title: Specific binding of activated Vip3Aa10 to Helicoverpa armigera brush border membrane vesicles results in pore formation.
abstract: 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.
authors.affiliation: Beijing Key Laboratory of New Technology in Agricultural Application, Beijing University of Agriculture, Beijing 102206, China.
authors.forename: Jing-Guo
authors.initials: JG
authors.lastname: Liu
authors.forename: Ai-Zhen
authors.initials: AZ
authors.lastname: Yang
authors.forename: Xiao-Hong
authors.initials: XH
authors.lastname: Shen
authors.forename: Bao-Guang
authors.initials: BG
authors.lastname: Hua
authors.forename: Guang-Lu
authors.initials: GL
authors.lastname: Shi
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D041981:Gastrointestinal Tract / Q000378:metabolism; D054884:Host-Pathogen Interactions; D007300:Insect Control / Q000379:methods*; D007305:Insecticide Resistance; D007473:Ion Channels / Q000187:drug effects; D007915:Lepidoptera / Q000382:microbiology; D008871:Microvilli / Q000378:metabolism; D010572:Pest Control, Biological / Q000379:methods*; D011485:Protein Binding; D022161:Transport Vesicles / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D007473:Ion Channels; C447139:Vip3A protein, Bacillus thuringiensis