Brush border membrane binding properties of Bacillus thuringiensis Vip3A toxin to Heliothis virescens and Helicoverpa zea midguts.
The binding properties of Vip3A, a new family of Bacillus thuringiensis insecticidal toxins, have been examined in the major cotton pests, Heliothis virescens and Helicoverpa zea. Vip3A bound specifically to brush border membrane vesicles (BBMV) prepared from both insect larval midguts. In order to examine the cross-resistance potential of Vip3A to the commercially available Cry1Ac and Cry2Ab2 toxins, the membrane binding site relationship among these toxins was investigated. Competition binding assays demonstrated that Vip3A does not inhibit the binding of either Cry1Ac or Cry2Ab2 and vice versa. BBMV protein blotting experiments showed that Vip3A does not bind to the known Cry1Ac receptors. These distinct binding properties and the unique protein sequence of Vip3A support its use as a novel insecticidal agent. This study indicates a very low cross-resistance potential between Vip3A and currently deployed Cry toxins and hence supports its use in an effective resistance management strategy in cotton.
Lee
Mi Kyong
MK
Syngenta Biotechnology, Inc., 3054 Cornwallis Road, Research Triangle Park, NC 27709, USA. mikyong.lee@syngenta.com
Miles
Paul
P
Chen
Jeng-Shong
JS
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism*; D001665:Binding Sites; D002478:Cells, Cultured; D019476:Insect Proteins / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000378:metabolism*; D007915:Lepidoptera / Q000378:metabolism*; D008871:Microvilli / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism*
D001426:Bacterial Proteins; D001427:Bacterial Toxins; C095416:Cry toxin receptors; D019476:Insect Proteins; D011956:Receptors, Cell Surface; C447139:Vip3A protein, Bacillus thuringiensis