Specific binding of activated Vip3Aa10 to Helicoverpa armigera brush border membrane vesicles results in pore formation

• Published in: Journal of invertebrate pathology 2011-10, Vol.108 (2), p.92-97
• Main Authors: Liu, Jing-Guo, Yang, Ai-Zhen, Shen, Xiao-Hong, Hua, Bao-Guang, Shi, Guang-Lu
• Format: Article
• Language: English
• Subjects: Animals; Bacillus thuringiensis; Bacterial Proteins - metabolism; Binding Sites; Biological and medical sciences; Brush border membrane vesicles; Brush border membranes; Escherichia coli; Fundamental and applied biological sciences. Psychology; Gastrointestinal Tract - metabolism; Helicoverpa armigera; Host-Pathogen Interactions; Insect Control - methods; Insecta; insecticidal properties; Insecticide Resistance; insects; Invertebrates; ion channels; Ion Channels - drug effects; Lepidoptera - microbiology; mechanism of action; Microvilli - metabolism; midgut; Pathology; Pest Control, Biological - methods; pests; population; Pore formation; Protein Binding; toxins; Transport Vesicles - metabolism; trypsin; Vip3Aa10
• ISSN: 0022-2011; 1096-0805
• DOI: 10.1016/j.jip.2011.07.007

Activated Vip3Aa10 specifically binds to brush border membrane vesicles of Helicoverpa armigera. This interaction results in the formation of ion channel on the BBMV. [Display omitted] ► Only the main proteolytic product of Vip3Aa10 (Vip3Aa10-T) specifically interacts with BBMV of Helicoverpa armigera. ► This interaction is not affected by the presence of Cry1Ab toxin. ► Vip3Aa10-T forms an ion channel on the H. armigera BBMV. ► Vip3Aa10-T is slightly associated with lipid rafts of H. armigera BBMV. 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 62 kDa 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.