机构地区:[1]Key Laboratory of Applied Entomology," Key Laboratory of Plant Protection Resources and Pest Management, Ministry of Education~ College of Plant Protection, Northwest Agriculture and Forestry University, Yangling 712100, P.R.China [2]State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R.China
出 处:《Journal of Integrative Agriculture》2012年第11期1845-1851,共7页农业科学学报(英文版)
基 金:supported by the National Basic Research Program of China (31071693)
摘 要:With the long-term use of Bacillus thuringiensis (Bt) insecticide and expansion of CrylA-expressing transgenic plants, some insect pests have developed resistance to Bt in open fields, greenhouses, and in the laboratory. Bt resistance is complex and there appear to be different ways for resistance development. Understanding the Bt resistance mechanisms is critical to prolong its usefulness. In this article, Bt receptors, the cadherin and aminopeptidase N (APN), in brush border membrane vesicles (/3BMV) of Helicoverpa armigera were examined in both CrylAc-susceptible (96S) and CrylAc- resistant (LF120) strains, to compare CrylAc toxin oligomerization and pore formation in these two strains. CrylAc toxin oligomerization and pore formation in these two strains were compared. Results showed that cadherin and aminopeptidase N proteins could express normally in both susceptible and resistant 11. armigera strains. The ability to form CrylAc oligomers and ion channels on BBMVs was also not significantly different between these two strains.With the long-term use of Bacillus thuringiensis (Bt) insecticide and expansion of CrylA-expressing transgenic plants, some insect pests have developed resistance to Bt in open fields, greenhouses, and in the laboratory. Bt resistance is complex and there appear to be different ways for resistance development. Understanding the Bt resistance mechanisms is critical to prolong its usefulness. In this article, Bt receptors, the cadherin and aminopeptidase N (APN), in brush border membrane vesicles (/3BMV) of Helicoverpa armigera were examined in both CrylAc-susceptible (96S) and CrylAc- resistant (LF120) strains, to compare CrylAc toxin oligomerization and pore formation in these two strains. CrylAc toxin oligomerization and pore formation in these two strains were compared. Results showed that cadherin and aminopeptidase N proteins could express normally in both susceptible and resistant 11. armigera strains. The ability to form CrylAc oligomers and ion channels on BBMVs was also not significantly different between these two strains.
关 键 词:Helicoverpa armigera Bt resistance OLIGOMERIZATION pore formation
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