Specific binding of activated Vip3Aa10 to Helicoverpa armigera brush border membrane vesicles results in pore formation
| Autor: | Ai-Zhen Yang, Bao-Guang Hua, Xiao-Hong Shen, Jing-Guo Liu, Guang-lu Shi |
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| Rok vydání: | 2011 |
| Předmět: |
Brush border
Helicoverpa armigera medicine.disease_cause Insect Control Ion Channels Insecticide Resistance Bacterial Proteins Bacillus thuringiensis medicine Animals Binding site Pest Control Biological Transport Vesicles Lipid raft Ecology Evolution Behavior and Systematics Binding Sites Microvilli biology Toxin fungi Midgut biology.organism_classification Trypsin Gastrointestinal Tract Lepidoptera Biochemistry Host-Pathogen Interactions Protein Binding medicine.drug |
| Zdroj: | Journal of Invertebrate Pathology. 108:92-97 |
| ISSN: | 0022-2011 |
| DOI: | 10.1016/j.jip.2011.07.007 |
| Popis: | Helicoverpa armigera is one of the most harmful pests in China. Although it had been successfully controlled by Cry1A toxins, some H. armigera populations are building up resistance to Cry1A toxins in the laboratory. Vip3A, secreted by Bacillus thuringiensis, is another potential toxin against H. armigera. Previous reports showed that activated Vip3A performs its function by inserting into the midgut brush border membrane vesicles (BBMV) of susceptible insects. To further investigate the binding of Vip3A to BBMV of H. armigera, the full-length Vip3Aa10 toxin expressed in Escherichia coli was digested by trypsin or midgut juice extract, respectively. Among the fragments of digested Vip3Aa10, only a 62kDa fragment (Vip3Aa10-T) exhibited binding to BBMV of H. armigera and has insecticidal activity. Moreover, this interaction was specific and was not affected by the presence of Cry1Ab toxin. Binding of Vip3Aa10-T to BBMV resulted in the formation of an ion channel. Unlike Cry1A toxins, Vip3Aa10-T was just slightly associated with lipid rafts of BBMV. These data suggest that although activated Vip3Aa10 specifically interacts with BBMV of H. armigera and forms an ion channel, the mode of action of it may be different from that of Cry1A toxins. |
| Databáze: | OpenAIRE |
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