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Science 5 January 1990:
Vol. 247. no. 4938, pp. 72 - 74
DOI: 10.1126/science.2294593
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Articles

Science, Vol 247, Issue 4938, 72-74
Copyright © 1990 by American Association for the Advancement of Science

articles

Mechanism of insect resistance to the microbial insecticide Bacillus thuringiensis

J Van Rie, WH McGaughey, DE Johnson, BD Barnett, and H Van Mellaert

Plant Genetic Systems, Gent, Belgium.

Receptor binding studies show that resistance of a laboratory-selected Plodia interpunctella strain to a Bacillus thuringiensis insecticidal crystal protein (ICP) is correlated with a 50-fold reduction in affinity of the membrane receptor for this protein. The strain is sensitive to a second type of ICP that apparently recognizes a different receptor. Understanding the mechanism of resistance will provide strategies to prevent or delay resistance and hence prolong the usefulness of B. thuringiensis ICPs as environmentally safe insecticides.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Common, but Complex, Mode of Resistance of Plutella xylostella to Bacillus thuringiensis Toxins Cry1Ab and Cry1Ac.
A. H. Sayyed, R. Gatsi, M. S. Ibiza-Palacios, B. Escriche, D. J. Wright, and N. Crickmore (2005)
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Disruption of a Cadherin Gene Associated with Resistance to Cry1Ac {delta}-Endotoxin of Bacillus thuringiensis in Helicoverpa armigera.
X. Xu, L. Yu, and Y. Wu (2005)
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Genetic and Biochemical Characterization of Field-Evolved Resistance to Bacillus thuringiensis Toxin Cry1Ac in the Diamondback Moth, Plutella xylostella.
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Loss of the membrane anchor of the target receptor is a mechanism of bioinsecticide resistance.
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Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins.
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Identification of a Gene Associated with Bt Resistance in Heliothis virescens.
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Role of Bacillus thuringiensis Toxin Domains in Toxicity and Receptor Binding in the Diamondback Moth.
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E. Gazit, P. L. Rocca, M. S. P. Sansom, and Y. Shai (1998)
PNAS 95, 12289-12294
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Bacillus thuringiensis and Its Pesticidal Crystal Proteins.
E. Schnepf, N. Crickmore, J. Van Rie, D. Lereclus, J. Baum, J. Feitelson, D. R. Zeigler, and D. H. Dean (1998)
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Insecticidal Toxins from the Bacterium Photorhabdus luminescens.
D. Bowen, T. A. Rocheleau, M. Blackburn, O. Andreev, E. Golubeva, R. Bhartia, and R. H. ffrench-Constant (1998)
Science 280, 2129-2132
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Effects of Midgut-Protein-Preparative and Ligand Binding Procedures on the Toxin Binding Characteristics of BT-R1, a Common High-Affinity Receptor in Manduca sexta for Cry1A Bacillus thuringiensis Toxins.
T. P. Keeton, B. R. Francis, W. S. A. Maaty, and L. A. Bulla Jr. (1998)
Appl. Envir. Microbiol. 64, 2158-2165
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CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito, Culex quinquefasciatus.
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PNAS 94, 10536-10540
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Proteinase-mediated Insect Resistance to Bacillus thuringiensis Toxins.
B. Oppert, K. J. Kramer, R. W. Beeman, D. Johnson, and W. H. McGaughey (1997)
J. Biol. Chem. 272, 23473-23476
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Initial frequency of alleles for resistance to Bacillus thuringiensis toxins in field populations of Heliothis virescens.
F. Gould, A. Anderson, A. Jones, D. Sumerford, D. G. Heckel, J. Lopez, S. Micinski, R. Leonard, and M. Laster (1997)
PNAS 94, 3519-3523
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Protein engineering of Bacillus thuringiensis delta -endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae.
F. Rajamohan, O. Alzate, J. A. Cotrill, A. Curtiss, and D. H. Dean (1996)
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Mutations at Domain II, Loop 3,of Bacillus thuringiensis CryIAa and CryIAb delta -Endotoxins Suggest Loop 3Is Involved in Initial Binding to Lepidopteran Midguts.
F. Rajamohan, S.-R. A. Hussain, J. A. Cotrill, F. Gould, and D. H. Dean (1996)
J. Biol. Chem. 271, 25220-25226
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Role of Domain II, Loop 2 Residues of Bacillus thuringiensis CryIAb [IMAGE]-Endotoxin in Reversible and Irreversible Binding to Manduca sexta and Heliothis virescens.
F. Rajamohan, J. A. Cotrill, F. Gould, and D. H. Dean (1996)
J. Biol. Chem. 271, 2390-2396
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Identification, Isolation, and Cloning of a Bacillus thuringiensis CryIAc Toxin-binding Protein from the Midgut of the Lepidopteran Insect Heliothis virescens.
S. S. Gill, E. A. Cowles, and V. Francis (1995)
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Irreversible Binding Kinetics of Bacillus thuringiensis CryIA [IMAGE]-Endotoxins to Gypsy Moth Brush Border Membrane Vesicles Is Directly Correlated to Toxicity.
Y. Liang, S. S. Patel, and D. H. Dean (1995)
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The CryIA(c) Receptor Purified from Manduca sexta Displays Multiple Specificities.
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Kinetics of Bacillus thuringiensis Toxin Binding with Brush Border Membrane Vesicles from Susceptible and Resistant Larvae of Plutella xylostella.
L. Masson, A. Mazza, R. Brousseau, and B. Tabashnik (1995)
J. Biol. Chem. 270, 11887-11896
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Mutations in Domain I of Bacillus thuringiensis [IMAGE]-Endotoxin CryIAb Reduce the Irreversible Binding of Toxin to Manduca sexta Brush Border Membrane Vesicles.
X. J. Chen, A. Curtiss, E. Alcantara, and D. H. Dean (1995)
J. Biol. Chem. 270, 6412-6419
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The Assembly and Organization of the alpha5 and alpha7 Helices from the Pore-forming Domain of Bacillusthuringiensis [IMAGE]-Endotoxin.
E. Gazit and Y. Shai (1995)
J. Biol. Chem. 270, 2571-2578
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Managing Insect Resistance to Bacillus thuringiensis Toxins.
W. H. McGaughey and M. E. Whalon (1992)
Science 258, 1451-1455
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