Bt: Mode of action and use
- 18 November 2003
- journal article
- review article
- Published by Wiley in Archives of Insect Biochemistry and Physiology
- Vol. 54 (4) , 200-211
- https://doi.org/10.1002/arch.10117
Abstract
The insecticidal toxins from Bacillus thuringiensis (Bt) represent a class of biopesticides that are attractive alternatives to broad‐spectrum “hard” chemistries. The U.S. Food Quality Protection Act and the European Economic Council directives aimed at reducing the use of carbamate and organophosphate insecticides were expected to increase the use of narrowly targeted, “soft” compounds like Bt. Here we summarize the unique mode of action of Bt, which contributes to pest selectivity. We also review the patterns of Bt use in general agriculture and in specific niche markets. Despite continued predictions of dramatic growth for biopesticides due to US Food Quality Protection Act—induced cancellations of older insecticides, Bt use has remained relatively constant, even in niche markets where Bt has traditionally been relatively high. Arch. Insect Biochem. Physiol. 54:200–211, 2003.Keywords
This publication has 43 references indexed in Scilit:
- Protozoa and plant growth: the microbial loop in soil revisitedNew Phytologist, 2004
- Silencing of Midgut Aminopeptidase N of Spodoptera litura by Double-stranded RNA Establishes Its Role asBacillus thuringiensis Toxin ReceptorJournal of Biological Chemistry, 2002
- Identification of a Gene Associated with Bt Resistance in Heliothis virescensScience, 2001
- Different Mechanisms of Resistance to Bacillus thuringiensis Toxins in the Indianmeal MothApplied and Environmental Microbiology, 2001
- Genetic and Biochemical Approach for Characterization of Resistance to Bacillus thuringiensis Toxin Cry1Ac in a Field Population of the Diamondback Moth, Plutella xylostellaApplied and Environmental Microbiology, 2000
- 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 toxinJournal of Molecular Biology, 1999
- Intracellular proteases in sporulatedBacillus thuringiensissubsp.kurstakiand their role in protoxin activationFEMS Microbiology Letters, 1998
- The Heliothis virescens 170kDa aminopeptidase functions as “Receptor A” by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formationInsect Biochemistry and Molecular Biology, 1997
- The receptor for Bacillus thuringiensis CrylA(c) delta‐endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase NMolecular Microbiology, 1994
- The toxic moiety of the Bacillus thuringiensis protoxin undergoes a conformational change upon activationBiochemical and Biophysical Research Communications, 1991