Crickmore, and D. J. Ellar. 1994. The receptor for Bacillus thuringiensis CryIAc δ-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N. Mol. Microbiol. 11:429-436.
    • (1994) Mol. Microbiol. , vol.11 , pp. 429-436
    • Knight, P.J.K.1    Crickmore, N.2    Ellar, D.J.3
  • 35
    • 0023183759 scopus 로고
    • Colloid-osmotic lysis is a general feature of the mechanisms of action of Bacillus thuringiensis δ-endotoxins with different insect specificities
    • Knowles, B. H., and D. J. Ellar. 1987. Colloid-osmotic lysis is a general feature of the mechanisms of action of Bacillus thuringiensis δ-endotoxins with different insect specificities. Biochim. Biophys. Acta 924:509-518.
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 509-518
    • Knowles, B.H.1    Ellar, D.J.2
  • 36
    • 0000035290 scopus 로고
    • Lectin-like binding of Bacillus thuringiensis var. kurstaki lepidopteran-specific toxin is an initial step in insecticidal action
    • Knowles, B. H., W. E. Thomas, and D. J. Ellar. 1984. Lectin-like binding of Bacillus thuringiensis var. kurstaki lepidopteran-specific toxin is an initial step in insecticidal action. FEBS Lett. 168:197-202.
    • (1984) FEBS Lett. , vol.168 , pp. 197-202
    • Knowles, B.H.1    Thomas, W.E.2    Ellar, D.J.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0028846881 scopus 로고
    • Domain III exchanges of Bacillus thuringiensis Cry1A toxins affect binding to different gypsy moth midgut receptors
    • Lee, M. K., B. A. Young, and D. H. Dean. 1995. Domain III exchanges of Bacillus thuringiensis Cry1A toxins affect binding to different gypsy moth midgut receptors. Biochem. Biophys. Res. Commun. 216:306-312.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 306-312
    • Lee, M.K.1    Young, B.A.2    Dean, D.H.3
  • 39
    • 0029892617 scopus 로고    scopus 로고
    • Inconsistencies in determining Bacillus thuringiensis toxin binding sites relationship by comparing competition assays with ligand blotting
    • Lee, M. K., and D. H. Dean. 1996. Inconsistencies in determining Bacillus thuringiensis toxin binding sites relationship by comparing competition assays with ligand blotting. Biochem. Biophys. Res. Commun. 220:575-580.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 575-580
    • Lee, M.K.1    Dean, D.H.2
  • 40
    • 0004098818 scopus 로고    scopus 로고
    • Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity
    • Lee, M. K., T. H. You, F. L. Gould, and D. H. Dean. 1999. Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity. Appl. Environ. Microbiol. 65:4513-4520.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4513-4520
    • Lee, M.K.1    You, T.H.2    Gould, F.L.3    Dean, D.H.4
  • 41
    • 0000823072 scopus 로고    scopus 로고
    • Aminopeptidase N purified from gypsy moth brush border membrane vesicles is a specific receptor for Bacillus thuringiensis CryIAc toxin
    • Lee, M. K., T. H. You, B. A. Young, J. A. Cotrill, A. P. Valaitis, and D. H. Dean. 1996. Aminopeptidase N purified from gypsy moth brush border membrane vesicles is a specific receptor for Bacillus thuringiensis CryIAc toxin. Appl. Environ. Microbiol. 62:2845-2849.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2845-2849
    • Lee, M.K.1    You, T.H.2    Young, B.A.3    Cotrill, J.A.4    Valaitis, A.P.5    Dean, D.H.6
  • 42
    • 0026760525 scopus 로고
    • Location of a Bombyx mori receptor binding region on a Bacillus thuringiensis δ-endotoxin
    • Lee, M. K., R. E. Milne, A. Z. Ge, and D. H. Dean. 1992. Location of a Bombyx mori receptor binding region on a Bacillus thuringiensis δ-endotoxin. J. Biol. Chem. 267:3115-3121.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3115-3121
    • Lee, M.K.1    Milne, R.E.2    Ge, A.Z.3    Dean, D.H.4
  • 43
    • 0026050639 scopus 로고
    • Crystal structure of an insecticidal protein. The δ-endotoxin from Bacillus thuringiensis subsp. tenebrionis at 2.5 Å resolution
    • Li, J., J. Carroll, and D. J. Ellar. 1991. Crystal structure of an insecticidal protein. The δ-endotoxin from Bacillus thuringiensis subsp. tenebrionis at 2.5 Å resolution. Nature (London) 353:815-821.
    • (1991) Nature (London) , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 44
    • 0028806599 scopus 로고
    • Irreversible binding kinetics of Bacillus thuringiensis CryIA δ-endotoxins to gypsy moth brush border membrane vesicles is directly correlated to toxicity
    • Liang, Y., S. S. Patel, and D. H. Dean. 1995. Irreversible binding kinetics of Bacillus thuringiensis CryIA δ-endotoxins to gypsy moth brush border membrane vesicles is directly correlated to toxicity. J. Biol. Chem. 270:24719-24724.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24719-24724
    • Liang, Y.1    Patel, S.S.2    Dean, D.H.3
  • 45
    • 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
  • 46
    • 0028128867 scopus 로고
    • Identification of amino acid residues of Bacillus thuringiensis δ-endotoxin CryIAa associated with membrane binding and toxicity to Bombyx mori
    • Lu, H., F. Rajamohan, and D. H. Dean. 1994. Identification of amino acid residues of Bacillus thuringiensis δ-endotoxin CryIAa associated with membrane binding and toxicity to Bombyx mori. J. Bacteriol. 176:5554-5559.
    • (1994) J. Bacteriol. , vol.176 , pp. 5554-5559
    • Lu, H.1    Rajamohan, F.2    Dean, D.H.3
  • 47
    • 32744455506 scopus 로고    scopus 로고
    • note
    • Reference deleted.
  • 48
    • 0031200935 scopus 로고    scopus 로고
    • The Heliothis virescens 170 kDa aminopeptidase functions as 'receptor A' by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formation
    • Luo, K., S. Sangadala, L. Masson, A. Mazza, R. Brousseau, and M. J. Adang. 1997. The Heliothis virescens 170 kDa aminopeptidase functions as 'receptor A' by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formation. Insect Biochem. Mol. Biol. 27:735-743.
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 735-743
    • Luo, K.1    Sangadala, S.2    Masson, L.3    Mazza, A.4    Brousseau, R.5    Adang, M.J.6
  • 49
    • 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
  • 50
    • 0029152148 scopus 로고
    • The CryIA(c) receptor purified from Manduca sexta displays multiple specificities
    • Masson, L., Y. J. Lu, A. Mazza, R. Brousseau, and M. J. Adang. 1995. The CryIA(c) receptor purified from Manduca sexta displays multiple specificities. J. Biol. Chem. 270:20309-20315.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20309-20315
    • Masson, L.1    Lu, Y.J.2    Mazza, A.3    Brousseau, R.4    Adang, M.J.5
  • 51
    • 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 (Cambridge) 9:409-417.
    • (2001) Structure (Cambridge) , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 53
    • 0032036960 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the Bombyx mori receptor for Bacillus thuringiensis insecticidal Cry1Aa toxin
    • Nagamatsu, Y., S. Toda, T. Koike, Y. Miyoshi, S. Shigematsu, and M. Kogure. 1998. Cloning, sequencing, and expression of the Bombyx mori receptor for Bacillus thuringiensis insecticidal Cry1Aa toxin. Biosci. Biotechnol. Biochem. 62:727-734.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 727-734
    • Nagamatsu, Y.1    Toda, S.2    Koike, T.3    Miyoshi, Y.4    Shigematsu, S.5    Kogure, M.6
  • 54
    • 0032701177 scopus 로고    scopus 로고
    • The cadherin-like protein is essential to specificity determination and cytotoxic action of the Bacillus thuringiensis insecticidal CryIAa toxin
    • Nagamatsu, Y., T. Koike, K. Sasaki, A. Yoshimoto, and Y. Furukawa. 1999. The cadherin-like protein is essential to specificity determination and cytotoxic action of the Bacillus thuringiensis insecticidal CryIAa toxin. FEBS Lett. 460:385-390.
    • (1999) FEBS Lett. , vol.460 , pp. 385-390
    • Nagamatsu, Y.1    Koike, T.2    Sasaki, K.3    Yoshimoto, A.4    Furukawa, Y.5
  • 55
    • 0021275136 scopus 로고
    • A toxic fragment from the entomocidal crystal protein of Bacillus thuringiensis
    • Nagamatsu, Y., Y. Itai, C. Hatanaka, G. Funatsu, and K. Hayashi. 1984. A toxic fragment from the entomocidal crystal protein of Bacillus thuringiensis. Agric. Biol. Chem. 48:611-619.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 611-619
    • Nagamatsu, Y.1    Itai, Y.2    Hatanaka, C.3    Funatsu, G.4    Hayashi, K.5
  • 56
    • 0014087002 scopus 로고
    • Enzyme-labeled antibodies for the light and electron microscopic localization of tissue antigens
    • Nakane, P. K., and G. B. Pierce, Jr. 1967. Enzyme-labeled antibodies for the light and electron microscopic localization of tissue antigens. J. Cell Biol. 33:307-318.
    • (1967) J. Cell Biol. , vol.33 , pp. 307-318
    • Nakane, P.K.1    Pierce Jr., G.B.2
  • 57
    • 0032998413 scopus 로고    scopus 로고
    • Bacillus thuringiensis insecticidal Cry1Aa toxin binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary success
    • Nakanishi, K., K. Yaoi, N. Shimada, T. Kadotani, and R. Sato. 1999. Bacillus thuringiensis insecticidal Cry1Aa toxin binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary success. Biochim. Biophys. Acta 1432:57-63.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 57-63
    • Nakanishi, K.1    Yaoi, K.2    Shimada, N.3    Kadotani, T.4    Sato, R.5
  • 58
    • 0037157109 scopus 로고    scopus 로고
    • Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella: Their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin
    • Nakanishi, K., K. Yaoi, Y. Nagino, H. Hara, M. Kitami, S. Atsumi, N. Miura, and R. Sato. 2002. Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella: their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin. FEBS Lett. 519:215-220.
    • (2002) FEBS Lett. , vol.519 , pp. 215-220
    • Nakanishi, K.1    Yaoi, K.2    Nagino, Y.3    Hara, H.4    Kitami, M.5    Atsumi, S.6    Miura, N.7    Sato, R.8
  • 59
    • 0023183736 scopus 로고
    • Nucleotide sequence of the insecticidal protein gene of Bacillus thuringiensis strain aizawai IPL7 and its high-level expression in Escherichia coli
    • Oeda, K., K. Oshie, M. Shimizu, K. Nakamura, H. Yamamoto, I. Nakayama, and H. Ohkawa. 1987. Nucleotide sequence of the insecticidal protein gene of Bacillus thuringiensis strain aizawai IPL7 and its high-level expression in Escherichia coli. Gene 53:113-119.
    • (1987) Gene , vol.53 , pp. 113-119
    • Oeda, K.1    Oshie, K.2    Shimizu, M.3    Nakamura, K.4    Yamamoto, H.5    Nakayama, I.6    Ohkawa, H.7
  • 60
    • 0037033087 scopus 로고    scopus 로고
    • Silencing of midgut aminopeptidase N of Spodoptera litura by dsRNA establishes its role as Bt toxin receptor
    • Rajagopal, R., S. Sivakumar, N. Agrawal, P. Malhotra, and R. K. Bhatnagar. 2002. Silencing of midgut aminopeptidase N of Spodoptera litura by dsRNA establishes its role as Bt toxin receptor. J. Biol. Chem. 277:46849-46851.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46849-46851
    • Rajagopal, R.1    Sivakumar, S.2    Agrawal, N.3    Malhotra, P.4    Bhatnagar, R.K.5
  • 61
    • 0029007022 scopus 로고
    • Single amino acid changes in domain II of Bacillus thuringiensis CryIAb δ-endotoxin affect irreversible binding to Manduca sexta midgut membrane vesicles
    • Rajamohan, F., E. Alcantara, M. K. Lee, X. J. Chen, A. Curtiss, and D. H. Dean. 1995. Single amino acid changes in domain II of Bacillus thuringiensis CryIAb δ-endotoxin affect irreversible binding to Manduca sexta midgut membrane vesicles. J. Bacteriol. 177:2276-2282.
    • (1995) J. Bacteriol. , vol.177 , pp. 2276-2282
    • Rajamohan, F.1    Alcantara, E.2    Lee, M.K.3    Chen, X.J.4    Curtiss, A.5    Dean, D.H.6
  • 62
    • 0029908854 scopus 로고    scopus 로고
    • Protein engineering of Bacillus thuringiensis δ-endotoxin: Mutations at domain II of Cry1Ab enhance receptor affinity and toxicity towards gypsy moth larvae
    • Rajamohan, F., O. Alzate, J. A. Cotrill, A. Curtiss, and D. H. Dean. 1996. Protein engineering of Bacillus thuringiensis δ-endotoxin: mutations at domain II of Cry1Ab enhance receptor affinity and toxicity towards gypsy moth larvae. Proc. Natl. Acad. Sci. USA 93:14338-14343.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14338-14343
    • Rajamohan, F.1    Alzate, O.2    Cotrill, J.A.3    Curtiss, A.4    Dean, D.H.5
  • 63
    • 0030070158 scopus 로고    scopus 로고
    • Role of domain II, loop 2 residues of Bacillus thuringiensis CryIAb δ-endotoxin in reversible and irreversible binding to Manduca sexta and Heliothis virescens
    • Rajamohan, F., J. A. Cotrill, F. Gould, and D. H. Dean. 1996. Role of domain II, loop 2 residues of Bacillus thuringiensis CryIAb δ-endotoxin in reversible and irreversible binding to Manduca sexta and Heliothis virescens. J. Biol. Chem. 271:2390-2397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2390-2397
    • Rajamohan, F.1    Cotrill, J.A.2    Gould, F.3    Dean, D.H.4
  • 64
    • 0029792870 scopus 로고    scopus 로고
    • Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb δ-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts
    • Rajamohan, F., S. R. A. Hussain, J. A. Cotrill, F. Gould, and D. H. Dean. 1996. Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb δ-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts. J. Biol. Chem. 271:25220-25226.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25220-25226
    • Rajamohan, F.1    Hussain, S.R.A.2    Cotrill, J.A.3    Gould, F.4    Dean, D.H.5
  • 67
    • 0021799565 scopus 로고
    • The amino acid sequence of a crystal protein from Bacillus thuringiensis deduced from the DNA base sequence
    • Schnepf, H. E., H. C. Wong, and H. R. Whiteley. 1985. The amino acid sequence of a crystal protein from Bacillus thuringiensis deduced from the DNA base sequence. J. Biol. Chem. 260:6264-6272.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6264-6272
    • Schnepf, H.E.1    Wong, H.C.2    Whiteley, H.R.3
  • 68
    • 0027513963 scopus 로고
    • Lepidopteran-specific crystal toxins from Bacillus thuringiensis form cation- and anion-selective channels in planar lipid bilayers
    • Schwartz, J. L., L. Garneau, D. Savaria, L. Masson, R. Brousseau, and E. Rousseau. 1993. Lepidopteran-specific crystal toxins from Bacillus thuringiensis form cation- and anion-selective channels in planar lipid bilayers. J. Membr. Biol. 132:53-62.
    • (1993) J. Membr. Biol. , vol.132 , pp. 53-62
    • Schwartz, J.L.1    Garneau, L.2    Savaria, D.3    Masson, L.4    Brousseau, R.5    Rousseau, E.6
  • 69
    • 0030756318 scopus 로고    scopus 로고
    • Single-site mutations in the conserved alternating-arginine region affect ionic channels formed by CryIAa, a Bacillus thuringiensis toxin
    • Schwartz, J. L., L. Potvin, X. J. Chen, R. Brousseau, R. Laprade, and D. H. Dean. 1997. Single-site mutations in the conserved alternating-arginine region affect ionic channels formed by CryIAa, a Bacillus thuringiensis toxin. Appl. Environ. Microbiol. 63:3978-3984.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3978-3984
    • Schwartz, J.L.1    Potvin, L.2    Chen, X.J.3    Brousseau, R.4    Laprade, R.5    Dean, D.H.6
  • 70
    • 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. L., Y. J. Lu., P. Sohnlein, R. Brousseau, R. Laprade, L. Masson, and M. J. Adang. 1997. Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors. FEBS Lett. 412:270-276.
    • (1997) FEBS Lett. , vol.412 , pp. 270-276
    • Schwartz, J.L.1    Lu, Y.J.2    Sohnlein, P.3    Brousseau, R.4    Laprade, R.5    Masson, L.6    Adang, M.J.7
  • 71
    • 0033023111 scopus 로고    scopus 로고
    • Binding of phylogenetically distant Bacillus thuringiensis Cry toxins to a Bombyx mori aminopeptidase N suggests importance of Cry toxin's conserved structure in receptor binding
    • Shinkawa, A., K. Yaoi, T. Kadotani, M. Imamura, N. Koizumi, H. Iwahana, and R. Sato. 1999. Binding of phylogenetically distant Bacillus thuringiensis Cry toxins to a Bombyx mori aminopeptidase N suggests importance of Cry toxin's conserved structure in receptor binding. Curr. Microbiol. 39:14-20.
    • (1999) Curr. Microbiol. , vol.39 , pp. 14-20
    • Shinkawa, A.1    Yaoi, K.2    Kadotani, T.3    Imamura, M.4    Koizumi, N.5    Iwahana, H.6    Sato, R.7
  • 72
    • 0029993089 scopus 로고    scopus 로고
    • Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion
    • Smedley, D. P., and D. J. Ellar. 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.
    • (1996) Microbiology , vol.142 , pp. 1617-1624
    • Smedley, D.P.1    Ellar, D.J.2
  • 73
    • 0028907322 scopus 로고
    • Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis
    • Vadlamudi, R. K., E. Weber, I. H. Ji, T. H. Ji, and L. A. Bulla. 1995. Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis. J. Biol. Chem. 270:5490-5494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5490-5494
    • Vadlamudi, R.K.1    Weber, E.2    Ji, I.H.3    Ji, T.H.4    Bulla, L.A.5
  • 74
    • 0029584379 scopus 로고
    • Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as the receptor for the CryIA(c) δ-endotoxin of Bacillus thuringiensis
    • Valaitis, A. P., M. K. Lee, F. Rajamohan, and D. H. Dean. 1995. Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as the receptor for the CryIA(c) δ-endotoxin of Bacillus thuringiensis. Insect Biochem. Mol. Biol. 25:1143-1151.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 1143-1151
    • Valaitis, A.P.1    Lee, M.K.2    Rajamohan, F.3    Dean, D.H.4
  • 75
    • 0030022109 scopus 로고    scopus 로고
    • Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles
    • Wolfersberger, M. G., X. J. Chen, and D. H. Dean. 1996. Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles. Appl. Environ. Microbiol. 62:279-282.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 279-282
    • Wolfersberger, M.G.1    Chen, X.J.2    Dean, D.H.3
  • 76
    • 0029869450 scopus 로고    scopus 로고
    • Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA δ-endotoxin
    • Wu, S. J., and D. H. Dean. 1996. Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA δ-endotoxin. J. Mol. Biol. 255:628-640.
    • (1996) J. Mol. Biol. , vol.255 , pp. 628-640
    • Wu, S.J.1    Dean, D.H.2
  • 77
    • 0030964231 scopus 로고    scopus 로고
    • Aminopeptidase N from Bombyx mori as a candidate for the receptor of Bacillus thuringiensis Cry1Aa toxin
    • Yaoi, K., T. Kadotani, H. Kuwana, A. Shinkawa, T. Takahashi, H. Iwahana, and R. Sato. 1997. Aminopeptidase N from Bombyx mori as a candidate for the receptor of Bacillus thuringiensis Cry1Aa toxin. Eur. J. Biochem. 246:652-657.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 652-657
    • Yaoi, K.1    Kadotani, T.2    Kuwana, H.3    Shinkawa, A.4    Takahashi, T.5    Iwahana, H.6    Sato, R.7


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