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R. Vadlamudi, E. Weber, Inhae Ji, T. Ji, L. Bulla (1995)
Cloning and Expression of a Receptor for an Insecticidal Toxin of Bacillus thuringiensis(*)The Journal of Biological Chemistry, 270
T. Flo, Kelly Smith, Shintaro Sato, David Rodriguez, M. Holmes, R. Strong, S. Akira, A. Aderem (2004)
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating ironNature, 432
P. Bergman, L. Johansson, Hong Wan, A. Jones, R. Gallo, G. Gudmundsson, T. Hökfelt, A. Jonsson, B. Agerberth (2006)
Induction of the Antimicrobial Peptide CRAMP in the Blood-Brain Barrier and Meninges after Meningococcal InfectionInfection and Immunity, 74
J. Shaw, L. Beadle (1949)
A simplified ultramicro Kjeldahl method for the estimation of protein and total nitrogen in fluid samples of less than 1-0 mu 1.The Journal of experimental biology, 26 1
Y. Shitomi, T. Hayakawa, D. Hossain, M. Higuchi, K. Miyamoto, K. Nakanishi, R. Sato, H. Hori (2006)
A novel 96-kDa aminopeptidase localized on epithelial cell membranes of Bombyx mori midgut, which binds to Cry1Ac toxin of Bacillus thuringiensis.Journal of biochemistry, 139 2
J. Ferré, J. Rie (2002)
Biochemistry and Genetics of Insect Resistance to Bacillus thuringiensisAnnual Review of Entomology, 47
P. Knight, N. Crickmore, D. Ellar (1994)
The receptor for Bacillus thuringiensis CrylA(c) delta‐endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase NMolecular Microbiology, 11
H. Ihara, T. Uemura, Miho Masuhara, S. Ikawa, Kenji Sugimoto, A. Wadano, M. Himeno (1998)
Purification and partial amino acid sequences of the binding protein from Bombyx mori for CryIAa δ-endotoxin of Bacillus thuringiensisComparative Biochemistry and Physiology B, 120
NG Pandian, T Ishikawa, M Togashi, Y Shitomi, K Haginoya, K Yamamoto, T Nishiumi, H Hori (2008)
Bombyx mori midgut membrane protein P252 which binds to Cry1A of Bacillus thuringiensis is a chlorophyllide binding protein and its resulting complex has antimicrobial activityAppl Environ Microbiol, 74
B. Mauchamp, C. Royer, A. Garel, A. Jalabert, M. Rocha, A. Grenier, V. Labas, J. Vinh, K. Mita, K. Kadono, G. Chavancy (2006)
Polycalin (chlorophyllid A binding protein): a novel, very large fluorescent lipocalin from the midgut of the domestic silkworm Bombyx mori L.Insect biochemistry and molecular biology, 36 8
J. Yang, C. Wu, H. Martinez (1986)
Calculation of protein conformation from circular dichroism.Methods in enzymology, 130
E. Schnepf, N. Crickmore, J. Rie, D. Lereclus, J. Baum, J. Feitelson, D. Zeigler, D. Dean (1998)
Bacillus thuringiensis and Its Pesticidal Crystal ProteinsMicrobiology and Molecular Biology Reviews, 62
M. Metz (2003)
Bacillus thuringiensis: A Cornerstone of Modern Agriculture
S. Gill, E. Cowles, V. Francis (1995)
Identification, Isolation, and Cloning of a Bacillus thuringiensis CryIAc Toxin-binding Protein from the Midgut of the Lepidopteran Insect Heliothis virescens(*)The Journal of Biological Chemistry, 270
Joel Griffitts, R. Aroian (2005)
Many roads to resistance: how invertebrates adapt to Bt toxinsBioEssays, 27
T. Kishimoto, H. Hori, D. Takano, Yoshiyasu Nakano, Mayumi Watanabe, T. Mitsui (2001)
Rice α‐mannosidase digesting the high mannose glycopeptide of glutelinPhysiologia Plantarum, 112
B. Federici (2003)
Effects of Bt on Non-Target OrganismsJournal of New Seeds, 5
K. Tomimoto, T. Hayakawa, H. Hori (2006)
Pronase digestion of brush border membrane-bound Cry1Aa shows that almost the whole activated Cry1Aa molecule penetrates into the membrane.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 144 4
L. Indrasith, Katsutoshi Ogiwara, Masayoshi MlNAMI, Tomoko Iwasa, T. Maruyama, N. Suzuki, S. Asan, Kazunobu Sakanaka, H. Hori (1991)
Processing of Delta Endotoxin from Bacillus thuringiensis Subspp.Kurstaki HD-1 and HD-73 by Immobilized Trypsin and ChymotrypsinApplied Entomology and Zoology, 26
Y. Nagamatsu, Satoshi Toda, T. Koike, Yoko Miyoshi, S. Shigematsu, M. Kogure (1998)
Cloning, sequencing, and expression of the Bombyx mori receptor for Bacillus thuringiensis insecticidal CryIA(a) toxin.Bioscience, biotechnology, and biochemistry, 62 4
B. Tabashnik (1994)
Evolution of Resistance to Bacillus ThuringiensisAnnual Review of Entomology, 39
G. Pandian, T. Ishikawa, M. Togashi, Y. Shitomi, Kohsuke Haginoya, Shûhei Yamamoto, T. Nishiumi, H. Hori (2008)
Bombyx mori Midgut Membrane Protein P252, Which Binds to Bacillus thuringiensis Cry1A, Is a Chlorophyllide-Binding Protein, and the Resulting Complex Has Antimicrobial ActivityApplied and Environmental Microbiology, 74
S. Sangadala, F. Walters, L. English, M. Adang (1994)
A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal CryIA(c) toxin binding and 86Rb(+)-K+ efflux in vitro.The Journal of biological chemistry, 269 13
J. Rie, W. Mcgaughey, D. Johnson, B. Barnett, H. Mellaert (1990)
Mechanism of insect resistance to the microbial insecticide Bacillus thuringiensis.Science, 247 4938
Robert Russell, J. Robertson, N. Savin (1977)
POLO: A New Computer Program for Probit AnalysisBulletin of the Entomological Society of America, 23
Y. Nagamatsu, S. Toda, F. Yamaguchi, M. Ogo, M. Kogure, M. Nakamura, Y. Shibata, T. Katsumoto (1998)
Identification of Bombyx mori midgut receptor for Bacillus thuringiensis insecticidal CryIA(a) toxin.Bioscience, biotechnology, and biochemistry, 62 4
D. Heckel (1994)
The Complex Genetic Basis of Resistance to Bacillus thuringiensis Toxin in InsectsBiocontrol Science and Technology, 4
S. Ong, J. Ho, B. Ho, J. Ding (2006)
Iron-withholding strategy in innate immunity.Immunobiology, 211 4
Delwer Hossain, Y. Shitomi, Yohei Nanjo, D. Takano, T. Nishiumi, T. Hayakawa, T. Mitsui, R. Sato, H. Hori (2005)
Localization of a novel 252-kDa plasma membrane protein that binds Cry1A toxins in the midgut epithelia of Bombyx moriApplied Entomology and Zoology, 40
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
Robert Coleman, B. Pugh (1997)
Slow dimer dissociation of the TATA binding protein dictates the kinetics of DNA binding.Proceedings of the National Academy of Sciences of the United States of America, 94 14
A. Valaitis, M. Lee, F. Rajamohan, D. Dean (1995)
Brush border membrane aminopeptidase-N in the midgut of the gypsy moth serves as the receptor for the CryIA(c) delta-endotoxin of Bacillus thuringiensis.Insect biochemistry and molecular biology, 25 10
J. Kough (2003)
The Safety of Bacillus thuringiensis for Human ConsumptionJournal of New Seeds, 5
Satita Tapaneeyakorn, Walairat Pornwiroon, G. Katzenmeier, C. Angsuthanasombat (2005)
Structural requirements of the unique disulphide bond and the proline-rich motif within the α4-α5 loop for larvicidal activity of the Bacillus thuringiensis Cry4Aa δ-endotoxinBiochemical and Biophysical Research Communications, 330
C. Angelucci, G. Barrett-Wilt, D. Hunt, R. Akhurst, P. East, K. Gordon, P. Campbell (2008)
Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: identification of proteins binding the delta-endotoxin, Cry1Ac of Bacillus thuringiensis.Insect biochemistry and molecular biology, 38 7
L. Gilbert, K. Iatrou, S. Gill (2004)
comprehensive molecular insect science
A. Shelton, J. Robertson, Juliet Tang, C. Pérez, S. Eigenbrode, H. Preisler, W. Wilsey, R. Cooley (1993)
Resistance of diamondback moth (Lepidoptera : Plutellidae) to Bacillus thuringiensis subspecies in the fieldJournal of Economic Entomology, 86
A. Bravo, M. Soberón (2005)
6.6 – Bacillus thuringiensis: Mechanisms and Use, 6
A. Bravo, S. Gill, M. Soberón (2007)
Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control.Toxicon : official journal of the International Society on Toxinology, 49 4
Suzuki Nobukazu, H. Hori, K. Ogiwara, S. Asano, R. Sato, M. Ohba, H. Iwahana (1992)
Insecticidal spectrum of a novel isolate of Bacillus thuringiensis serovar japonensisBiological Control, 2
D. Hossain, Y. Shitomi, Kenta Moriyama, M. Higuchi, T. Hayakawa, T. Mitsui, R. Sato, H. Hori (2004)
Characterization of a Novel Plasma Membrane Protein, Expressed in the Midgut Epithelia of Bombyx mori, That Binds to Cry1A ToxinsApplied and Environmental Microbiology, 70
M. Nair, D. Dean (2008)
All Domains of Cry1A Toxins Insert into Insect Brush Border Membranes*Journal of Biological Chemistry, 283
Craig Pigott, D. Ellar (2007)
Role of Receptors in Bacillus thuringiensis Crystal Toxin ActivityMicrobiology and Molecular Biology Reviews, 71
A. Janmaat, J. Myers (2003)
Rapid evolution and the cost of resistance to Bacillus thuringiensis in greenhouse populations of cabbage loopers, Trichoplusia niProceedings of the Royal Society of London. Series B: Biological Sciences, 270
Yong Kim, K. Kanda, F. Kato, A. Murata (1998)
Effect of the carboxyl-terminal portion of Cry1Ab in Bacillus thuringiensis on toxicity against the silkworm, Bombyx mori.Applied Entomology and Zoology, 33
P252, a 252-kDa Bombyx mori protein located on the larval midgut membrane, has been shown to bind strongly with Bacillus thuringiensis Cry1A toxins (Hossain et al. Appl Environ Microbiol 70:4604–4612, 2004). P252 was also shown to bind chlorophyllide (Chlide) to form red fluorescence–emitting complex Bm252RFP with significant antimicrobial activity (Pandian et al. Appl Environ Microbiol 74:1324–1331, 2008). In this article, we show that Cry1A toxin bound with Bm252RFP and Bm252RFP–Cry1A macrocomplex, with both antimicrobial and insecticidal activities, was formed. The insecticidal activity of Bm252RFP–Cry1Ab was reduced from an LD50 of 1.62 to 5.05 μg, but Bm252RFP–Cry1Aa and Bm252RFP–Cry1Ac did not show such reduction. On the other hand, the antimicrobial activity of Bm252RFP–Cry1Ab was shown to retain almost the same activity as Bm252RFP, while the other two complexes lost around 30% activity. The intensity of photo absorbance and fluorescence emission of Bm252RFP–Cry1Ab were significantly reduced compared to those of the other two complexes. Circular dichroism showed that the contents of Cry1Ab α-helix was significantly decreased in Bm252RFP–Cry1Ab but not in the other two toxins. These data suggested that the reduction of contents of α-helix in Cry1Ab affected the insecticidal activity of the macrocomplex but did not alter the antimicrobial moiety in the macrocomplex of Bm252RFP–Cry1Ab.
The Journal of Membrane Biology – Springer Journals
Published: Nov 16, 2010
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